Current Diabetes Reviews

Current Diabetes Reviews

Editor-in-Chief

ISSN (Print): 1573-3998
ISSN (Online): 1875-6417

Back Subscribe
Review Article

Circulating Biomarkers as a Window into the Relationship between Sarcopenia and Diabetes: Implications for Effective Management

Author(s): Ali Tajikorcid of author, Vahid Mahdavizadeh, Farzin Hadizadeh and Neda Shakour*

Volume 22, Issue 4, 2026

Published on: 13 February, 2025

Article ID: e15733998349193

Pages: 31

DOI: 10.2174/0115733998349193250207045239

open_access

Become a Editorial Board Member
Become a Reviewer
Become a Editor
Become a Section Editor

Abstract

Introduction/Aims: This study aims to investigate the relationship between sarcopenia and circulating biomarkers in diabetes, with a focus on early detection and effective management strategies.

Methods: A literature review was conducted using the ScienceDirect, Scopus, PubMed, and Web of Science databases up to December 2024. Key search terms included “diabetes,” “sarcopenia,” “HbA1c”, “glucose,” “insulin,” and specific biomarkers such as inflammatory markers, adipokines, and myokines.

Results and Discussion: Aging is associated with a decline in organ and bodily system functionality, with sarcopenia being particularly prominent due to its progressive loss of muscle mass and function. This condition increases health risks and mortality in the elderly. Muscles, as the primary consumers of glucose, play a crucial role in glucose uptake; reduced mass can exacerbate insulin resistance. Sarcopenia and diabetes share common pathophysiological mechanisms, including insulin resistance, inflammation, and vascular complications. Circulating biomarkers, crucial for diabetes management, may offer insights into the early stages of sarcopenia.

Conclusion: The complex relationship between sarcopenia and diabetes, influenced by shared pathophysiological pathways, presents challenges in geriatric healthcare. Circulating biomarkers hold promise for early detection and monitoring of sarcopenia, potentially enhancing patient outcomes and quality of life. Further research is necessary to validate these connections and develop targeted treatments for individuals affected by these conditions.

Keywords: Aging, sarcopenia, glucose uptake, diabetes, circulating biomarkers, HbA1c, insulin.

[1]
Cruz-Jentoft AJ, Sayer AA. Sarcopenia. Lancet 2019; 393(10191): 2636-46.
[http://dx.doi.org/10.1016/S0140-6736(19)31138-9] [PMID: 31171417]
[2]
Cruz-Jentoft AJ, Landi F, Schneider SM, et al. Prevalence of and interventions for sarcopenia in ageing adults: A systematic review. Report of the International Sarcopenia Initiative (EWGSOP and IWGS). Age Ageing 2014; 43(6): 748-59.
[http://dx.doi.org/10.1093/ageing/afu115] [PMID: 25241753]
[3]
Shachar SS, Williams GR, Muss HB, Nishijima TF. Prognostic value of sarcopenia in adults with solid tumours: A meta-analysis and systematic review. Eur J Cancer 2016; 57: 58-67.
[http://dx.doi.org/10.1016/j.ejca.2015.12.030]
[4]
Shu X, Lin T, Wang H, et al. Diagnosis, prevalence, and mortality of sarcopenia in dialysis patients: A systematic review and meta-analysis. J Cachexia Sarcopenia Muscle 2022; 13(1): 145-58.
[http://dx.doi.org/10.1002/jcsm.12890] [PMID: 34989172]
[5]
Tantai X, Liu Y, Yeo YH, et al. Effect of sarcopenia on survival in patients with cirrhosis: A meta-analysis. J Hepatol 2022; 76(3): 588-99.
[http://dx.doi.org/10.1016/j.jhep.2021.11.006] [PMID: 34785325]
[6]
Feng L, Gao Q, Hu K, et al. Prevalence and risk factors of sarcopenia in patients with diabetes: A meta-analysis. J Clin Endocrinol Metab 2022; 107(5): 1470-83.
[http://dx.doi.org/10.1210/clinem/dgab884] [PMID: 34904651]
[7]
Mukund K, Subramaniam S. Skeletal muscle: A review of molecular structure and function, in health and disease. Wiley Interdiscip Rev Syst Biol Med 2020; 12(1): e1462.
[http://dx.doi.org/10.1002/wsbm.1462] [PMID: 31407867]
[8]
Oberbach A, Bossenz Y, Lehmann S, et al. Antioxidant effects of a novel pioglitazone analogue (PA9) in a rat model of diabetes: Modulation of redox homeostasis and preservation of tissue architecture. J Diabetes Complications 2024; 38(12): 108897.
[http://dx.doi.org/10.1016/j.jdiacomp.2024.108897] [PMID: 39489911]
[9]
Nishikawa H, Fukunishi S, Asai A, et al. Sarcopenia, frailty and type 2 diabetes mellitus (Review). Mol Med Rep 2021; 24(6): 854.
[http://dx.doi.org/10.3892/mmr.2021.12494] [PMID: 34651658]
[10]
Shakour N, Hoseinpoor S, Sepehri S, Iranshahi M, Badpeyma M. Novel hits for targeting kidney failure in type 2 diabetes derived via in silico screening of the ZINC natural product database. J Comput Sci 2024; 85: 102497.
[http://dx.doi.org/10.1016/j.jocs.2024.102497]
[11]
Nosrati M, Shakour N, Sahranavard T, et al. Association between diabetes mellitus and rs2868371: A polymorphism of HSPB1. 2022; 9(1)
[12]
Oberbach A, Bossenz Y, Lehmann S, et al. Altered fiber distribution and fiber-specific glycolytic and oxidative enzyme activity in skeletal muscle of patients with type 2 diabetes. Diabetes Care 2006; 29(4): 895-900.
[http://dx.doi.org/10.2337/diacare.29.04.06.dc05-1854] [PMID: 16567834]
[13]
Nishikawa H, Asai A, Fukunishi S, Nishiguchi S, Higuchi K. Metabolic syndrome and sarcopenia. Nutrients 2021; 13(10): 3519.
[http://dx.doi.org/10.3390/nu13103519] [PMID: 34684520]
[14]
Severinsen MCK, Pedersen BK. Muscle–Organ crosstalk: The emerging roles of myokines. Endocr Rev 2020; 41(4): 594-609.
[http://dx.doi.org/10.1210/endrev/bnaa016] [PMID: 32393961]
[15]
Seo JA, Kang MC, Yang WM, et al. Apolipoprotein J is a hepatokine regulating muscle glucose metabolism and insulin sensitivity. Nat Commun 2020; 11(1): 2024.
[http://dx.doi.org/10.1038/s41467-020-15963-w] [PMID: 32332780]
[16]
Ciaraldi TP, Abrams L, Nikoulina S, Mudaliar S, Henry RR. Glucose transport in cultured human skeletal muscle cells. Regulation by insulin and glucose in nondiabetic and non-insulin-dependent diabetes mellitus subjects. J Clin Invest 1995; 96(6): 2820-7.
[http://dx.doi.org/10.1172/JCI118352] [PMID: 8675652]
[17]
Wolfe RR, Allsop JR, Burke JF. Glucose metabolism in man: Responses to intravenous glucose infusion. Metabolism 1979; 28(3): 210-20.
[http://dx.doi.org/10.1016/0026-0495(79)90066-0] [PMID: 763155]
[18]
Al-Mhanna SB, Rocha-Rodriguesc S, Mohamed M, et al. Effects of combined aerobic exercise and diet on cardiometabolic health in patients with obesity and type 2 diabetes: A systematic review and meta-analysis. BMC Sports Sci Med Rehabil 2023; 15(1): 165.
[http://dx.doi.org/10.1186/s13102-023-00766-5] [PMID: 38049873]
[19]
Piotrowska K, Zgutka K, Tkacz M, Tarnowski M. Physical activity as a modern intervention in the fight against obesity-related inflammation in type 2 diabetes mellitus and gestational diabetes. Antioxidants 2023; 12(8): 1488.
[http://dx.doi.org/10.3390/antiox12081488] [PMID: 37627482]
[20]
Rodbard HW, Barnard-Kelly K, Pfeiffer AFH, Mauersberger C, Schnell O, Giorgino F. Practical strategies to manage obesity in type 2 diabetes. Diabetes Obes Metab 2024; 26(6): 2029-45.
[http://dx.doi.org/10.1111/dom.15556] [PMID: 38514387]
[21]
Pratt-Phillips S. Effect of exercise conditioning on countering the effects of obesity and insulin resistance in horses: A review. Animals 2024; 14(5): 727.
[http://dx.doi.org/10.3390/ani14050727] [PMID: 38473112]
[22]
Sgrò P, Emerenziani GP, Antinozzi C, Sacchetti M, Di Luigi L. Exercise as a drug for glucose management and prevention in type 2 diabetes mellitus. Curr Opin Pharmacol 2021; 59: 95-102.
[http://dx.doi.org/10.1016/j.coph.2021.05.006] [PMID: 34182427]
[23]
Shakour N, Hoseinpoor S, Rajabian F, et al. Discovery of non-peptide GLP-1r natural agonists for enhancing coronary safety in type 2 diabetes patients. J Biomol Struct Dyn 2024; 1-18.
[http://dx.doi.org/10.1080/07391102.2023.2298734] [PMID: 38165453]
[24]
Škrha J, Šoupal J, Škrha J Jr, Prázný M. Glucose variability, HbA1c and microvascular complications. Rev Endocr Metab Disord 2016; 17(1): 103-10.
[http://dx.doi.org/10.1007/s11154-016-9347-2] [PMID: 26975588]
[25]
Huang S, Xiang C, Song Y. Identification of the shared gene signatures and pathways between sarcopenia and type 2 diabetes mellitus. PLoS One 2022; 17(3): e0265221.
[http://dx.doi.org/10.1371/journal.pone.0265221] [PMID: 35271662]
[26]
Lin Y, Zhang Y, Shen X, Huang L, Yan S. Influence of glucose, insulin fluctuation, and glycosylated hemoglobin on the outcome of sarcopenia in patients with type 2 diabetes mellitus. J Diabetes Complications 2021; 35(6): 107926.
[http://dx.doi.org/10.1016/j.jdiacomp.2021.107926] [PMID: 33865681]
[27]
Mori H, Kuroda A, Ishizu M, et al. Association of accumulated advanced glycation end-products with a high prevalence of sarcopenia and dynapenia in patients with type 2 diabetes. J Diabetes Investig 2019; 10(5): 1332-40.
[http://dx.doi.org/10.1111/jdi.13014] [PMID: 30677242]
[28]
Haus JM, Carrithers JA, Trappe SW, Trappe TA. Collagen, cross-linking, and advanced glycation end products in aging human skeletal muscle. J Appl Physiol 2007; 103(6): 2068-76.
[http://dx.doi.org/10.1152/japplphysiol.00670.2007] [PMID: 17901242]
[29]
He N, Zhang Y, Zhang L, Zhang S, Ye H. Relationship between sarcopenia and cardiovascular diseases in the elderly: An overview. Front Cardiovasc Med 2021; 8: 743710.
[http://dx.doi.org/10.3389/fcvm.2021.743710] [PMID: 34957238]
[30]
Damluji AA, Alfaraidhy M, AlHajri N, et al. Sarcopenia and cardiovascular diseases. Circulation 2023; 147(20): 1534-53.
[http://dx.doi.org/10.1161/CIRCULATIONAHA.123.064071] [PMID: 37186680]
[31]
Mesinovic J, Zengin A, De Courten B, Ebeling PR, Scott D. Sarcopenia and type 2 diabetes mellitus: A bidirectional relationship. Diabetes Metab Syndr Obes 2019; 12: 1057-72.
[http://dx.doi.org/10.2147/DMSO.S186600] [PMID: 31372016]
[32]
Ortiz-Martínez M, González-González M, Martagón AJ, Hlavinka V, Willson RC, Rito-Palomares M. Recent developments in biomarkers for diagnosis and screening of type 2 diabetes mellitus. Curr Diab Rep 2022; 22(3): 95-115.
[http://dx.doi.org/10.1007/s11892-022-01453-4] [PMID: 35267140]
[33]
Wolkowicz KL, Aiello EM, Vargas E, et al. A review of biomarkers in the context of type 1 diabetes: Biological sensing for enhanced glucose control. Bioeng Transl Med 2021; 6(2): e10201.
[http://dx.doi.org/10.1002/btm2.10201] [PMID: 34027090]
[34]
Rentflejsz J, Wojszel ZB. Diabetes Mellitus should be considered while analysing sarcopenia-related biomarkers. J Clin Med 2024; 13(4): 1107.
[http://dx.doi.org/10.3390/jcm13041107] [PMID: 38398421]
[35]
Lisco G, Disoteo OE, De Tullio A, et al. Sarcopenia and diabetes: A detrimental liaison of advancing age. Nutrients 2023; 16(1): 63.
[http://dx.doi.org/10.3390/nu16010063] [PMID: 38201893]
[36]
Curcio F, Ferro G, Basile C, et al. Biomarkers in sarcopenia: A multifactorial approach. Exp gerontology 2016; 85: 1-8.
[PMID: 27633530]
[37]
Gerich JE. Physiology of glucose homeostasis. Diabetes Obes Metab 2000; 2(6): 345-50.
[http://dx.doi.org/10.1046/j.1463-1326.2000.00085.x] [PMID: 11225963]
[38]
Loscalzo J, Fauci AS, Kasper DL, Hauser SL, Longo DL, Jameson JL. Harrison’s principles of internal medicine. MC Graw Hill 2022.
[39]
Carstensen B, Lindström J, Sundvall J, Borch-Johnsen K, Tuomilehto J. Measurement of blood glucose: Comparison between different types of specimens. Ann Clin Biochem 2008; 45(2): 140-8.
[http://dx.doi.org/10.1258/acb.2007.006212] [PMID: 18325176]
[40]
Heikkinen S, Argmann CA, Champy MF, Auwerx J. Evaluation of glucose homeostasis. Curr Protoc Mol Biol 2007; 77(1)
[http://dx.doi.org/10.1002/0471142727.mb29b03s77]
[41]
Ighodaro OM. Molecular pathways associated with oxidative stress in diabetes mellitus. Biomed Pharmacother 2018; 108: 656-62.
[http://dx.doi.org/10.1016/j.biopha.2018.09.058] [PMID: 30245465]
[42]
Haraguchi M, Miyaaki H, Ichikawa T, et al. Glucose fluctuations reduce quality of sleep and of life in patients with liver cirrhosis. Hepatol Int 2017; 11(1): 125-31.
[http://dx.doi.org/10.1007/s12072-016-9762-1] [PMID: 27624504]
[43]
Yang W, Liu M, Tian Y, et al. The increased prevalence of depression and anxiety in T2DM patients associated with blood glucose fluctuation and sleep quality. BMC Endocr Disord 2022; 22(1): 232.
[http://dx.doi.org/10.1186/s12902-022-01147-8] [PMID: 36114534]
[44]
Wang H, Deng J, Chen L, Ding K, Wang Y. Acute glucose fluctuation induces inflammation and neurons apoptosis in hippocampal tissues of diabetic rats. J Cell Biochem 2021; 122(9): 1239-47.
[http://dx.doi.org/10.1002/jcb.29523] [PMID: 31713299]
[45]
Fujiwara T, Takeda N. Glucose fluctuation and cardiovascular diseases. Int Heart J 2020; 61(4): 633-5.
[http://dx.doi.org/10.1536/ihj.20-417] [PMID: 32727998]
[46]
Ogama N, Sakurai T, Kawashima S, et al. Association of glucose fluctuations with sarcopenia in older adults with type 2 diabetes mellitus. J Clin Med 2019; 8(3): 319.
[http://dx.doi.org/10.3390/jcm8030319] [PMID: 30845785]
[47]
Balamurugan Jr M, Sarumathy Sr S, Robinson Jr R, Balamurugan M, Robinson R. Lobeglitazone and its therapeutic benefits: A review. Cureus 2023; 15(12): e50085.
[http://dx.doi.org/10.7759/cureus.50085] [PMID: 38186506]
[48]
Shi X, Liu W, Zhang L, et al. Sex-Specific associations between low muscle mass and glucose fluctuations in patients with type 2 diabetes mellitus. Front Endocrinol (Lausanne) 2022; 13: 913207.
[http://dx.doi.org/10.3389/fendo.2022.913207] [PMID: 35909561]
[49]
Massimino E, Izzo A, Riccardi G, Della Pepa G. The impact of glucose-lowering drugs on sarcopenia in type 2 diabetes: current evidence and underlying mechanisms. Cells 2021; 10(8): 1958.
[http://dx.doi.org/10.3390/cells10081958] [PMID: 34440727]
[50]
Massimino E, Izzo A, Riccardi G, Della Pepa G. Pharmacologic approaches to glycemic treatment. Standards of Medical Care in Diabetes 2021; 44 (Suppl. 1): S111-24.
[http://dx.doi.org/10.2337/dc21-S009]
[51]
Mosenzon O, Del Prato S, Schechter M, et al. From glucose lowering agents to disease/diabetes modifying drugs: A “SIMPLE” approach for the treatment of type 2 diabetes. Cardiovasc Diabetol 2021; 20(1): 92.
[http://dx.doi.org/10.1186/s12933-021-01281-y] [PMID: 33910583]
[52]
Shakour N, Karami S, Iranshahi M, et al. Antifibrotic effects of sodium-glucose cotransporter-2 inhibitors: A comprehensive review. Diabetes Metab Syndr 2023; 18(1): 102934.
[http://dx.doi.org/10.1016/j.dsx.2023.102934.]
[53]
Rahbar S, Blumenfeld O, Ranney HM. Studies of an unusual hemoglobin in patients with diabetes mellitus. Biochem Biophys Res Commun 1969; 36(5): 838-43.
[http://dx.doi.org/10.1016/0006-291X(69)90685-8] [PMID: 5808299]
[54]
Saudek CD, Brick JC. The clinical use of hemoglobin A1c. J Diabetes Sci Technol 2009; 3(4): 629-34.
[http://dx.doi.org/10.1177/193229680900300402] [PMID: 20144304]
[55]
Eyth E, Naik R. Hemoglobin A1c. Treasure Island, FL: StatPearls Publishing LLC 2019.
[56]
Gupta S, Jain U, Chauhan N. Laboratory diagnosis of HbA1c: A review. J Nanomed Res 2017; 5(4): 00120.
[57]
Heinemann L, Freckmann G. Quality of HbA1c measurement in the practice: The German perspective. J Diabetes Sci Technol 2015; 9(3): 687-95.
[http://dx.doi.org/10.1177/1932296815572254] [PMID: 25691655]
[58]
Pilla R, Palleti SK, Rayala R, Skss SR, Abdul Razzack A, Kalla S. Glycated haemoglobin (HbA1c) variations in nondiabetics with nutritional anemia. Cureus 2020; 12(11): e11479.
[http://dx.doi.org/10.7759/cureus.11479] [PMID: 33329975]
[59]
Lacy ME, Wellenius GA, Sumner AE, et al. Association of sickle cell trait with hemoglobin A1c in African Americans. JAMA 2017; 317(5): 507-15.
[http://dx.doi.org/10.1001/jama.2016.21035] [PMID: 28170479]
[60]
Radin MS. Pitfalls in hemoglobin A1c measurement: When results may be misleading. J Gen Intern Med 2014; 29(2): 388-94.
[http://dx.doi.org/10.1007/s11606-013-2595-x] [PMID: 24002631]
[61]
Guo W, Zhou Q, Jia Y, Xu J. Increased levels of glycated hemoglobin A1c and iron deficiency anemia: A review. Med Sci Monit 2019; 25: 8371-8.
[http://dx.doi.org/10.12659/MSM.916719] [PMID: 31696865]
[62]
Gram-Hansen P, Eriksen J, Mourits-Andersen T, Olesen L. Glycosylated haemoglobin (HbA1c) in iron- and vitamin B12 deficiency. J Intern Med 1990; 227(2): 133-6.
[http://dx.doi.org/10.1111/j.1365-2796.1990.tb00131.x] [PMID: 2299304]
[63]
Shepard JG, Airee A, Dake AW, McFarland MS, Vora A. Limitations of A1c interpretation. South Med J 2015; 108(12): 724-9.
[http://dx.doi.org/10.14423/SMJ.0000000000000381] [PMID: 26630892]
[64]
Kaji A, Hashimoto Y, Kobayashi Y, et al. Sarcopenia is associated with tongue pressure in older patients with type 2 diabetes: A cross-sectional study of the KAMOGAWA-DM cohort study. Geriatr Gerontol Int 2019; 19(2): 153-8.
[http://dx.doi.org/10.1111/ggi.13577] [PMID: 30585390]
[65]
Sazlina S-G, Lee PY, Chan YM, A Hamid MS, Tan NC. The prevalence and factors associated with sarcopenia among community living elderly with type 2 diabetes mellitus in primary care clinics in Malaysia. PLoS One 2020; 15(5): e0233299.
[http://dx.doi.org/10.1371/journal.pone.0233299] [PMID: 32433712]
[66]
Kalyani RR, Metter EJ, Egan J, Golden SH, Ferrucci L. Hyperglycemia predicts persistently lower muscle strength with aging. Diabetes Care 2015; 38(1): 82-90.
[http://dx.doi.org/10.2337/dc14-1166] [PMID: 25392294]
[67]
Sugimoto K, Tabara Y, Ikegami H, et al. Hyperglycemia in non-obese patients with type 2 diabetes is associated with low muscle mass: The multicenter study for clarifying evidence for sarcopenia in patients with diabetes mellitus. J Diabetes Investig 2019; 10(6): 1471-9.
[http://dx.doi.org/10.1111/jdi.13070] [PMID: 31074209]
[68]
Yoon JW, Ha YC, Kim KM, et al. Hyperglycemia is associated with impaired muscle quality in older men with diabetes: The Korean longitudinal study on health and aging. Diabetes Metab J 2016; 40(2): 140-6.
[http://dx.doi.org/10.4093/dmj.2016.40.2.140] [PMID: 27126884]
[69]
Pechmann LM, Jonasson TH, Canossa VS, et al. Sarcopenia in type 2 diabetes mellitus: A cross-sectional observational study. Int J Endocrinol 2020; 2020: 1-9.
[http://dx.doi.org/10.1155/2020/7841390] [PMID: 33178269]
[70]
Mori H, Kuroda A, Araki M, et al. Advanced glycation end-products are a risk for muscle weakness in Japanese patients with type 1 diabetes. J Diabetes Investig 2017; 8(3): 377-82.
[http://dx.doi.org/10.1111/jdi.12582] [PMID: 27727515]
[71]
Öztürk ZA, Türkbeyler İH, Demir Z, Bilici M, Kepekçi Y. The effect of blood glucose regulation on sarcopenia parameters in obese and diabetic patients. Turk J Phys Med Rehabil 2017; 64(1): 72-9.
[http://dx.doi.org/10.5606/tftrd.2018.1068] [PMID: 31453492]
[72]
Ferrari U, Then C, Rottenkolber M, et al. Longitudinal association of type 2 diabetes and insulin therapy with muscle parameters in the KORA-Age study. Acta Diabetol 2020; 57(9): 1057-63.
[http://dx.doi.org/10.1007/s00592-020-01523-7] [PMID: 32246270]
[73]
Sung MJ, Lim TS, Jeon MY, et al. Sarcopenia is independently associated with the degree of liver fibrosis in patients with type 2 diabetes mellitus. Gut Liver 2020; 14(5): 626-35.
[http://dx.doi.org/10.5009/gnl19126] [PMID: 32135582]
[74]
Ida S, Kaneko R, Nagata H, et al. Association between sarcopenia and sleep disorder in older patients with diabetes. Geriatr Gerontol Int 2019; 19(5): 399-403.
[http://dx.doi.org/10.1111/ggi.13627] [PMID: 30773802]
[75]
Hashimoto Y, Kaji A, Sakai R, et al. Sarcopenia is associated with blood pressure variability in older patients with type 2 diabetes: A cross-sectional study of the KAMOGAWA-DM cohort study. Geriatr Gerontol Int 2018; 18(9): 1345-9.
[http://dx.doi.org/10.1111/ggi.13487] [PMID: 30039599]
[76]
Okamura T, Miki A, Hashimoto Y, et al. 2019; Okamura T, Miki A, Hashimoto Y, et al. Shortage of energy intake rather than protein intake is associated with sarcopenia in elderly patients with type 2 diabetes: A cross-sectional study of the KAMOGAWA-DM cohort. J Diabetes 2019; 11(6): 477-83.
[http://dx.doi.org/10.1111/1753-0407.12874] [PMID: 30407749]
[77]
Okamura T, Hashimoto Y, Miki A, et al. High brain natriuretic peptide is associated with sarcopenia in patients with type 2 diabetes: A cross-sectional study of KAMOGAWA-DM cohort study. Endocr J 2019; 66(4): 369-77.
[http://dx.doi.org/10.1507/endocrj.EJ19-0024] [PMID: 31019148]
[78]
Cui M, Gang X, Wang G, et al. A cross-sectional study. Medicine (Baltimore) 2020; 99(2): e18708.
[http://dx.doi.org/10.1097/MD.0000000000018708] [PMID: 31914078]
[79]
Ida S, Murata K, Nakadachi D, et al. Association between dynapenia and decline in higher-level functional capacity in older men with diabetes. Geriatr Gerontol Int 2018; 18(9): 1393-7.
[http://dx.doi.org/10.1111/ggi.13498] [PMID: 30094914]
[80]
Murai J, Nishizawa H, Otsuka A, et al. Low muscle quality in Japanese type 2 diabetic patients with visceral fat accumulation. Cardiovasc Diabetol 2018; 17(1): 112.
[http://dx.doi.org/10.1186/s12933-018-0755-3] [PMID: 30077183]
[81]
Osaka T, Hamaguchi M, Hashimoto Y, et al. Decreased the creatinine to cystatin C ratio is a surrogate marker of sarcopenia in patients with type 2 diabetes. Diabetes Res Clin Pract 2018; 139: 52-8.
[http://dx.doi.org/10.1016/j.diabres.2018.02.025] [PMID: 29496508]
[82]
Fukuda T, Bouchi R, Takeuchi T, et al. Sarcopenic obesity assessed using dual energy X-ray absorptiometry (DXA) can predict cardiovascular disease in patients with type 2 diabetes: A retrospective observational study. Cardiovasc Diabetol 2018; 17(1): 55.
[http://dx.doi.org/10.1186/s12933-018-0700-5] [PMID: 29636045]
[83]
de Freitas MM, de Oliveira VLP, Grassi T, et al. Difference in sarcopenia prevalence and associated factors according to 2010 and 2018 European consensus (EWGSOP) in elderly patients with type 2 diabetes mellitus. Exp Gerontol 2020; 132: 110835.
[http://dx.doi.org/10.1016/j.exger.2020.110835] [PMID: 31954325]
[84]
Ida S, Nakai M, Ito S. Association between sarcopenia and mild cognitive impairment using the Japanese version of the SARC-F in elderly patients with diabetes J Am Med Dir Assoc 2016; 18(9): 809.
[http://dx.doi.org/10.1016/j.jamda.2017.06.012] [PMID: 28739493]
[85]
Liccini AP, Malmstrom TK. Frailty and sarcopenia as predictors of adverse health outcomes in persons with diabetes mellitus. J Am Med Dir Assoc 2016; 17(9): 846-51.
[http://dx.doi.org/10.1016/j.jamda.2016.07.007] [PMID: 27569712]
[86]
Murata Y, Kadoya Y, Yamada S, Sanke T. Sarcopenia in elderly patients with type 2 diabetes mellitus: prevalence and related clinical factors. Diabetol Int 2018; 9(2): 136-42.
[http://dx.doi.org/10.1007/s13340-017-0339-6] [PMID: 30603361]
[87]
Chien YH, Tsai CJ, Wang DC, Chuang PH, Lin HT. Effects of 12-week progressive sandbag exercise training on glycemic control and muscle strength in patients with type 2 diabetes mellitus combined with possible sarcopenia. Int J Environ Res Public Health 2022; 19(22): 15009.
[http://dx.doi.org/10.3390/ijerph192215009] [PMID: 36429728]
[88]
Alfaro-Alvarado FA, Rosas-Barrientos JV, Ocharan-Hernández ME, Díaz-Chiguer D, Vargas-De-León C. Association between sarcopenia and poor glycemic control in older adults with type 2 diabetes mellitus. Diseases 2023; 11(4): 175.
[http://dx.doi.org/10.3390/diseases11040175] [PMID: 38131980]
[89]
Pechmann LM, Jonasson TH, Canossa VS, et al. Sarcopenia in type 2 diabetes mellitus: A cross-sectional observational study. Int J Endocrinol 2020; 2020(1): 1-9.
[http://dx.doi.org/10.1155/2020/7841390] [PMID: 33178269]
[90]
Ma G-C, Zou L-L, Dai W, Wang Z-Z, Cao YH. The association between glucose fluctuation with sarcopenia in elderly patients with type 2 diabetes mellitus. European Rev Med pharmacol Sci 2023; 27(5): 1912-20.
[PMID: 36930518]
[91]
Hou L, Liu Y, Li X, et al. Changes and risk factors of skeletal muscle mass and strength in patients with type 2 diabetes over 60 years old: A Cross-sectional study from China. J Diabetes Res 2020; 2020(1): 1-7.
[http://dx.doi.org/10.1155/2020/9815485] [PMID: 33381601]
[92]
Li C, Yu K, Shyh-Chang N, et al. Circulating factors associated with sarcopenia during ageing and after intensive lifestyle intervention. J Eachexia Sarcopenia Muscle 2019; 10(3): 586-600.
[http://dx.doi.org/10.1002/jcsm.12417] [PMID: 30969486]
[93]
Fukuoka Y, Narita T, Fujita H, et al. Importance of physical evaluation using skeletal muscle mass index and body fat percentage to prevent sarcopenia in elderly Japanese diabetes patients. J Diabetes Investig 2019; 10(2): 322-30.
[http://dx.doi.org/10.1111/jdi.12908] [PMID: 30098231]
[94]
Bouchi R, Fukuda T, Takeuchi T, et al. Insulin treatment attenuates decline of muscle mass in Japanese patients with type 2 diabetes. Calcif Tissue Int 2017; 101(1): 1-8.
[http://dx.doi.org/10.1007/s00223-017-0251-x] [PMID: 28246927]
[95]
Lu Y, Lim WS, Jin X, et al. Lower insulin level is associated with sarcopenia in community-dwelling frail and non-frail older adults. Front Med (Lausanne) 2022; 9: 971622.
[http://dx.doi.org/10.3389/fmed.2022.971622] [PMID: 36482911]
[96]
Kosaki K, Kamijo-Ikemori A, Sugaya T, et al. Relationship between exercise capacity and urinary liver-type fatty acid-binding protein in middle-aged and older individuals. Clin Exp Nephrol 2017; 21(5): 810-7.
[http://dx.doi.org/10.1007/s10157-017-1385-x] [PMID: 28197733]
[97]
Can B, Kara O, Kizilarslanoglu MC, et al. Serum markers of inflammation and oxidative stress in sarcopenia. Aging Clin Exp Res 2017; 29(4): 745-52.
[http://dx.doi.org/10.1007/s40520-016-0626-2] [PMID: 27571781]
[98]
Chen MJ, Leng J, Ni JP, Xiong AL, Hu MY. U-shaped association between plasma C-peptide and sarcopenia: A cross-sectional study of elderly Chinese patients with diabetes mellitus. PLoS One 2023; 18(10): e0292654.
[http://dx.doi.org/10.1371/journal.pone.0292654] [PMID: 37862294]
[99]
Wallach JB. Interpretation of diagnostic tests. Lippincott Williams & Wilkins 2007.
[100]
Kamijo-Ikemori A, Sugaya T, Yasuda T, et al. Clinical significance of urinary liver-type fatty acid-binding protein in diabetic nephropathy of type 2 diabetic patients. Diabetes Care 2011; 34(3): 691-6.
[http://dx.doi.org/10.2337/dc10-1392] [PMID: 21273494]
[101]
Damas P, Reuter A, Gysen P, Demonty J, Lamy M, Franchimont P. Tumor necrosis factor and interleukin-1 serum levels during severe sepsis in humans. Crit Care Med 1989; 17(10): 975-8.
[http://dx.doi.org/10.1097/00003246-198910000-00001] [PMID: 2791581]
[102]
Song M, Kellum JA. Interleukin-6. Crit Care Med 2005; 33(12) (Suppl.): S463-5.
[http://dx.doi.org/10.1097/01.CCM.0000186784.62662.A1] [PMID: 16340422]
[103]
Wilcox G. Insulin and insulin resistance. Clin Biochem Rev 2005; 26(2): 19-39.
[PMID: 16278749]
[104]
Shen Y, Prinyawiwatkul W, Xu Z. Insulin: A review of analytical methods. Analyst (Lond) 2019; 144(14): 4139-48.
[http://dx.doi.org/10.1039/C9AN00112C] [PMID: 31143899]
[105]
Pørksen N, Hollingdal M, Juhl C, Butler P, Veldhuis JD, Schmitz O. Pulsatile insulin secretion: detection, regulation, and role in diabetes. Diabetes 2002; 51 (Suppl. 1): S245-54.
[http://dx.doi.org/10.2337/diabetes.51.2007.S245] [PMID: 11815487]
[106]
Bratanova-Tochkova TK, Cheng H, Daniel S, et al. Triggering and augmentation mechanisms, granule pools, and biphasic insulin secretion. Diabetes 2002; 51(6): S83-90.
[http://dx.doi.org/10.2337/diabetes.51.2007.S83] [PMID: 11815463]
[107]
Kahn CR. The molecular mechanism of insulin action. Annu Rev Med 1985; 36(1): 429-51.
[http://dx.doi.org/10.1146/annurev.me.36.020185.002241] [PMID: 2986528]
[108]
Petersen MC, Shulman GI. Mechanisms of insulin action and insulin resistance. Physiol Rev 2018; 98(4): 2133-223.
[http://dx.doi.org/10.1152/physrev.00063.2017] [PMID: 30067154]
[109]
Kahn CR, Baird KL, Flier JS, et al. Academic Press 1981; pp. Insulin receptors, receptor antibodies, and the mechanism of insulin action. Recent Progress in Hormone Research, Proceedings of the 1980 Laurentian Hormone Conference. 477-538.
[110]
Epstein FH, Moller DE, Flier JS. Insulin resistance--mechanisms, syndromes, and implications. N Engl J Med 1991; 325(13): 938-48.
[http://dx.doi.org/10.1056/NEJM199109263251307] [PMID: 1881419]
[111]
Liu Z, Zhu C. Causal relationship between insulin resistance and sarcopenia. Diabetol Metab Syndr 2023; 15(1): 46.
[http://dx.doi.org/10.1186/s13098-023-01022-z] [PMID: 36918975]
[112]
Stangl MK, Böcker W, Chubanov V, et al. Sarcopenia–endocrinological and neurological aspects. Exp Clin Endocrinol Diabetes 2019; 127(1): 8-22.
[PMID: 30199918]
[113]
Schiaffino S, Dyar KA, Ciciliot S, Blaauw B, Sandri M. Mechanisms regulating skeletal muscle growth and atrophy. FEBS J 2013; 280(17): 4294-314.
[http://dx.doi.org/10.1111/febs.12253] [PMID: 23517348]
[114]
Pereira S, Marliss EB, Morais JA, Chevalier S, Gougeon R. Insulin resistance of protein metabolism in type 2 diabetes. Diabetes 2008; 57(1): 56-63.
[http://dx.doi.org/10.2337/db07-0887] [PMID: 17940118]
[115]
Das AK, Yang QY, Fu X, et al. AMP-activated protein kinase stimulates myostatin expression in C2C12 cells. Biochem Biophys Res Commun 2012; 427(1): 36-40.
[http://dx.doi.org/10.1016/j.bbrc.2012.08.138] [PMID: 22995402]
[116]
Hong S, Choi KM. Sarcopenic obesity, insulin resistance, and their implications in cardiovascular and metabolic consequences. Int J Mol Sci 2020; 21(2): 494.
[http://dx.doi.org/10.3390/ijms21020494] [PMID: 31941015]
[117]
Zhu S, Tian Z, Torigoe D, et al. Aging- and obesity-related peri-muscular adipose tissue accelerates muscle atrophy. PLoS One 2019; 14(8): e0221366.
[http://dx.doi.org/10.1371/journal.pone.0221366] [PMID: 31442231]
[118]
Bosma M. Lipid droplet dynamics in skeletal muscle. Exp Cell Res 2016; 340(2): 180-6.
[http://dx.doi.org/10.1016/j.yexcr.2015.10.023] [PMID: 26515552]
[119]
Chung HS, Choi KM. Adipokines and myokines: A pivotal role in metabolic and cardiovascular disorders. Curr Med Chem 2018; 25(20): 2401-15.
[http://dx.doi.org/10.2174/0929867325666171205144627] [PMID: 29210643]
[120]
Koo BK, Roh E, Yang YS, Moon MK. Difference between old and young adults in contribution of β-cell function and sarcopenia in developing diabetes mellitus. J Diabetes Investig 2016; 7(2): 233-40.
[http://dx.doi.org/10.1111/jdi.12392] [PMID: 27042276]
[121]
Rasmussen BB, Fujita S, Wolfe RR, et al. Insulin resistance of muscle protein metabolism in aging. FASEB J 2006; 20(6): 768-9.
[http://dx.doi.org/10.1096/fj.05-4607fje] [PMID: 16464955]
[122]
Srikanthan P, Hevener AL, Karlamangla AS. Sarcopenia exacerbates obesity-associated insulin resistance and dysglycemia: Findings from the National Health and Nutrition Examination Survey III. PLoS One 2010; 5(5): e10805.
[http://dx.doi.org/10.1371/journal.pone.0010805] [PMID: 22421977]
[123]
Kim TN, Park MS, Lim KI, et al. Relationships between sarcopenic obesity and insulin resistance, inflammation, and vitamin D status: The Korean Sarcopenic obesity study. Clin Endocrinol (Oxf) 2013; 78(4): 525-32.
[http://dx.doi.org/10.1111/j.1365-2265.2012.04433.x] [PMID: 22563924]
[124]
Sugimoto K, Ikegami H, Takata Y, et al. Glycemic control and insulin improve muscle mass and gait speed in type 2 diabetes: The MUSCLES-DM study. J Am Med Dir Assoc 2021; 22(4): 834-838.e1.
[http://dx.doi.org/10.1016/j.jamda.2020.11.003] [PMID: 33278348]
[125]
Wahren J, Ekberg K, Johansson J, et al. Role of C-peptide in human physiology. Am J Physiol Endocrinol Metab 2000; 278(5): E759-68.
[http://dx.doi.org/10.1152/ajpendo.2000.278.5.E759] [PMID: 10780930]
[126]
Jones AG, Hattersley AT. The clinical utility of C-peptide measurement in the care of patients with diabetes. Diabet Med 2013; 30(7): 803-17.
[http://dx.doi.org/10.1111/dme.12159] [PMID: 23413806]
[127]
Little RR, Rohlfing CL, Tennill AL, et al. Standardization of C-peptide measurements. Clin Chem 2008; 54(6): 1023-6.
[http://dx.doi.org/10.1373/clinchem.2007.101287] [PMID: 18420730]
[128]
Leighton E, Sainsbury CAR, Jones GC. A practical review of C-peptide testing in diabetes. Diabetes Ther 2017; 8(3): 475-87.
[http://dx.doi.org/10.1007/s13300-017-0265-4] [PMID: 28484968]
[129]
Rigler R, Pramanik A, Jonasson P, et al. Specific binding of proinsulin C-peptide to human cell membranes. Proc Natl Acad Sci USA 1999; 96(23): 13318-23.
[http://dx.doi.org/10.1073/pnas.96.23.13318] [PMID: 10557318]
[130]
Henriksson M, Shafqat J, Liepinsh E, et al. Unordered structure of proinsulin C-peptide in aqueous solution and in the presence of lipid vesicles. Cell Mol Life Sci 2000; 57(2): 337-42.
[http://dx.doi.org/10.1007/PL00000695] [PMID: 10766028]
[131]
Maurotti S, Pujia R, Galluccio A, et al. Preventing muscle wasting: Pro-insulin C-peptide prevents loss in muscle mass in streptozotocin-diabetic rats. J Cachexia Sarcopenia Muscle 2023; 14(2): 1117-29.
[http://dx.doi.org/10.1002/jcsm.13210] [PMID: 36878894]
[132]
Hardie DG. AMPK--sensing energy while talking to other signaling pathways. Cell Metab 2014; 20(6): 939-52.
[http://dx.doi.org/10.1016/j.cmet.2014.09.013] [PMID: 25448702]
[133]
O’Neill HM, Holloway GP, Steinberg GR. AMPK regulation of fatty acid metabolism and mitochondrial biogenesis: Implications for obesity. Mol Cell Endocrinol 2013; 366(2): 135-51.
[http://dx.doi.org/10.1016/j.mce.2012.06.019] [PMID: 22750049]
[134]
Jensen TE, Richter EA. Regulation of glucose and glycogen metabolism during and after exercise. J Physiol 2012; 590(5): 1069-76.
[http://dx.doi.org/10.1113/jphysiol.2011.224972] [PMID: 22199166]
[135]
Nakashima K, Yakabe Y. AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes. Biosci Biotechnol Biochem 2007; 71(7): 1650-6.
[http://dx.doi.org/10.1271/bbb.70057] [PMID: 17617726]
[136]
Sandri M, Sandri C, Gilbert A, et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 2004; 117(3): 399-412.
[http://dx.doi.org/10.1016/S0092-8674(04)00400-3] [PMID: 15109499]
[137]
O’Neill BT, Bhardwaj G, Penniman CM, et al. FoxO transcription factors are critical regulators of diabetes-related muscle atrophy. Diabetes 2019; 68(3): 556-70.
[http://dx.doi.org/10.2337/db18-0416] [PMID: 30523026]
[138]
Price SR, Bailey JL, Wang X, et al. Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription. J Clin Invest 1996; 98(8): 1703-8.
[http://dx.doi.org/10.1172/JCI118968] [PMID: 8878419]
[139]
Lawlor MA, Alessi DR. PKB/Akt: A key mediator of cell proliferation, survival and insulin responses? J Cell Sci 2001; 114(16): 2903-10.
[http://dx.doi.org/10.1242/jcs.114.16.2903] [PMID: 11686294]
[140]
Zhong Z, Davidescu A, Ehrén I, et al. C-peptide stimulates ERK1/2 and JNK MAP kinases via activation of protein kinase C in human renal tubular cells. Diabetologia 2005; 48(1): 187-97.
[http://dx.doi.org/10.1007/s00125-004-1602-5] [PMID: 15624099]
[141]
Zierath JR, Handberg A, Tally M, Wallberg-Henriksson H. C-peptide stimulates glucose transport in isolated human skeletal muscle independent of insulin receptor and tyrosine kinase activation. Diabetologia 1996; 39(3): 306-13.
[http://dx.doi.org/10.1007/BF00418346] [PMID: 8721776]
[142]
Johansson BL, Linde B, Wahren J. Effects of C-peptide on blood flow, capillary diffusion capacity and glucose utilization in the exercising forearm of type 1 (insulin-dependent) diabetic patients. Diabetologia 1992; 35(12): 1151-8.
[http://dx.doi.org/10.1007/BF00401369] [PMID: 1478367]
[143]
Tanaka K, Kanazawa I, Sugimoto T. Reduction in endogenous insulin secretion is a risk factor of sarcopenia in men with type 2 diabetes mellitus. Calcif Tissue Int 2015; 97(4): 385-90.
[http://dx.doi.org/10.1007/s00223-015-9990-8] [PMID: 25850525]
[144]
Fang H, Judd RL. Adiponectin regulation and function. Compr Physiol 2018; 8(3): 1031-63.
[PMID: 29978896]
[145]
Parida S, Siddharth S, Sharma D. Adiponectin, obesity, and cancer: Clash of the bigwigs in health and disease. Int J Mol Sci 2019; 20(10): 2519.
[http://dx.doi.org/10.3390/ijms20102519] [PMID: 31121868]
[146]
Magkos F, Sidossis LS. Recent advances in the measurement of adiponectin isoform distribution. Curr Opin Clin Nutr Metab Care 2007; 10(5): 571-5.
[http://dx.doi.org/10.1097/MCO.0b013e3282bf6ea8] [PMID: 17693739]
[147]
Kadowaki T, Yamauchi T. Adiponectin and adiponectin receptors. Endocr Rev 2005; 26(3): 439-51.
[http://dx.doi.org/10.1210/er.2005-0005] [PMID: 15897298]
[148]
Tsuchida A, Yamauchi T, Ito Y, et al. Insulin/Foxo1 pathway regulates expression levels of adiponectin receptors and adiponectin sensitivity. J Biol Chem 2004; 279(29): 30817-22.
[http://dx.doi.org/10.1074/jbc.M402367200] [PMID: 15123605]
[149]
Kalkman HO. An explanation for the adiponectin paradox. Pharmaceuticals 2021; 14(12): 1266.
[http://dx.doi.org/10.3390/ph14121266] [PMID: 34959666]
[150]
Tomas E, Tsao TS, Saha AK, et al. Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl–CoA carboxylase inhibition and AMP-activated protein kinase activation. Proc Natl Acad Sci USA 2002; 99(25): 16309-13.
[http://dx.doi.org/10.1073/pnas.222657499] [PMID: 12456889]
[151]
Yoon MJ, Lee GY, Chung JJ, Ahn YH, Hong SH, Kim JB. Adiponectin increases fatty acid oxidation in skeletal muscle cells by sequential activation of AMP-activated protein kinase, p38 mitogen-activated protein kinase, and peroxisome proliferator-activated receptor α. Diabetes 2006; 55(9): 2562-70.
[http://dx.doi.org/10.2337/db05-1322] [PMID: 16936205]
[152]
Fang X, Palanivel R, Zhou X, et al. Hyperglycemia- and hyperinsulinemia-induced alteration of adiponectin receptor expression and adiponectin effects in L6 myoblasts. J Mol Endocrinol 2005; 35(3): 465-76.
[http://dx.doi.org/10.1677/jme.1.01877] [PMID: 16326833]
[153]
Ceddia RB, Somwar R, Maida A, Fang X, Bikopoulos G, Sweeney G. Globular adiponectin increases GLUT4 translocation and glucose uptake but reduces glycogen synthesis in rat skeletal muscle cells. Diabetologia 2005; 48(1): 132-9.
[http://dx.doi.org/10.1007/s00125-004-1609-y] [PMID: 15619075]
[154]
Tanaka Y, Kita S, Nishizawa H, et al. Adiponectin promotes muscle regeneration through binding to T-cadherin. Sci Rep 2019; 9(1): 16.
[http://dx.doi.org/10.1038/s41598-018-37115-3] [PMID: 30626897]
[155]
Singh AK, Shree S, Chattopadhyay S, et al. Small molecule adiponectin receptor agonist GTDF protects against skeletal muscle atrophy. Mol Cell Endocrinol 2017; 439: 273-85.
[http://dx.doi.org/10.1016/j.mce.2016.09.013] [PMID: 27645900]
[156]
Komici K, Dello Iacono A, De Luca A, et al. Adiponectin and sarcopenia: A systematic review with meta-analysis. Front Endocrinol (Lausanne) 2021; 12: 576619.
[http://dx.doi.org/10.3389/fendo.2021.576619] [PMID: 33935962]
[157]
Alizadeh Pahlavani H. Exercise therapy for people with sarcopenic obesity: Myokines and adipokines as effective actors. Front Endocrinol (Lausanne) 2022; 13: 811751.
[http://dx.doi.org/10.3389/fendo.2022.811751] [PMID: 35250869]
[158]
Inoue A, Cheng XW, Huang Z, et al. Exercise restores muscle stem cell mobilization, regenerative capacity and muscle metabolic alterations via adiponectin/AdipoR1 activation in SAMP10 mice. J Cachexia Sarcopenia Muscle 2017; 8(3): 370-85.
[http://dx.doi.org/10.1002/jcsm.12166] [PMID: 27897419]
[159]
Kim TN, Won JC, Kim YJ, et al. Serum adipocyte fatty acid-binding protein levels are independently associated with sarcopenic obesity. Diabetes Res Clin Pract 2013; 101(2): 210-7.
[http://dx.doi.org/10.1016/j.diabres.2013.05.014] [PMID: 23830287]
[160]
Lu Y, Karagounis LG, Ng TP, et al. Systemic and metabolic signature of sarcopenia in community-dwelling older adults. J Gerontol 2020; 75(2): 309-17.
[PMID: 30624690]
[161]
Rossi FE, Lira FS, Silva BSA, Freire APCF, Ramos EMC, Gobbo LA. Influence of skeletal muscle mass and fat mass on the metabolic and inflammatory profile in sarcopenic and non-sarcopenic overfat elderly. Aging Clin Exp Res 2019; 31(5): 629-35.
[http://dx.doi.org/10.1007/s40520-018-1029-3] [PMID: 30178443]
[162]
Baker JF, Newman AB, Kanaya A, et al. The adiponectin paradox in the elderly: Associations with body composition, physical functioning, and mortality. J Gerontol A Biol Sci Med Sci 2019; 74(2): 247-53.
[http://dx.doi.org/10.1093/gerona/gly017] [PMID: 29438496]
[163]
Cnop M, Havel PJ, Utzschneider KM, et al. Relationship of adiponectin to body fat distribution, insulin sensitivity and plasma lipoproteins: Evidence for independent roles of age and sex. Diabetologia 2003; 46(4): 459-69.
[http://dx.doi.org/10.1007/s00125-003-1074-z] [PMID: 12687327]
[164]
Böttner A, Kratzsch J, Müller G, et al. Gender differences of adiponectin levels develop during the progression of puberty and are related to serum androgen levels. J Clin Endocrinol Metab 2004; 89(8): 4053-61.
[http://dx.doi.org/10.1210/jc.2004-0303] [PMID: 15292348]
[165]
Myers MG, Cowley MA, Münzberg H. Mechanisms of leptin action and leptin resistance. Annu Rev Physiol 2008; 70(1): 537-56.
[http://dx.doi.org/10.1146/annurev.physiol.70.113006.100707] [PMID: 17937601]
[166]
Ahima RS, Prabakaran D, Mantzoros C, et al. Role of leptin in the neuroendocrine response to fasting. Nature 1996; 382(6588): 250-2.
[http://dx.doi.org/10.1038/382250a0] [PMID: 8717038]
[167]
Bates SH, Myers MG Jr. The role of leptin receptor signaling in feeding and neuroendocrine function. Trends Endocrinol Metab 2003; 14(10): 447-52.
[http://dx.doi.org/10.1016/j.tem.2003.10.003] [PMID: 14643059]
[168]
Faggioni R, Feingold KR, Grunfeld C. Leptin regulation of the immune response and the immunodeficiency of malnutrition. FASEB J 2001; 15(14): 2565-71.
[http://dx.doi.org/10.1096/fj.01-0431rev] [PMID: 11726531]
[169]
Friedman JM. Leptin and the endocrine control of energy balance. Nat Metab 2019; 1(8): 754-64.
[http://dx.doi.org/10.1038/s42255-019-0095-y] [PMID: 32694767]
[170]
Elmquist JK, Maratos-Flier E, Saper CB, Flier JS. Unraveling the central nervous system pathways underlying responses to leptin. Nat Neurosci 1998; 1(6): 445-50.
[http://dx.doi.org/10.1038/2164] [PMID: 10196541]
[171]
Clément K, Vaisse C, Lahlou N, et al. A mutation in the human leptin receptor gene causes obesity and pituitary dysfunction. Nature 1998; 392(6674): 398-401.
[http://dx.doi.org/10.1038/32911] [PMID: 9537324]
[172]
Maffei M, Halaas J, Ravussin E, et al. Leptin levels in human and rodent: Measurement of plasma leptin and ob RNA in obese and weight-reduced subjects. Nat Med 1995; 1(11): 1155-61.
[http://dx.doi.org/10.1038/nm1195-1155] [PMID: 7584987]
[173]
Wallace AM. Measurement of leptin and leptin binding in the human circulation. Ann Clin Biochem 2000; 37(3): 244-52.
[http://dx.doi.org/10.1258/0004563001899311] [PMID: 10817237]
[174]
Zhao S, Kusminski CM, Elmquist JK, Scherer PE. Leptin: Less is more. Diabetes 2020; 69(5): 823-9.
[http://dx.doi.org/10.2337/dbi19-0018] [PMID: 32312898]
[175]
Poetsch MS, Strano A, Guan K. Role of leptin in cardiovascular diseases. Front Endocrinol (Lausanne) 2020; 11: 354.
[http://dx.doi.org/10.3389/fendo.2020.00354] [PMID: 32655492]
[176]
Wolsk E, Mygind H, Grøndahl TS, Pedersen BK, van Hall G. Human skeletal muscle releases leptin in vivo. Cytokine 2012; 60(3): 667-73.
[http://dx.doi.org/10.1016/j.cyto.2012.08.021] [PMID: 23010500]
[177]
da Costa Teixeira LA, Avelar NCP, Peixoto MFD, et al. Inflammatory biomarkers at different stages of sarcopenia in older women. Sci Rep 2023; 13(1): 10367.
[http://dx.doi.org/10.1038/s41598-023-37229-3] [PMID: 37365209]
[178]
Yang ZY, Chen WL. Examining the association between serum leptin and sarcopenic obesity. J Inflamm Res 2021; 14: 3481-7.
[http://dx.doi.org/10.2147/JIR.S320445] [PMID: 34326656]
[179]
Papadopoulou SK, Voulgaridou G, Kondyli FS, et al. Nutritional and nutrition-related biomarkers as prognostic factors of sarcopenia, and their role in disease progression. Diseases 2022; 10(3): 42.
[http://dx.doi.org/10.3390/diseases10030042] [PMID: 35892736]
[180]
Mehra MR, Vaduganathan M, Fu M, et al. A comprehensive analysis of the effects of rivaroxaban on stroke or transient ischaemic attack in patients with heart failure, coronary artery disease, and sinus rhythm: the COMMANDER HF trial. Eur Heart J 2019; 40(44): 3593-602.
[http://dx.doi.org/10.1093/eurheartj/ehz427] [PMID: 31461239]
[181]
Rodríguez A, Becerril S, Méndez-Giménez L, et al. Leptin administration activates irisin-induced myogenesis via nitric oxide-dependent mechanisms, but reduces its effect on subcutaneous fat browning in mice. Int J Obes 2015; 39(3): 397-407.
[http://dx.doi.org/10.1038/ijo.2014.166] [PMID: 25199621]
[182]
Arounleut P, Bowser M, Upadhyay S, et al. Absence of functional leptin receptor isoforms in the POUND (Lepr(db/lb)) mouse is associated with muscle atrophy and altered myoblast proliferation and differentiation. PLoS One 2013; 8(8): e72330.
[http://dx.doi.org/10.1371/journal.pone.0072330] [PMID: 23967295]
[183]
Hamrick MW, Herberg S, Arounleut P, et al. The adipokine leptin increases skeletal muscle mass and significantly alters skeletal muscle miRNA expression profile in aged mice. Biochem Biophys Res Commun 2010; 400(3): 379-83.
[http://dx.doi.org/10.1016/j.bbrc.2010.08.079] [PMID: 20800581]
[184]
Sáinz N, Rodríguez A, Catalán V, et al. Leptin administration downregulates the increased expression levels of genes related to oxidative stress and inflammation in the skeletal muscle of ob/ob mice. Mediators Inflamm 2010; 2010(1): 1-15.
[http://dx.doi.org/10.1155/2010/784343] [PMID: 20671928]
[185]
Kao TW, Peng TC, Chen WL, Chi YC, Chen CL, Yang WS. Higher serum leptin levels are associated with a reduced risk of sarcopenia but a higher risk of dynapenia among older adults. J Inflamm Res 2021; 14: 5817-25.
[http://dx.doi.org/10.2147/JIR.S335694] [PMID: 34764673]
[186]
Kohara K, Ochi M, Tabara Y, Nagai T, Igase M, Miki T. Leptin in sarcopenic visceral obesity: possible link between adipocytes and myocytes. PLoS One 2011; 6(9): e24633.
[http://dx.doi.org/10.1371/journal.pone.0024633] [PMID: 21931785]
[187]
Edwards PA, Ericsson J. Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway. Annu Rev Biochem 1999; 68(1): 157-85.
[http://dx.doi.org/10.1146/annurev.biochem.68.1.157] [PMID: 10872447]
[188]
Incardona JP, Eaton S. Cholesterol in signal transduction. Curr Opin Cell Biol 2000; 12(2): 193-203.
[http://dx.doi.org/10.1016/S0955-0674(99)00076-9] [PMID: 10712926]
[189]
Vona R, Iessi E, Matarrese P. Role of cholesterol and lipid rafts in cancer signaling: A promising therapeutic opportunity? Front Cell Dev Biol 2021; 9: 622908.
[http://dx.doi.org/10.3389/fcell.2021.622908] [PMID: 33816471]
[190]
Zhao J, Zhang X, Gao T, et al. SIK2 enhances synthesis of fatty acid and cholesterol in ovarian cancer cells and tumor growth through PI3K/Akt signaling pathway. Cell Death Dis 2020; 11(1): 25.
[http://dx.doi.org/10.1038/s41419-019-2221-x] [PMID: 31932581]
[191]
Xu H, Zhou S, Tang Q, Xia H, Bi F. Cholesterol metabolism: New functions and therapeutic approaches in cancer. Biochim Biophys Acta Rev Cancer 2020; 1874(1): 188394.
[http://dx.doi.org/10.1016/j.bbcan.2020.188394] [PMID: 32698040]
[192]
Nieddu G, Michelucci E, Formato M, et al. Molecular characterization of plasma HDL, LDL, and VLDL lipids cargos from atherosclerotic patients with advanced carotid lesions: A preliminary report. Int J Mol Sci 2022; 23(20): 12449.
[http://dx.doi.org/10.3390/ijms232012449] [PMID: 36293312]
[193]
Arora S, Patra SK, Saini R. HDL: A molecule with a multi-faceted role in coronary artery disease. Clin Chim Acta 2016; 452: 66-81.
[http://dx.doi.org/10.1016/j.cca.2015.10.021] [PMID: 26519003]
[194]
Hevonoja T, Pentikäinen MO, Hyvönen MT, Kovanen PT, Ala-Korpela M. Structure of low density lipoprotein (LDL) particles: Basis for understanding molecular changes in modified LDL. Biochim Biophys Acta Mol Cell Biol Lipids 2000; 1488(3): 189-210.
[http://dx.doi.org/10.1016/S1388-1981(00)00123-2] [PMID: 11082530]
[195]
Barrientos G, Sánchez-Aguilera P, Jaimovich E, Hidalgo C, Llanos P. Membrane cholesterol in skeletal muscle: A novel player in excitation-contraction coupling and insulin resistance. J Diabetes Res 2017; 2017: 1-8.
[http://dx.doi.org/10.1155/2017/3941898] [PMID: 28367451]
[196]
Fecchi K, Volonte D, Hezel MP, Schmeck K, Galbiati F. Spatial and temporal regulation of GLUT4 translocation by flotillin-1 and caveolin-3 in skeletal muscle cells. FASEB J 2006; 20(6): 705-7.
[http://dx.doi.org/10.1096/fj.05-4661fje] [PMID: 16455755]
[197]
Habegger KM, Penque BA, Sealls W, et al. Fat-induced membrane cholesterol accrual provokes cortical filamentous actin destabilisation and glucose transport dysfunction in skeletal muscle. Diabetologia 2012; 55(2): 457-67.
[http://dx.doi.org/10.1007/s00125-011-2334-y] [PMID: 22002007]
[198]
Roccio F, Claude-Taupin A, Botti J, Morel E, Codogno P, Dupont N. Monitoring lipophagy in kidney epithelial cells in response to shear stress. In: Kepp O, Galluzzi L, Eds. Methods in Cell Biology. Academic Press 2021; pp. 11-25.
[199]
Denton RM, Randle PJ. Concentrations of glycerides and phospholipids in rat heart and gastrocnemius muscles. Effects of alloxan-diabetes and perfusion. Biochem J 1967; 104(2): 416-22.
[http://dx.doi.org/10.1042/bj1040416] [PMID: 6048783]
[200]
Tuttle LJ, Sinacore DR, Mueller MJ. Intermuscular adipose tissue is muscle specific and associated with poor functional performance. J Aging Res 2012; 2012: 1-7.
[http://dx.doi.org/10.1155/2012/172957] [PMID: 22666591]
[201]
Hirschfeld HP, Kinsella R, Duque G. Osteosarcopenia: Where bone, muscle, and fat collide. Osteoporos Int 2017; 28(10): 2781-90.
[http://dx.doi.org/10.1007/s00198-017-4151-8] [PMID: 28733716]
[202]
Storlien LH, Jenkins AB, Chisholm DJ, Pascoe WS, Khouri S, Kraegen EW. Influence of dietary fat composition on development of insulin resistance in rats. Relationship to muscle triglyceride and ω-3 fatty acids in muscle phospholipid. Diabetes 1991; 40(2): 280-9.
[http://dx.doi.org/10.2337/diab.40.2.280] [PMID: 1991575]
[203]
Chung TH, Kwon YJ, Shim JY, Lee YJ. Association between serum triglyceride to high-density lipoprotein cholesterol ratio and sarcopenia in elderly Korean males: The Korean National Health and Nutrition Examination Survey. Clin Chim Acta 2016; 463: 165-8.
[http://dx.doi.org/10.1016/j.cca.2016.10.032] [PMID: 27983997]
[204]
Hida T, Imagama S, Ando K, et al. Sarcopenia and physical function are associated with inflammation and arteriosclerosis in community-dwelling people: The Yakumo study. Mod Rheumatol 2018; 28(2): 345-50.
[http://dx.doi.org/10.1080/14397595.2017.1349058] [PMID: 28741974]
[205]
Wang N, Chen M, Fang D. Relationship between serum triglyceride to high-density lipoprotein cholesterol ratio and sarcopenia occurrence rate in community-dwelling Chinese adults. Lipids Health Dis 2020; 19(1): 248.
[http://dx.doi.org/10.1186/s12944-020-01422-4] [PMID: 33276798]
[206]
Lin Y, Zhong S, Sun Z. Association between serum triglyceride to high-density lipoprotein cholesterol ratio and sarcopenia among elderly patients with diabetes: A secondary data analysis of the China Health and Retirement Longitudinal Study. BMJ Open 2023; 13(8): e075311.
[http://dx.doi.org/10.1136/bmjopen-2023-075311] [PMID: 37652587]
[207]
Sotak Š. Inflammatory markers in clinical practice. Vnitr Lek 2022; 68(7): E11-6.
[http://dx.doi.org/10.36290/vnl.2022.100] [PMID: 36402554]
[208]
Watson J, Round A, Hamilton W. Raised inflammatory markers. BMJ 2012; 344(feb03 1): e454.
[http://dx.doi.org/10.1136/bmj.e454] [PMID: 22306478]
[209]
Haddad F, Zaldivar F, Cooper DM, Adams GR. IL-6-induced skeletal muscle atrophy. J Appl Physiol 2005; 98(3): 911-7.
[http://dx.doi.org/10.1152/japplphysiol.01026.2004] [PMID: 15542570]
[210]
Ichinose K, Maeshima Y, Yamamoto Y, et al. 2-(8-hydroxy-6-methoxy-1-oxo-1h-2-benzopyran-3-yl) propionic acid, an inhibitor of angiogenesis, ameliorates renal alterations in obese type 2 diabetic mice. Diabetes 2006; 55(5): 1232-42.
[http://dx.doi.org/10.2337/db05-1367] [PMID: 16644677]
[211]
de Rekeneire N, Peila R, Ding J, et al. Diabetes, hyperglycemia, and inflammation in older individuals: the health, aging and body composition study. Diabetes Care 2006; 29(8): 1902-8.
[http://dx.doi.org/10.2337/dc05-2327] [PMID: 16873800]
[212]
King DE, Mainous AG III, Buchanan TA, Pearson WS. C-reactive protein and glycemic control in adults with diabetes. Diabetes Care 2003; 26(5): 1535-9.
[http://dx.doi.org/10.2337/diacare.26.5.1535] [PMID: 12716818]
[213]
Singhai M, Faizy A, Goyal R, Siddiqui SS. Evaluation of TNF-α and IL-6 levels in obese and non-obese diabetics: Pre- and postinsulin effects. N Am J Med Sci 2012; 4(4): 180-4.
[http://dx.doi.org/10.4103/1947-2714.94944] [PMID: 22536561]
[214]
Vozarova B, Weyer C, Hanson K, Tataranni PA, Bogardus C, Pratley RE. Circulating interleukin-6 in relation to adiposity, insulin action, and insulin secretion. Obes Res 2001; 9(7): 414-7.
[http://dx.doi.org/10.1038/oby.2001.54] [PMID: 11445664]
[215]
Camussi G, Albano E, Tetta C, Bussolino F. The molecular action of tumor necrosis factor-α. Eur J Biochem 1991; 202(1): 3-14.
[http://dx.doi.org/10.1111/j.1432-1033.1991.tb16337.x] [PMID: 1657606]
[216]
Larrick JW, Wright SC. Cytotoxic mechanism of tumor necrosis factor-α. FASEB J 1990; 4(14): 3215-23.
[http://dx.doi.org/10.1096/fasebj.4.14.2172061] [PMID: 2172061]
[217]
Petrovas C, Daskas SM, Lianidou ES. Determination of tumor necrosis factor-α (TNF-α) in serum by a highly sensitive enzyme amplified lanthanide luminescence immunoassay. Clin Biochem 1999; 32(4): 241-7.
[http://dx.doi.org/10.1016/S0009-9120(99)00004-1] [PMID: 10463815]
[218]
Chu WM. Tumor necrosis factor. Cancer Lett 2013; 328(2): 222-5.
[http://dx.doi.org/10.1016/j.canlet.2012.10.014] [PMID: 23085193]
[219]
Chédotal H, Narayanan D, Povlsen K, et al. Small-molecule modulators of tumor necrosis factor signaling. Drug Discov Today 2023; 28(6): 103575.
[http://dx.doi.org/10.1016/j.drudis.2023.103575] [PMID: 37003513]
[220]
Vasanthi P, Nalini G. Role of tumor necrosis factor-alpha in rheumatoid arthritis: A review. 2007; 10(4): 270-4.
[221]
Dhaliwal A, Quinlan JI, Overthrow K, et al. Sarcopenia in inflammatory bowel disease: A narrative overview. Nutrients 2021; 13(2): 656.
[http://dx.doi.org/10.3390/nu13020656] [PMID: 33671473]
[222]
Challenging correlations between psoriasis severity and tnf-α levels in hard-to-treat areas. 2023; 71(6): 1217-23.
[223]
Zhao WB, Lin KR, Xu QF. Correlation of serum IL-6, TNF-α levels and disease activity in patients with ankylosing spondylitis. 2024; 28(1): 80-9.
[PMID: 38235860]
[224]
Pan L, Xie W, Fu X, et al. Inflammation and sarcopenia: A focus on circulating inflammatory cytokines. Exp Gerontol 2021; 154: 111544.
[http://dx.doi.org/10.1016/j.exger.2021.111544] [PMID: 34478826]
[225]
Tracey KJ, Vlassara H, Cerami A. Cachectin/tumour necrosis factor. Lancet 1989; 1(8647): 1122-6.
[http://dx.doi.org/10.1016/S0140-6736(89)92394-5] [PMID: 2566060]
[226]
Uciechowski P, Dempke WCM. Interleukin-6: A masterplayer in the cytokine network. Oncology 2020; 98(3): 131-7.
[http://dx.doi.org/10.1159/000505099] [PMID: 31958792]
[227]
Rothaug M, Becker-Pauly C, Rose-John S. The role of interleukin-6 signaling in nervous tissue. Biochim Biophys Acta 2016; 1863(6): 1218-27.
[228]
Scheller J, Chalaris A, Schmidt-Arras D, Rose-John S. The pro-and anti-inflammatory properties of the cytokine interleukin-6. Biochimica et Biophysica Acta 2011; 1813(5): 878-88.
[PMID: 21296109]
[229]
Leng SX, McElhaney JE, Walston JD, Xie D, Fedarko NS, Kuchel GA. ELISA and multiplex technologies for cytokine measurement in inflammation and aging research. J Gerontol A Biol Sci Med Sci 2008; 63(8): 879-84.
[http://dx.doi.org/10.1093/gerona/63.8.879] [PMID: 18772478]
[230]
Schaper F, Rose-John S. Interleukin-6: Biology, signaling and strategies of blockade. Cytokine Growth Factor Rev 2015; 26(5): 475-87.
[http://dx.doi.org/10.1016/j.cytogfr.2015.07.004] [PMID: 26189695]
[231]
Kaur S, Bansal Y, Kumar R, Bansal G. A panoramic review of IL-6: Structure, pathophysiological roles and inhibitors. Bioorg Med Chem 2020; 28(5): 115327.
[http://dx.doi.org/10.1016/j.bmc.2020.115327] [PMID: 31992476]
[232]
Narazaki M, Tanaka T, Kishimoto T. The role and therapeutic targeting of IL-6 in rheumatoid arthritis. Expert Rev Clin Immunol 2017; 13(6): 535-51.
[http://dx.doi.org/10.1080/1744666X.2017.1295850] [PMID: 28494214]
[233]
Ridker PM, Rane M. Interleukin-6 signaling and anti-interleukin-6 therapeutics in cardiovascular disease. Circ Res 2021; 128(11): 1728-46.
[http://dx.doi.org/10.1161/CIRCRESAHA.121.319077] [PMID: 33998272]
[234]
Hirano T. IL-6 in inflammation, autoimmunity and cancer. Int Immunol 2021; 33(3): 127-48.
[http://dx.doi.org/10.1093/intimm/dxaa078] [PMID: 33337480]
[235]
Rothaug M, Becker-Pauly C. Rose-John SJBeBA-MCR (2016) The role of interleukin-6 signaling in nervous tissue. 2016; (6): 1863.
[236]
Bian AL, Hu HY, Rong YD, Wang J, Wang JX, Zhou XZ. A study on relationship between elderly sarcopenia and inflammatory factors IL-6 and TNF-α. Eur J Med Res 2017; 22(1): 25.
[http://dx.doi.org/10.1186/s40001-017-0266-9] [PMID: 28701179]
[237]
Tillett WS, Francis T Jr. Serological reactions in pneumonia with a non-protein somatic fraction of pneumococcus. J Exp Med 1930; 52(4): 561-71.
[http://dx.doi.org/10.1084/jem.52.4.561] [PMID: 19869788]
[238]
Eklund CM. Proinflammatory cytokines in CRP baseline regulation. Adv Clin Chem 2009; 48: 111-36.
[http://dx.doi.org/10.1016/S0065-2423(09)48005-3] [PMID: 19803417]
[239]
Janeway CA Jr, Medzhitov R. Innate immune recognition. Annu Rev Immunol 2002; 20(1): 197-216.
[http://dx.doi.org/10.1146/annurev.immunol.20.083001.084359] [PMID: 11861602]
[240]
Nakakuki T, Ito M, Iwasaki H, et al. Rho/Rho-kinase pathway contributes to C-reactive protein-induced plasminogen activator inhibitor-1 expression in endothelial cells. Arterioscler Thromb Vasc Biol 2005; 25(10): 2088-93.
[http://dx.doi.org/10.1161/01.ATV.0000183607.50230.9f] [PMID: 16123329]
[241]
Khanmiri HH, Yazdanfar F, Mobed A, Rezamohammadi F, Rahmani M, Haghgouei T. Biosensors; noninvasive method in detection of C-reactive protein (CRP). Biomed Microdevices 2023; 25(3): 27.
[http://dx.doi.org/10.1007/s10544-023-00666-y] [PMID: 37498420]
[242]
Christodoulides N, Mohanty S, Miller CS, et al. Application of microchip assay system for the measurement of C-reactive protein in human saliva. Lab Chip 2005; 5(3): 261-9.
[http://dx.doi.org/10.1039/b414194f] [PMID: 15726202]
[243]
Pramudji H, Demes CM, Dewi K, Tasmini T, Ahmad HS. Association of -174 G>C interleukin-6 gene polymorphism with interleukin-6 and c-reactive protein levels and obesity: A case-control study among people/residents of Western Indonesia. Med J Malaysia 2019; 74(5): 400-4.
[PMID: 31649216]
[244]
Du Clos TW. Function of C-reactive protein. Ann Med 2000; 32(4): 274-8.
[http://dx.doi.org/10.3109/07853890009011772] [PMID: 10852144]
[245]
Volanakis J. Human C-reactive protein: Expression, structure, and function. Mol Immunol 2001; 38(2-3): 189-97.
[http://dx.doi.org/10.1016/S0161-5890(01)00042-6] [PMID: 11532280]
[246]
Sproston NR, Ashworth JJ. Role of C-reactive protein at sites of inflammation and infection. Front Immunol 2018; 9: 754.
[http://dx.doi.org/10.3389/fimmu.2018.00754] [PMID: 29706967]
[247]
Melnikov I, Kozlov S, Saburova O, Avtaeva Y, Guria K, Gabbasov Z. Monomeric C-reactive protein in atherosclerotic cardiovascular disease: Advances and perspectives. Int J Mol Sci 2023; 24(3): 2079.
[http://dx.doi.org/10.3390/ijms24032079] [PMID: 36768404]
[248]
Cooper J, Pastorello Y, Slevin M. A meta-analysis investigating the relationship between inflammation in autoimmune disease, elevated CRP, and the risk of dementia. Front Immunol 2023; 14: 1087571.
[http://dx.doi.org/10.3389/fimmu.2023.1087571] [PMID: 36776896]
[249]
Luan Y, Yao Y. The clinical significance and potential role of C-reactive protein in chronic inflammatory and neurodegenerative diseases. Front Immunol 2018; 9: 1302.
[http://dx.doi.org/10.3389/fimmu.2018.01302] [PMID: 29951057]
[250]
Shokri-mashhadi N, Moradi S, Heidari Z, Saadat S. Association of circulating C-reactive protein and high-sensitivity C-reactive protein with components of sarcopenia: A systematic review and meta-analysis of observational studies. Exp Gerontol 2021; 150: 111330.
[http://dx.doi.org/10.1016/j.exger.2021.111330] [PMID: 33848566]
[251]
Mesinovic J, McMillan LB, Shore-Lorenti C, De Courten B, Ebeling PR, Scott D. Metabolic syndrome and its associations with components of sarcopenia in overweight and obese older adults. J Clin Med 2019; 8(2): 145.
[http://dx.doi.org/10.3390/jcm8020145] [PMID: 30691198]
[252]
Makki K, Froguel P, Wolowczuk I. Adipose tissue in obesity-related inflammation and insulin resistance: cells, cytokines, and chemokines. ISRN Inflamm 2013; 2013: 1-12.
[http://dx.doi.org/10.1155/2013/139239] [PMID: 24455420]
[253]
Serrano AL, Baeza-Raja B, Perdiguero E, Jardí M, Muñoz-Cánoves P. Interleukin-6 is an essential regulator of satellite cell-mediated skeletal muscle hypertrophy. Cell Metab 2008; 7(1): 33-44.
[http://dx.doi.org/10.1016/j.cmet.2007.11.011] [PMID: 18177723]
[254]
Bach E, Nielsen RR, Vendelbo MH, et al. Direct effects of TNF-α on local fuel metabolism and cytokine levels in the placebo-controlled, bilaterally infused human leg: Increased insulin sensitivity, increased net protein breakdown, and increased IL-6 release. Diabetes 2013; 62(12): 4023-9.
[http://dx.doi.org/10.2337/db13-0138] [PMID: 23835341]
[255]
Park SW, Goodpaster BH, Strotmeyer ES, et al. Accelerated loss of skeletal muscle strength in older adults with type 2 diabetes: The health, aging, and body composition study. Diabetes Care 2007; 30(6): 1507-12.
[http://dx.doi.org/10.2337/dc06-2537] [PMID: 17363749]
[256]
Cruz-Jentoft AJ, Bahat G, Bauer J, et al. Sarcopenia: Revised European consensus on definition and diagnosis. Age Ageing 2019; 48(1): 16-31.
[http://dx.doi.org/10.1093/ageing/afy169] [PMID: 30312372]
[257]
Paris MT, Bell KE, Mourtzakis M. Myokines and adipokines in sarcopenia: Understanding cross-talk between skeletal muscle and adipose tissue and the role of exercise. Curr Opin Pharmacol 2020; 52: 61-6.
[http://dx.doi.org/10.1016/j.coph.2020.06.003] [PMID: 32668398]
[258]
Kirk B, Feehan J, Lombardi G, Duque G. Muscle, bone, and fat crosstalk: the biological role of myokines, osteokines, and adipokines. Curr Osteoporos Rep 2020; 18(4): 388-400.
[http://dx.doi.org/10.1007/s11914-020-00599-y] [PMID: 32529456]
[259]
Chen MM, Zhao YP, Zhao Y, Deng SL, Yu K. Regulation of myostatin on the growth and development of skeletal muscle. Front Cell Dev Biol 2021; 9: 785712.
[http://dx.doi.org/10.3389/fcell.2021.785712] [PMID: 35004684]
[260]
Trendelenburg AU, Meyer A, Rohner D, Boyle J, Hatakeyama S, Glass DJ. Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size. Am J Physiol Cell Physiol 2009; 296(6): C1258-70.
[http://dx.doi.org/10.1152/ajpcell.00105.2009] [PMID: 19357233]
[261]
Zhu L, Wang X, Wei Z, et al. Myostatin deficiency enhances antioxidant capacity of bovine muscle via the SMAD-AMPK-G6PD pathway. Oxid Med Cell Longev 2022; 2022: 1-15.
[http://dx.doi.org/10.1155/2022/3497644] [PMID: 35663205]
[262]
Marco-Bonilla M, Fresnadillo M, Largo R, Herrero-Beaumont G. Energy regulation in inflammatory sarcopenia by the purinergic system. Int J Mol Sci 2023; 24(23): 16904.
[263]
Visser M, Pahor M, Taaffe DR, et al. Relationship of interleukin-6 and tumor necrosis factor-alpha with muscle mass and muscle strength in elderly men and women: the Health ABC Study. J Gerontol A Biol Sci Med Sci 2002; 57(5): M326-32.
[http://dx.doi.org/10.1093/gerona/57.5.M326] [PMID: 11983728]
[264]
Hamer M, Molloy GJ. Association of C-reactive protein and muscle strength in the English longitudinal study of ageing. Age (Omaha) 2009; 31(3): 171-7.
[http://dx.doi.org/10.1007/s11357-009-9097-0] [PMID: 19466582]
[265]
Langhans W, Wiesenreiter F, Scharrer E. Different effects of subcutaneous D,L-3-hydroxybutyrate and acetoacetate injections on food intake in rats. Physiol Behav 1983; 31(4): 483-6.
[http://dx.doi.org/10.1016/0031-9384(83)90070-7] [PMID: 6657769]
[266]
Cahill GF Jr. Fuel metabolism in starvation. Annu Rev Nutr 2006; 26(1): 1-22.
[http://dx.doi.org/10.1146/annurev.nutr.26.061505.111258] [PMID: 16848698]
[267]
Stubbs BJ, Koutnik AP, Volek JS, Newman JC. From bedside to battlefield: Intersection of ketone body mechanisms in geroscience with military resilience. Geroscience 2021; 43(3): 1071-81.
[http://dx.doi.org/10.1007/s11357-020-00277-y] [PMID: 33006708]
[268]
Laffel L. Ketone bodies: A review of physiology, pathophysiology and application of monitoring to diabetes. Diabetes Metab Res Rev 1999; 15(6): 412-26.
[http://dx.doi.org/10.1002/(SICI)1520-7560(199911/12)15:6<412::AID-DMRR72>3.0.CO;2-8] [PMID: 10634967]
[269]
Stentz FB, Umpierrez GE, Cuervo R, Kitabchi AE. Proinflammatory cytokines, markers of cardiovascular risks, oxidative stress, and lipid peroxidation in patients with hyperglycemic crises. Diabetes 2004; 53(8): 2079-86.
[http://dx.doi.org/10.2337/diabetes.53.8.2079] [PMID: 15277389]
[270]
Noyes KJ, Crofton P, Bath LE, et al. Hydroxybutyrate near-patient testing to evaluate a new end-point for intravenous insulin therapy in the treatment of diabetic ketoacidosis in children. Pediatr Diabetes 2007; 8(3): 150-6.
[http://dx.doi.org/10.1111/j.1399-5448.2007.00240.x] [PMID: 17550425]
[271]
Rothera ACH. Note on the sodium nitro-prusside reaction for acetone. J Physiol 1908; 37(5-6): 491-4.
[http://dx.doi.org/10.1113/jphysiol.1908.sp001285] [PMID: 16992945]
[272]
Wallace TM, Matthews DR. Recent advances in the monitoring and management of diabetic ketoacidosis. QJM 2004; 97(12): 773-80.
[http://dx.doi.org/10.1093/qjmed/hch132] [PMID: 15569808]
[273]
Dhillon KK, Gupta S. Biochemistry, Ketogenesis. Treasure Island, FL: StatPearls Publishing LLC 2023.
[274]
Robinson AM, Williamson DH. Physiological roles of ketone bodies as substrates and signals in mammalian tissues. Physiol Rev 1980; 60(1): 143-87.
[http://dx.doi.org/10.1152/physrev.1980.60.1.143] [PMID: 6986618]
[275]
McGarry JD, Woeltje KF, Kuwajima M, Foster DW. Regulation of ketogenesis and the renaissance of carnitine palmitoyltransferase. Diabetes Metab Rev 1989; 5(3): 271-84.
[http://dx.doi.org/10.1002/dmr.5610050305] [PMID: 2656156]
[276]
Fisler J, Egawa M, Bray GA. Peripheral 3-hydroxybutyrate and food intake in a model of dietary-fat induced obesity: Effect of vagotomy. Physiol Behav 1995; 58(1): 1-7.
[http://dx.doi.org/10.1016/0031-9384(94)00376-G] [PMID: 7667404]
[277]
Arase K, Fisler JS, Shargill NS, York DA, Bray GA. Intracerebroventricular infusions of 3-OHB and insulin in a rat model of dietary obesity. Am J Physiol Regul Integr Comp Physiol 1988; 255(6): R974-81.
[http://dx.doi.org/10.1152/ajpregu.1988.255.6.R974] [PMID: 3059829]
[278]
Qu SY, Yang YK, Li JY, Zeng Q, Gantz I. Agouti-related protein is a mediator of diabetic hyperphagia. Regul Pept 2001; 98(1-2): 69-75.
[http://dx.doi.org/10.1016/S0167-0115(00)00230-5] [PMID: 11179781]
[279]
Sahu A, Sninsky CA, Phelps CP, Dube MG, Kalra PS, Kalra SP. Neuropeptide Y release from the paraventricular nucleus increases in association with hyperphagia in streptozotocin-induced diabetic rats. Endocrinology 1992; 131(6): 2979-85.
[http://dx.doi.org/10.1210/endo.131.6.1446635] [PMID: 1446635]
[280]
Janardhan A, Chen J, Crawford PA. Altered systemic ketone body metabolism in advanced heart failure. Tex Heart Inst J 2011; 38(5): 533-8.
[PMID: 22163128]
[281]
Hashim SA, VanItallie TB. Ketone body therapy: From the ketogenic diet to the oral administration of ketone ester. J Lipid Res 2014; 55(9): 1818-26.
[http://dx.doi.org/10.1194/jlr.R046599] [PMID: 24598140]
[282]
Roberts MN, Wallace MA, Tomilov AA, et al. A ketogenic diet extends longevity and healthspan in adult mice. Cell Metab 2017; 26(3): 539-546.e5.
[http://dx.doi.org/10.1016/j.cmet.2017.08.005] [PMID: 28877457]
[283]
Felig P, Owen OE, Wahren J, Cahill GF Jr. Amino acid metabolism during prolonged starvation. J Clin Invest 1969; 48(3): 584-94.
[http://dx.doi.org/10.1172/JCI106017] [PMID: 5773094]
[284]
Sherwin RS, Hendler RG, Felig P. Effect of ketone infusions on amino acid and nitrogen metabolism in man. J Clin Invest 1975; 55(6): 1382-90.
[http://dx.doi.org/10.1172/JCI108057] [PMID: 1133179]
[285]
Maiz A, Moldawer LL, Bistrian BR, Birkhahn RH, Long CL, Blackburn GL. Monoacetoacetin and protein metabolism during parenteral nutrition in burned rats. Biochem J 1985; 226(1): 43-50.
[http://dx.doi.org/10.1042/bj2260043] [PMID: 3977880]
[286]
Thomsen HH, Rittig N, Johannsen M, et al. Effects of 3-hydroxybutyrate and free fatty acids on muscle protein kinetics and signaling during LPS-induced inflammation in humans: anticatabolic impact of ketone bodies. Am J Clin Nutr 2018; 108(4): 857-67.
[http://dx.doi.org/10.1093/ajcn/nqy170] [PMID: 30239561]
[287]
Koutnik AP, Poff AM, Ward NP, et al. Ketone bodies attenuate wasting in models of atrophy. J Cachexia Sarcopenia Muscle 2020; 11(4): 973-96.
[http://dx.doi.org/10.1002/jcsm.12554] [PMID: 32239651]
[288]
Shukla SK, Gebregiworgis T, Purohit V, et al. Metabolic reprogramming induced by ketone bodies diminishes pancreatic cancer cachexia. Cancer Metab 2014; 2(1): 18.
[http://dx.doi.org/10.1186/2049-3002-2-18] [PMID: 25228990]
[289]
Nair KS, Welle SL, Halliday D, Campbell RG. Effect of beta-hydroxybutyrate on whole-body leucine kinetics and fractional mixed skeletal muscle protein synthesis in humans. J Clin Invest 1988; 82(1): 198-205.
[http://dx.doi.org/10.1172/JCI113570] [PMID: 3392207]
[290]
Vandoorne T, De Smet S, Ramaekers M, et al. Intake of a ketone ester drink during recovery from exercise promotes mTORC1 signaling but not glycogen resynthesis in human muscle. Front Physiol 2017; 8: 310.
[http://dx.doi.org/10.3389/fphys.2017.00310] [PMID: 28588499]
[291]
Tomita I, Kume S, Sugahara S, et al. SGLT2 inhibition mediates protection from diabetic kidney disease by promoting ketone body-induced mTORC1 inhibition. Metabolism 2020; 32(3): 404-419.e6.
[PMID: 32726607]
[292]
Veech RL, Todd King M, Pawlosky R, Kashiwaya Y, Bradshaw PC, Curtis W. The “great” controlling nucleotide coenzymes. IUBMB Life 2019; 71(5): 565-79.
[http://dx.doi.org/10.1002/iub.1997] [PMID: 30624851]
[293]
Zou X, Meng J, Li L, et al. Acetoacetate accelerates muscle regeneration and ameliorates muscular dystrophy in mice. J Biol Chem 2016; 291(5): 2181-95.
[http://dx.doi.org/10.1074/jbc.M115.676510] [PMID: 26645687]
[294]
Koutnik AP, D’Agostino DP, Egan B. Anticatabolic effects of ketone bodies in skeletal muscle. Trends Endocrinol Metab 2019; 30(4): 227-9.
[http://dx.doi.org/10.1016/j.tem.2019.01.006] [PMID: 30712977]
[295]
Bjornsson TD. Use of serum creatinine concentrations to determine renal function. Clin Pharmacokinet 1979; 4(3): 200-22.
[http://dx.doi.org/10.2165/00003088-197904030-00003] [PMID: 383355]
[296]
Bosch JP, Saccaggi A, Lauer A, Ronco C, Belledonne M, Glabman S. Renal functional reserve in humans. Am J Med 1983; 75(6): 943-50.
[http://dx.doi.org/10.1016/0002-9343(83)90873-2] [PMID: 6650549]
[297]
Ferguson MA, Waikar SS. Established and emerging markers of kidney function. Clin Chem 2012; 58(4): 680-9.
[http://dx.doi.org/10.1373/clinchem.2011.167494] [PMID: 22311920]
[298]
Schwartz GJ, Kwong T, Erway B, et al. Validation of creatinine assays utilizing HPLC and IDMS traceable standards in sera of children. Pediatr Nephrol 2009; 24(1): 113-9.
[http://dx.doi.org/10.1007/s00467-008-0957-0] [PMID: 18769945]
[299]
Patke VG, Kansara GSJIJDMS. A comparative analytical quality evaluation study between two methods for blood urea nitrogen estimation. 2018; 17: 48-56.
[300]
Ukwueze C, Nweze E, Ukwueze IJCCP. Evaluation of haematological and biochemical changes following xylazine, tramadol and lignocaine premedicated propofol anaesthesia in West African dwarf goat. Metabolism 2023; 32(3): 433-40.
[301]
Levey AS, Bosch JP, Lewis JB, Greene T, Rogers N, Roth D. A more accurate method to estimate glomerular filtration rate from serum creatinine: A new prediction equation. Ann Intern Med 1999; 130(6): 461-70.
[http://dx.doi.org/10.7326/0003-4819-130-6-199903160-00002] [PMID: 10075613]
[302]
Stevens LA, Levey AS. Measurement of kidney function. Med Clin North Am 2005; 89(3): 457-73.
[http://dx.doi.org/10.1016/j.mcna.2004.11.009] [PMID: 15755462]
[303]
Perrone RD, Madias NE, Levey AS. Serum creatinine as an index of renal function: New insights into old concepts. Clin Chem 1992; 38(10): 1933-53.
[http://dx.doi.org/10.1093/clinchem/38.10.1933] [PMID: 1394976]
[304]
Rule AD, Bergstralh EJ, Slezak JM, Bergert J, Larson TS. Glomerular filtration rate estimated by cystatin C among different clinical presentations. Kidney Int 2006; 69(2): 399-405.
[http://dx.doi.org/10.1038/sj.ki.5000073] [PMID: 16408133]
[305]
Abrahamson M, Dalbøge H, Olafsson I, Carlsen S, Grubb A. Efficient production of native, biologically active human cystatin C by Escherichia coli. FEBS Lett 1988; 236(1): 14-8.
[http://dx.doi.org/10.1016/0014-5793(88)80276-X] [PMID: 3042461]
[306]
Curhan G. Cystatin C: A marker of renal function or something more?. Oxford University Press 2005; pp. 293-4.
[307]
Taglieri N, Koenig W, Kaski JC. Cystatin C and cardiovascular risk. Clin Chem 2009; 55(11): 1932-43.
[http://dx.doi.org/10.1373/clinchem.2009.128397] [PMID: 19713275]
[308]
van Deventer HE, Paiker JE, Katz IJ, George JA. A comparison of cystatin C- and creatinine-based prediction equations for the estimation of glomerular filtration rate in black South Africans. Nephrol Dial Transplant 2011; 26(5): 1553-8.
[http://dx.doi.org/10.1093/ndt/gfq621] [PMID: 20961892]
[309]
Hossain MA, Emara M, El moselhi H, Shoker A. Comparing measures of cystatin C in human sera by three methods. Am J Nephrol 2009; 29(5): 381-91.
[http://dx.doi.org/10.1159/000168486] [PMID: 18974639]
[310]
Manetti L, Pardini E, Genovesi M, et al. Thyroid function differently affects serum cystatin Cand creatinine concentrations. J Endocrinol Invest 2005; 28(6): 346-9.
[http://dx.doi.org/10.1007/BF03347201] [PMID: 15966508]
[311]
Knight EL, Verhave JC, Spiegelman D, et al. Factors influencing serum cystatin C levels other than renal function and the impact on renal function measurement. Kidney Int 2004; 65(4): 1416-21.
[http://dx.doi.org/10.1111/j.1523-1755.2004.00517.x] [PMID: 15086483]
[312]
Ockner RK, Manning JA, Poppenhausen RB, Ho WKL. A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium, and other tissues. Science 1972; 177(4043): 56-8.
[http://dx.doi.org/10.1126/science.177.4043.56] [PMID: 5041774]
[313]
Basak S, Mallick R, Banerjee A, Pathak S, Duttaroy AK. Cytoplasmic fatty acid-binding proteins in metabolic diseases and cancers. In: Donev R, Ed. Advances in Protein Chemistry and Structural Biology. Academic Press 2022; pp. 143-74.
[314]
Xu Y, Xie Y, Shao X, Ni Z, Mou S. L-FABP: A novel biomarker of kidney disease. Clin Chim Acta 2015; 445: 85-90.
[http://dx.doi.org/10.1016/j.cca.2015.03.017] [PMID: 25797895]
[315]
Araki S, Haneda M, Koya D, et al. Predictive effects of urinary liver-type fatty acid-binding protein for deteriorating renal function and incidence of cardiovascular disease in type 2 diabetic patients without advanced nephropathy. Diabetes Care 2013; 36(5): 1248-53.
[http://dx.doi.org/10.2337/dc12-1298] [PMID: 23223350]
[316]
Xu A, Wang Y, Xu JY, et al. Adipocyte fatty acid-binding protein is a plasma biomarker closely associated with obesity and metabolic syndrome. Clin Chem 2006; 52(3): 405-13.
[http://dx.doi.org/10.1373/clinchem.2005.062463] [PMID: 16423904]
[317]
Yeung DCY, Wang Y, Xu A, et al. Epidermal fatty-acid-binding protein: A new circulating biomarker associated with cardio-metabolic risk factors and carotid atherosclerosis. Eur Heart J 2008; 29(17): 2156-63.
[http://dx.doi.org/10.1093/eurheartj/ehn295] [PMID: 18603624]
[318]
Choi EB, Jeong JH, Jang HM, et al. Skeletal lipocalin-2 is associated with iron-related oxidative stress in ob/ob mice with sarcopenia. Antioxidants 2021; 10(5): 758.
[http://dx.doi.org/10.3390/antiox10050758] [PMID: 34064680]
[319]
Zheng C, Wang E, Li JS, et al. Serum creatinine/cystatin C ratio as a screening tool for sarcopenia and prognostic indicator for patients with esophageal cancer. BMC Geriatr 2022; 22(1): 207.
[http://dx.doi.org/10.1186/s12877-022-02925-8] [PMID: 35287579]
[320]
Ribeiro HS, Neri SGR, Oliveira JS, Bennett PN, Viana JL, Lima RM. Association between sarcopenia and clinical outcomes in chronic kidney disease patients: A systematic review and meta-analysis. Clin Nutr 2022; 41(5): 1131-40.
[http://dx.doi.org/10.1016/j.clnu.2022.03.025] [PMID: 35430544]
[321]
Wilkinson TJ, Miksza J, Yates T, et al. Association of sarcopenia with mortality and end-stage renal disease in those with chronic kidney disease: A UK biobank study. J Cachexia Sarcopenia Muscle 2021; 12(3): 586-98.
[http://dx.doi.org/10.1002/jcsm.12705] [PMID: 33949807]
[322]
Shin JY. Low serum creatinine to cystatin C ratio is independently associated with sarcopenia and high carotid plaque score in patients with type 2 diabetes. Nutr Metab Cardiovasc Dis 2022; 32(6): 1454-62.
[http://dx.doi.org/10.1016/j.numecd.2022.02.005] [PMID: 35256230]
[323]
Hashimoto Y, Takahashi F, Okamura T, et al. Relationship between serum creatinine to cystatin C ratio and subclinical atherosclerosis in patients with type 2 diabetes. BMJ Open Diabetes Res Care 2022; 10(3): e002910.
[http://dx.doi.org/10.1136/bmjdrc-2022-002910] [PMID: 35738823]
[324]
He Q, Jiang J, Xie L, Zhang L, Yang M. A sarcopenia index based on serum creatinine and cystatin C cannot accurately detect either low muscle mass or sarcopenia in urban community-dwelling older people. Sci Rep 2018; 8(1): 11534.
[http://dx.doi.org/10.1038/s41598-018-29808-6] [PMID: 30068907]
[325]
Yang R, Zhang Y, Shen X, Yan S. Sarcopenia associated with renal function in the patients with type 2 diabetes. Diabetes Res Clin Pract 2016; 118: 121-9.
[http://dx.doi.org/10.1016/j.diabres.2016.06.023] [PMID: 27368064]
[326]
Tanabe J, Ogura Y, Kosaki K, et al. Relationship between urinary liver-type fatty acid-binding protein (L-FABP) and sarcopenia in spontaneously diabetic torii fatty rats. J Diabetes Res 2020; 2020: 1-14.
[http://dx.doi.org/10.1155/2020/7614035] [PMID: 32405506]
[327]
Kosaki K, Kamijo-Ikemori A, Sugaya T, et al. Effect of habitual exercise on urinary liver-type fatty acid-binding protein levels in middle-aged and older adults. Scand J Med Sci Sports 2018; 28(1): 152-60.
[http://dx.doi.org/10.1111/sms.12867] [PMID: 28247579]
[328]
Oinonen C, Rouvinen J. Structural comparison of Ntn-hydrolases. Protein Sci 2000; 9(12): 2329-37.
[http://dx.doi.org/10.1110/ps.9.12.2329] [PMID: 11206054]
[329]
Wenham PR, Horn DB, Smith AF. In vitro studies upon the release of γ-glutamyltransferase from human liver. Clin Chim Acta 1986; 160(3): 223-33.
[http://dx.doi.org/10.1016/0009-8981(86)90189-0] [PMID: 2878744]
[330]
Bathum L, Petersen HC, Rosholm JU, Hyltoft Petersen P, Vaupel J, Christensen K. Evidence for a substantial genetic influence on biochemical liver function tests: results from a population-based Danish twin study. Clin Chem 2001; 47(1): 81-7.
[http://dx.doi.org/10.1093/clinchem/47.1.81] [PMID: 11148181]
[331]
Zhang R, Wang Q. Comparability of four clinical laboratory measurement methods for GGT and commutability of candidate reference materials. J Clin Lab Anal 2020; 34(12): e23557.
[http://dx.doi.org/10.1002/jcla.23557] [PMID: 32914473]
[332]
Kunutsor SK. Gamma-glutamyltransferase—friend or foe within? Liver Int 2016; 36(12): 1723-34.
[http://dx.doi.org/10.1111/liv.13221] [PMID: 27512925]
[333]
Ndrepepa G, Kastrati A. Gamma-glutamyl transferase and cardiovascular disease. Ann Transl Med 2016; 4(24): 481.
[http://dx.doi.org/10.21037/atm.2016.12.27] [PMID: 28149843]
[334]
André P, Balkau B, Born C, Charles MA, Eschwège E. Three-year increase of gamma-glutamyltransferase level and development of type 2 diabetes in middle-aged men and women: The D.E.S.I.R. cohort. Diabetologia 2006; 49(11): 2599-603.
[http://dx.doi.org/10.1007/s00125-006-0418-x] [PMID: 16969645]
[335]
Wannamethee SG, Shaper AG, Lennon L, Whincup PH. Hepatic enzymes, the metabolic syndrome, and the risk of type 2 diabetes in older men. Diabetes Care 2005; 28(12): 2913-8.
[http://dx.doi.org/10.2337/diacare.28.12.2913] [PMID: 16306554]
[336]
Ko SH, Baeg MK, Han KD, Ko SH, Ahn YB. Increased liver markers are associated with higher risk of type 2 diabetes. World J Gastroenterol 2015; 21(24): 7478-87.
[http://dx.doi.org/10.3748/wjg.v21.i24.7478] [PMID: 26139993]
[337]
Kaneko K, Yatsuya H, Li Y, et al. Association of gamma-glutamyl transferase and alanine aminotransferase with type 2 diabetes mellitus incidence in middle-aged Japanese men: 12-year follow up. J Diabetes Investig 2019; 10(3): 837-45.
[http://dx.doi.org/10.1111/jdi.12930] [PMID: 30204299]
[338]
Mantovani A, Byrne CD, Bonora E, Targher G. Nonalcoholic fatty liver disease and risk of incident type 2 diabetes: A meta-analysis. Diabetes Care 2018; 41(2): 372-82.
[http://dx.doi.org/10.2337/dc17-1902] [PMID: 29358469]
[339]
Henriksen EJ, Diamond-Stanic MK, Marchionne EM. Oxidative stress and the etiology of insulin resistance and type 2 diabetes. Free Radic Biol Med 2011; 51(5): 993-9.
[http://dx.doi.org/10.1016/j.freeradbiomed.2010.12.005] [PMID: 21163347]
[340]
Hong N, Lee EY, Kim CO. Gamma-glutamyl transferase is associated with sarcopenia and sarcopenic obesity in community-dwelling older adults: Results from the Fifth Korea National Health and Nutrition Examination Survey, 2010-2011. Endocr J 2015; 62(7): 585-92.
[http://dx.doi.org/10.1507/endocrj.EJ15-0119] [PMID: 25913781]
[341]
Sack C, Ferrari N, Friesen D, et al. Health risks of sarcopenic obesity in overweight children and adolescents: Data from the CHILT III programme (Cologne). J Clin Med 2022; 11(1): 277.
[http://dx.doi.org/10.3390/jcm11010277] [PMID: 35012017]
[342]
Buck M, Chojkier M. Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants. EMBO J 1996; 15(8): 1753-65.
[http://dx.doi.org/10.1002/j.1460-2075.1996.tb00524.x] [PMID: 8617220]
[343]
Tsujinaka T, Fujita J, Ebisui C, et al. Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice. J Clin Invest 1996; 97(1): 244-9.
[http://dx.doi.org/10.1172/JCI118398] [PMID: 8550842]
[344]
Karp DR, Shimooku K, Lipsky PE. Expression of γ-glutamyl transpeptidase protects ramos B cells from oxidation-induced cell death. J Biol Chem 2001; 276(6): 3798-804.
[http://dx.doi.org/10.1074/jbc.M008484200] [PMID: 11080500]
[345]
Xie W, Xiao G, Fan Y, He M, Lv S, Li Y. Sarcopenic obesity: Research advances in pathogenesis and diagnostic criteria. Aging Clin Exp Res 2021; 33(2): 247-52.
[http://dx.doi.org/10.1007/s40520-019-01435-9] [PMID: 31845200]
[346]
Wang H, Chu WS, Hemphill C, Elbein SC. Human resistin gene: molecular scanning and evaluation of association with insulin sensitivity and type 2 diabetes in Caucasians. J Clin Endocrinol Metab 2002; 87(6): 2520-4.
[http://dx.doi.org/10.1210/jcem.87.6.8528] [PMID: 12050208]
[347]
Yang RZ, Huang Q, Xu A, et al. Comparative studies of resistin expression and phylogenomics in human and mouse. Biochem Biophys Res Commun 2003; 310(3): 927-35.
[http://dx.doi.org/10.1016/j.bbrc.2003.09.093] [PMID: 14550293]
[348]
Bokarewa M, Nagaev I, Dahlberg L, Smith U, Tarkowski A. Resistin, an adipokine with potent proinflammatory properties. J Immunol 2005; 174(9): 5789-95.
[http://dx.doi.org/10.4049/jimmunol.174.9.5789] [PMID: 15843582]
[349]
Jamaluddin MS, Weakley SM, Yao Q, Chen C. Resistin: Functional roles and therapeutic considerations for cardiovascular disease. Br J Pharmacol 2012; 165(3): 622-32.
[http://dx.doi.org/10.1111/j.1476-5381.2011.01369.x] [PMID: 21545576]
[350]
Steppan CM, Brown EJ, Wright CM, et al. A family of tissue-specific resistin-like molecules. Proc Natl Acad Sci USA 2001; 98(2): 502-6.
[http://dx.doi.org/10.1073/pnas.98.2.502] [PMID: 11209052]
[351]
Benomar Y, Taouis M. Molecular mechanisms underlying obesity-induced hypothalamic inflammation and insulin resistance: Pivotal role of resistin/TLR4 pathways. Front Endocrinol (Lausanne) 2019; 10: 140.
[http://dx.doi.org/10.3389/fendo.2019.00140] [PMID: 30906281]
[352]
Gharibeh MY, Al Tawallbeh GM, Abboud MM, Radaideh A, Alhader AA, Khabour OF. Correlation of plasma resistin with obesity and insulin resistance in type 2 diabetic patients. Diabetes Metab 2010; 36(6): 443-9.
[http://dx.doi.org/10.1016/j.diabet.2010.05.003] [PMID: 20739208]
[353]
Osawa H, Ochi M, Kato K, et al. Serum resistin is associated with the severity of microangiopathies in type 2 diabetes. Biochem Biophys Res Commun 2007; 355(2): 342-6.
[http://dx.doi.org/10.1016/j.bbrc.2007.01.144] [PMID: 17303077]
[354]
Randeva H, Karteris E, Lewandowski KC, Sailesh S, O’Hare P, Hillhouse EW. Circadian rhythmicity of salivary leptin in healthy subjects. Mol Genet Metab 2003; 78(3): 229-35.
[http://dx.doi.org/10.1016/S1096-7192(03)00004-0] [PMID: 12649069]
[355]
Li M, Fisette A, Zhao X-Y, Deng J-Y, Mi J, Cianflone K. Serum resistin correlates with central obesity but weakly with insulin resistance in Chinese children and adolescents. Int J Obes 2009; 33(4): 424-39.
[http://dx.doi.org/10.1038/ijo.2009.44] [PMID: 19290012]
[356]
Benomar Y, Gertler A, De Lacy P, et al. Central resistin overexposure induces insulin resistance through Toll-like receptor 4. Diabetes 2013; 62(1): 102-14.
[http://dx.doi.org/10.2337/db12-0237] [PMID: 22961082]
[357]
Benomar Y, Amine H, Crépin D, et al. Central resistin/TLR4 impairs adiponectin signaling, contributing to insulin and FGF21 resistance. Diabetes 2016; 65(4): 913-26.
[http://dx.doi.org/10.2337/db15-1029] [PMID: 26740596]
[358]
Santilli F, Liani R, Di Fulvio P, et al. Increased circulating resistin is associated with insulin resistance, oxidative stress and platelet activation in type 2 diabetes mellitus. Thromb Haemost 2016; 116(12): 1089-99.
[http://dx.doi.org/10.1160/TH16-06-0471] [PMID: 27709225]
[359]
Pang SS, Le YY. Role of resistin in inflammation and inflammation-related diseases. Cell Mol Immunol 2006; 3(1): 29-34.
[PMID: 16549046]
[360]
Gao J, Deng M, Li Y, et al. Resistin as a systemic inflammation-related biomarker for sarcopenia in patients with chronic obstructive pulmonary disease. Front Nutr 2022; 9: 921399.
[http://dx.doi.org/10.3389/fnut.2022.921399] [PMID: 35903456]
[361]
Ikeda Y, Kawamura R, Takata Y, et al. Resistin G : A haplotype at SNP -420/-358 is associated with the latent sarcopenic obesity index in the toon genome study. J Diabetes Investig 2023; 14(5): 686-94.
[http://dx.doi.org/10.1111/jdi.13998] [PMID: 36897532]
[362]
Priego T, Martín AI, González-Hedström D, Granado M, López-Calderón A. Role of hormones in sarcopenia. Vitam Horm 2021; 115: 535-70.
[http://dx.doi.org/10.1016/bs.vh.2020.12.021] [PMID: 33706961]
[363]
O’Leary MF, Wallace GR, Davis ET, et al. Obese subcutaneous adipose tissue impairs human myogenesis, particularly in old skeletal muscle, via resistin-mediated activation of NFκB. Sci Rep 2018; 8(1): 15360.
[http://dx.doi.org/10.1038/s41598-018-33840-x] [PMID: 30337633]
[364]
Deacon CF, Ahrén B. Physiology of incretins in health and disease. Rev Diabet Stud 2011; 8(3): 293-306.
[http://dx.doi.org/10.1900/RDS.2011.8.293] [PMID: 22262068]
[365]
Bak MJ, Wewer Albrechtsen NJ, Pedersen J, et al. Specificity and sensitivity of commercially available assays for glucagon-like peptide-1 (GLP-1): Implications for GLP -1 measurements in clinical studies. Diabetes Obes Metab 2014; 16(11): 1155-64.
[http://dx.doi.org/10.1111/dom.12352] [PMID: 25041349]
[366]
Smith NK, Hackett TA, Galli A, Flynn CR. GLP-1: Molecular mechanisms and outcomes of a complex signaling system. Neurochem Int 2019; 128: 94-105.
[http://dx.doi.org/10.1016/j.neuint.2019.04.010] [PMID: 31002893]
[367]
Grieco M, Giorgi A, Gentile MC, et al. Glucagon-like peptide-1: A focus on neurodegenerative diseases. Front Neurosci 2019; 13: 1112.
[http://dx.doi.org/10.3389/fnins.2019.01112] [PMID: 31680842]
[368]
Andersen A, Lund A, Knop FK, Vilsbøll T. Glucagon-like peptide 1 in health and disease. Nat Rev Endocrinol 2018; 14(7): 390-403.
[http://dx.doi.org/10.1038/s41574-018-0016-2] [PMID: 29728598]
[369]
Gurjar AA, Kushwaha S, Chattopadhyay S, et al. Long acting GLP-1 analog liraglutide ameliorates skeletal muscle atrophy in rodents. Metabolism 2020; 103: 154044.
[http://dx.doi.org/10.1016/j.metabol.2019.154044] [PMID: 31812628]
[370]
Green CJ, Henriksen TI, Pedersen BK, Solomon TP. Glucagon like peptide-1-induced glucose metabolism in differentiated human muscle satellite cells is attenuated by hyperglycemia. PLoS One 2012; 7(8): e44284.
[http://dx.doi.org/10.1371/journal.pone.0044284]
[371]
Choung JS, Lee YS, Jun HS. Exendin-4 increases oxygen consumption and thermogenic gene expression in muscle cells. J Mol Endocrinol 2017; 58(2): 79-90.
[http://dx.doi.org/10.1530/JME-16-0078] [PMID: 27872157]
[372]
Sjøberg KA, Holst JJ, Rattigan S, Richter EA, Kiens B. GLP-1 increases microvascular recruitment but not glucose uptake in human and rat skeletal muscle. Am J Physiol Endocrinol Metab 2014; 306(4): E355-62.
[http://dx.doi.org/10.1152/ajpendo.00283.2013] [PMID: 24302010]
[373]
Yamamoto K, Amako M, Yamamoto Y, et al. Therapeutic effect of exendin-4, a long-acting analogue of glucagon-like peptide-1 receptor agonist, on nerve regeneration after the crush nerve injury. BioMed Res Int 2013; 2013: 1-7.
[http://dx.doi.org/10.1155/2013/315848] [PMID: 23984340]
[374]
Hong Y, Lee JH, Jeong KW, Choi CS, Jun HS. Amelioration of muscle wasting by glucagon-like peptide-1 receptor agonist in muscle atrophy. J Cachexia Sarcopenia Muscle 2019; 10(4): 903-18.
[http://dx.doi.org/10.1002/jcsm.12434] [PMID: 31020810]
[375]
Subaran SC, Sauder MA, Chai W, et al. GLP-1 at physiological concentrations recruits skeletal and cardiac muscle microvasculature in healthy humans. Clin Sci (Lond) 2014; 127(3): 163-70.
[http://dx.doi.org/10.1042/CS20130708] [PMID: 24552454]
[376]
Trahair LG, Horowitz M, Hausken T, Feinle-Bisset C, Rayner CK, Jones KL. Effects of exogenous glucagon-like peptide-1 on the blood pressure, heart rate, mesenteric blood flow, and glycemic responses to intraduodenal glucose in healthy older subjects. J Clin Endocrinol Metab 2014; 99(12): E2628-34.
[http://dx.doi.org/10.1210/jc.2014-2475] [PMID: 25210879]
[377]
Jensen EP, Poulsen SS, Kissow H, et al. Activation of GLP-1 receptors on vascular smooth muscle cells reduces the autoregulatory response in afferent arterioles and increases renal blood flow. Am J Physiol Renal Physiol 2015; 308(8): F867-77.
[http://dx.doi.org/10.1152/ajprenal.00527.2014] [PMID: 25656368]
[378]
Osaka T, Hamaguchi M, Fukui M. Favorable appendicular skeletal muscle mass changes in older patients with type 2 diabetes receiving GLP-1 receptor agonist and basal insulin co-therapy. Clin Med Insights Endocrinol Diabetes 2023; 16: 11795514231161885.
[http://dx.doi.org/10.1177/11795514231161885] [PMID: 37025567]
[379]
Xiang J, Qin L, Zhong J, Xia N, Liang Y. GLP-1RA liraglutide and semaglutide improves obesity-induced muscle atrophy via SIRT1 pathway. Diabetes Metab Syndr Obes 2023; 16: 2433-46.
[http://dx.doi.org/10.2147/DMSO.S425642] [PMID: 37602204]
[380]
Iwai S, Kaji K, Nishimura N, et al. Glucagon-like peptide-1 receptor agonist, semaglutide attenuates chronic liver disease-induced skeletal muscle atrophy in diabetic mice. Biochim Biophys Acta Mol Basis Dis 2023; 1869(7): 166770.
[http://dx.doi.org/10.1016/j.bbadis.2023.166770] [PMID: 37276988]
[381]
Perna S, Guido D, Bologna C, et al. Liraglutide and obesity in elderly: efficacy in fat loss and safety in order to prevent sarcopenia. A perspective case series study. Aging Clin Exp Res 2016; 28(6): 1251-7.
[http://dx.doi.org/10.1007/s40520-015-0525-y] [PMID: 26749118]