{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T19:47:23Z","timestamp":1792180043392,"version":"4.4.0"},"reference-count":95,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2020,5,28]],"date-time":"2020-05-28T00:00:00Z","timestamp":1590624000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Gyeongsangbuk-Do and Gyeongbuk Science &amp; Technology Promotion Center of Korea","award":["SF319003A"],"award-info":[{"award-number":["SF319003A"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The extracellular matrix (ECM) provides a scaffold for cells, controlling biological processes and providing structural as well as mechanical support to surrounding cells. Disruption of ECM homeostasis results in several pathological conditions. Skeletal muscle ECM is a complex network comprising collagens, proteoglycans, glycoproteins, and elastin. Recent therapeutic approaches targeting ECM remodeling have been extensively deliberated. Various ECM components are typically found to be augmented in the skeletal muscle of obese and\/or diabetic humans. Skeletal muscle ECM remodeling is thought to be a feature of the pathogenic milieu allied with metabolic dysregulation, obesity, and eventual diabetes. This narrative review explores the current understanding of key components of skeletal muscle ECM and their specific roles in the regulation of metabolic diseases. Additionally, we discuss muscle-specific integrins and their role in the regulation of insulin sensitivity. A better understanding of the importance of skeletal muscle ECM remodeling, integrin signaling, and other factors that regulate insulin activity may help in the development of novel therapeutics for managing diabetes and other metabolic disorders.<\/jats:p>","DOI":"10.3390\/ijms21113845","type":"journal-article","created":{"date-parts":[[2020,5,28]],"date-time":"2020-05-28T10:02:45Z","timestamp":1590660165000},"page":"3845","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":45,"title":["Implications of Skeletal Muscle Extracellular Matrix Remodeling in Metabolic Disorders: Diabetes Perspective"],"prefix":"10.3390","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1095-8445","authenticated-orcid":false,"given":"Khurshid","family":"Ahmad","sequence":"first","affiliation":[{"name":"Department of Medical Biotechnology, Yeungnam University, Gyeongsan 38541, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inho","family":"Choi","sequence":"additional","affiliation":[{"name":"Department of Medical Biotechnology, Yeungnam University, Gyeongsan 38541, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong-Ho","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Biomedical Science, Daegu Catholic University, Gyeongsan 38430, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,5,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"142","DOI":"10.3389\/fphar.2020.00142","article-title":"Cross-Talk Between Extracellular Matrix and Skeletal Muscle: Implications for Myopathies","volume":"11","author":"Ahmad","year":"2020","journal-title":"Front. Pharmacol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1038\/nrm3904","article-title":"Remodelling the extracellular matrix in development and disease","volume":"15","author":"Bonnans","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1007\/978-1-4939-9133-4_21","article-title":"Novel Approaches for Extracellular Matrix Targeting in Disease Treatment","volume":"1952","author":"Afratis","year":"2019","journal-title":"Methods Mol. Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.matbio.2018.03.023","article-title":"Extracellular matrix: The driving force of mammalian diseases","volume":"71\u201372","author":"Iozzo","year":"2018","journal-title":"Matrix Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1177\/1535370216675065","article-title":"Targeting extracellular matrix remodeling in disease: Could resveratrol be a potential candidate?","volume":"242","author":"Agarwal","year":"2017","journal-title":"Exp. Biol. Med. (Maywood)"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"42","DOI":"10.3389\/fphys.2019.00042","article-title":"Role of Myokines in Regulating Skeletal Muscle Mass and Function","volume":"10","author":"Lee","year":"2019","journal-title":"Front. Physiol."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Ahmad, K., Lee, E.J., Moon, J.S., Park, S.Y., and Choi, I. (2018). Multifaceted Interweaving Between Extracellular Matrix, Insulin Resistance, and Skeletal Muscle. Cells, 7.","DOI":"10.3390\/cells7100148"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1152\/physrev.00043.2011","article-title":"Satellite cells and the muscle stem cell niche","volume":"93","author":"Yin","year":"2013","journal-title":"Physiol. Rev."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"12601","DOI":"10.1074\/jbc.R200027200","article-title":"The basement membrane\/basal lamina of skeletal muscle","volume":"278","author":"Sanes","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"253","DOI":"10.3389\/fphys.2020.00253","article-title":"Skeletal Muscle Extracellular Matrix - What Do We Know About Its Composition, Regulation, and Physiological Roles? A Narrative Review","volume":"11","author":"Csapo","year":"2020","journal-title":"Front. Physiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.physbeh.2008.01.020","article-title":"Type 2 diabetes mellitus and skeletal muscle metabolic function","volume":"94","author":"Phielix","year":"2008","journal-title":"Physiol. Behav."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1002\/mus.22094","article-title":"Structure and function of the skeletal muscle extracellular matrix","volume":"44","author":"Gillies","year":"2011","journal-title":"Muscle Nerve"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"10542","DOI":"10.1038\/s41598-019-46896-0","article-title":"Extracellular matrix composition of connective tissues: A systematic review and meta-analysis","volume":"9","author":"McKee","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1042\/bj2191017","article-title":"Characterization of muscle epimysium, perimysium and endomysium collagens","volume":"219","author":"Light","year":"1984","journal-title":"Biochem. J."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.3181\/0703-MR-72","article-title":"Structure and function of basement membranes","volume":"232","author":"LeBleu","year":"2007","journal-title":"Exp. Biol. Med. (Maywood)"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"25404","DOI":"10.1074\/jbc.273.39.25404","article-title":"Collagen XVIII is a basement membrane heparan sulfate proteoglycan","volume":"273","author":"Halfter","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"256","DOI":"10.2353\/ajpath.2009.080522","article-title":"Laminin-111 restores regenerative capacity in a mouse model for alpha7 integrin congenital myopathy","volume":"174","author":"Rooney","year":"2009","journal-title":"Am. J. Pathol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1006\/excr.2002.5499","article-title":"Expression and distribution of laminin alpha1 and alpha2 chains in embryonic and adult mouse tissues: An immunochemical approach","volume":"275","author":"Sasaki","year":"2002","journal-title":"Exp. Cell Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3264","DOI":"10.1073\/pnas.87.9.3264","article-title":"Merosin, a tissue-specific basement membrane protein, is a laminin-like protein","volume":"87","author":"Ehrig","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Kim, T., Ahmad, K., Shaikh, S., Jan, A.T., Seo, M.G., Lee, E.J., and Choi, I. (2019). Dermatopontin in Skeletal Muscle Extracellular Matrix Regulates Myogenesis. Cells, 8.","DOI":"10.3390\/cells8040332"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1096\/fj.201700665R","article-title":"Fibromodulin and regulation of the intricate balance between myoblast differentiation to myocytes or adipocyte-like cells","volume":"32","author":"Lee","year":"2018","journal-title":"FASEB J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.lfs.2016.12.011","article-title":"Matrix gla protein: An extracellular matrix protein regulates myostatin expression in the muscle developmental program","volume":"172","author":"Ahmad","year":"2017","journal-title":"Life Sci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.biocel.2016.09.023","article-title":"Fibromodulin: A regulatory molecule maintaining cellular architecture for normal cellular function","volume":"80","author":"Jan","year":"2016","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2708","DOI":"10.1096\/fj.201500133R","article-title":"Fibromodulin: A master regulator of myostatin controlling progression of satellite cells through a myogenic program","volume":"30","author":"Lee","year":"2016","journal-title":"FASEB J."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Unamuno, X., Gomez-Ambrosi, J., Ramirez, B., Rodriguez, A., Becerril, S., Valenti, V., Moncada, R., Silva, C., Salvador, J., and Fruhbeck, G. (2020). Dermatopontin, A Novel Adipokine Promoting Adipose Tissue Extracellular Matrix Remodelling and Inflammation in Obesity. J. Clin. Med., 9.","DOI":"10.3390\/jcm9041069"},{"key":"ref_26","first-page":"a004978","article-title":"The collagen family","volume":"3","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1038\/nrm3902","article-title":"Extracellular matrix assembly: A multiscale deconstruction","volume":"15","author":"Mouw","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1111\/j.1432-0436.1984.tb00279.x","article-title":"Role of muscle fibroblasts in the deposition of type-IV collagen in the basal lamina of myotubes","volume":"28","author":"Kuhl","year":"1984","journal-title":"Differentiation"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1097\/00003677-200201000-00005","article-title":"Intramuscular extracellular matrix: Complex environment of muscle cells","volume":"30","author":"Kovanen","year":"2002","journal-title":"Exerc. Sport Sci. Rev."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.matbio.2011.12.003","article-title":"Expression of collagen VI alpha5 and alpha6 chains in human muscle and in Duchenne muscular dystrophy-related muscle fibrosis","volume":"31","author":"Sabatelli","year":"2012","journal-title":"Matrix Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/nrneurol.2011.81","article-title":"The collagen VI-related myopathies: Muscle meets its matrix","volume":"7","author":"Bonnemann","year":"2011","journal-title":"Nat. Rev. Neurol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2663","DOI":"10.1523\/JNEUROSCI.2847-15.2016","article-title":"Slow Muscle Precursors Lay Down a Collagen XV Matrix Fingerprint to Guide Motor Axon Navigation","volume":"36","author":"Guillon","year":"2016","journal-title":"J. Neurosci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"22514","DOI":"10.1074\/jbc.M400536200","article-title":"A novel marker of tissue junctions, collagen XXII","volume":"279","author":"Koch","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"4602","DOI":"10.1242\/dev.096024","article-title":"Knockdown of col22a1 gene in zebrafish induces a muscular dystrophy by disruption of the myotendinous junction","volume":"140","author":"Charvet","year":"2013","journal-title":"Development"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1210\/jc.2013-4381","article-title":"Weight gain reveals dramatic increases in skeletal muscle extracellular matrix remodeling","volume":"99","author":"Tam","year":"2014","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"416","DOI":"10.2337\/db10-1116","article-title":"Diet-induced muscle insulin resistance is associated with extracellular matrix remodeling and interaction with integrin alpha2beta1 in mice","volume":"60","author":"Kang","year":"2011","journal-title":"Diabetes"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"E560","DOI":"10.1152\/ajpendo.00202.2005","article-title":"Increased collagen content in insulin-resistant skeletal muscle","volume":"290","author":"Berria","year":"2006","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"E900","DOI":"10.1152\/ajpendo.00444.2005","article-title":"Effects of streptozotocin-induced diabetes and physical training on gene expression of extracellular matrix proteins in mouse skeletal muscle","volume":"290","author":"Lehti","year":"2006","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"111","DOI":"10.4161\/cam.22618","article-title":"Laminin-211 in skeletal muscle function","volume":"7","author":"Holmberg","year":"2013","journal-title":"Cell Adhes. Migr."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/s004410051279","article-title":"The alpha7beta1 integrin in muscle development and disease","volume":"296","author":"Burkin","year":"1999","journal-title":"Cell Tissue Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"14587","DOI":"10.1074\/jbc.R200022200","article-title":"Integrins: Redundant or important players in skeletal muscle?","volume":"278","author":"Mayer","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1016\/0092-8674(91)90035-W","article-title":"Membrane organization of the dystrophin-glycoprotein complex","volume":"66","author":"Ervasti","year":"1991","journal-title":"Cell"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1093\/emboj\/18.4.863","article-title":"Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins","volume":"18","author":"Talts","year":"1999","journal-title":"EMBO J."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1080\/03008200591008527","article-title":"Functional sites in the laminin alpha chains","volume":"46","author":"Suzuki","year":"2005","journal-title":"Connect. Tissue Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/S0092-8674(02)00971-6","article-title":"Integrins: Bidirectional, allosteric signaling machines","volume":"110","author":"Hynes","year":"2002","journal-title":"Cell"},{"key":"ref_46","unstructured":"Ahmad, K., Lee, E.J., Shaikh, S., Kumar, A., Rao, K.M., Park, S.Y., Jin, J.O., Han, S.S., and Choi, I. (2019). Targeting integrins for cancer management using nanotherapeutic approaches: Recent advances and challenges. Semin. Cancer Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"D1039","DOI":"10.2741\/A344","article-title":"Integrins during muscle development and in muscular dystrophies","volume":"3","author":"Gullberg","year":"1998","journal-title":"Front. Biosci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.tem.2015.05.006","article-title":"The extracellular matrix and insulin resistance","volume":"26","author":"Williams","year":"2015","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"139","DOI":"10.2174\/138945008783502494","article-title":"Collagen receptor integrins: Rising to the challenge","volume":"9","author":"Zutter","year":"2008","journal-title":"Curr. Drug Targets"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1007\/s00125-007-0591-6","article-title":"Focal adhesion kinase regulates insulin resistance in skeletal muscle","volume":"50","author":"Bisht","year":"2007","journal-title":"Diabetologia"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"4679","DOI":"10.1074\/jbc.M807408200","article-title":"Insulin resistance in striated muscle-specific integrin receptor beta1-deficient mice","volume":"284","author":"Zong","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"502","DOI":"10.2337\/db18-0418","article-title":"ADAMTS9 Regulates Skeletal Muscle Insulin Sensitivity Through Extracellular Matrix Alterations","volume":"68","author":"Graae","year":"2019","journal-title":"Diabetes"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"3251","DOI":"10.2337\/db13-0033","article-title":"Relaxin treatment reverses insulin resistance in mice fed a high-fat diet","volume":"62","author":"Bonner","year":"2013","journal-title":"Diabetes"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.2337\/db12-1502","article-title":"Hyaluronan accumulates with high-fat feeding and contributes to insulin resistance","volume":"62","author":"Kang","year":"2013","journal-title":"Diabetes"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Meakin, P.J., Morrison, V.L., Sneddon, C.C., Savinko, T., Uotila, L., Jalicy, S.M., Gabriel, J.L., Kang, L., Ashford, M.L., and Fagerholm, S.C. (2015). Mice Lacking beta2-Integrin Function Remain Glucose Tolerant in Spite of Insulin Resistance, Neutrophil Infiltration and Inflammation. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0138872"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/nrm1004","article-title":"CD44: From adhesion molecules to signalling regulators","volume":"4","author":"Ponta","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"7049","DOI":"10.1073\/pnas.1114513109","article-title":"Expression-based genome-wide association study links the receptor CD44 in adipose tissue with type 2 diabetes","volume":"109","author":"Kodama","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"E973","DOI":"10.1152\/ajpendo.00215.2019","article-title":"CD44 contributes to hyaluronan-mediated insulin resistance in skeletal muscle of high-fat-fed C57BL\/6 mice","volume":"317","author":"Hasib","year":"2019","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_59","first-page":"845","article-title":"Extracellular matrix and its receptors during development","volume":"39","author":"Gullberg","year":"1995","journal-title":"Int. J. Dev. Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1478-811X-8-3","article-title":"Dystroglycan versatility in cell adhesion: A tale of multiple motifs","volume":"8","author":"Moore","year":"2010","journal-title":"Cell Commun. Signal."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/0092-8674(95)90471-9","article-title":"Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy","volume":"82","author":"Brenman","year":"1995","journal-title":"Cell"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1161\/01.RES.0000126574.61061.25","article-title":"The dystrophin glycoprotein complex: Signaling strength and integrity for the sarcolemma","volume":"94","author":"Lapidos","year":"2004","journal-title":"Circ. Res."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1038\/nrm2289","article-title":"Synergistic control of cell adhesion by integrins and syndecans","volume":"8","author":"Morgan","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1146\/annurev.biochem.68.1.729","article-title":"Functions of cell surface heparan sulfate proteoglycans","volume":"68","author":"Bernfield","year":"1999","journal-title":"Annu. Rev. Biochem."},{"key":"ref_65","first-page":"1","article-title":"Syndecans in skeletal muscle development, regeneration and homeostasis","volume":"2","author":"Pisconti","year":"2012","journal-title":"Muscles Ligaments Tendons J."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1172\/JCI115780","article-title":"Glucose-free fatty acid cycle operates in human heart and skeletal muscle in vivo","volume":"89","author":"Nuutila","year":"1992","journal-title":"J. Clin. Investig."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.2337\/db15-1434","article-title":"Integrin-Linked Kinase in Muscle Is Necessary for the Development of Insulin Resistance in Diet-Induced Obese Mice","volume":"65","author":"Kang","year":"2016","journal-title":"Diabetes"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Grzelkowska-Kowalczyk, K. (2016). The importance of extracellular matrix in skeletal muscle development and function. Composition and Function of the Extracellular Matrix in the Human Body, IntechOpen.","DOI":"10.5772\/62230"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1038\/nm.4350","article-title":"Insulin action and resistance in obesity and type 2 diabetes","volume":"23","author":"Czech","year":"2017","journal-title":"Nat. Med."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.2522\/ptj.20080018","article-title":"Skeletal muscle insulin resistance: Roles of fatty acid metabolism and exercise","volume":"88","author":"Turcotte","year":"2008","journal-title":"Phys. Ther."},{"key":"ref_71","first-page":"D1153","article-title":"ProteomicsDB: A multi-omics and multi-organism resource for life science research","volume":"48","author":"Samaras","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"D607","DOI":"10.1093\/nar\/gky1131","article-title":"STRING v11: Protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets","volume":"47","author":"Szklarczyk","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1093\/nar\/28.1.27","article-title":"KEGG: Kyoto encyclopedia of genes and genomes","volume":"28","author":"Kanehisa","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1096\/fj.06-7022com","article-title":"The binding of Mss4 to \u03b1-integrin subunits regulates matrix metalloproteinase activation and fibronectin remodeling","volume":"21","author":"Knoblauch","year":"2007","journal-title":"FASEB J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1167\/iovs.08-2377","article-title":"Tight glycemic control regulates fibronectin expression and basement membrane thickening in retinal and glomerular capillaries of diabetic rats","volume":"50","author":"Cherian","year":"2009","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.metabol.2016.10.009","article-title":"Skeletal muscle extracellular matrix remodeling after short-term overfeeding in healthy humans","volume":"67","author":"Tam","year":"2017","journal-title":"Metabolism"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1007\/s00125-013-3128-1","article-title":"Matrix metalloproteinase 9 opposes diet-induced muscle insulin resistance in mice","volume":"57","author":"Kang","year":"2014","journal-title":"Diabetologia"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1111\/obr.12548","article-title":"The emerging role of skeletal muscle extracellular matrix remodelling in obesity and exercise","volume":"18","author":"McLennan","year":"2017","journal-title":"Obes. Rev."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"337","DOI":"10.4161\/cam.3.4.9338","article-title":"Role of matrix metalloproteinases in skeletal muscle: Migration, differentiation, regeneration and fibrosis","volume":"3","author":"Chen","year":"2009","journal-title":"Cell Adhes. Migr."},{"key":"ref_80","unstructured":"Schiaffino, S., and Partridge, T. (2008). Skeletal Muscle Repair and Regeneration, Springer Science & Business Media."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1080\/10409230290771483","article-title":"The structure, regulation, and function of human matrix metalloproteinase-13","volume":"37","author":"Leeman","year":"2002","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"C529","DOI":"10.1152\/ajpcell.00051.2013","article-title":"Matrix metalloproteinase 13 is a new contributor to skeletal muscle regeneration and critical for myoblast migration","volume":"305","author":"Lei","year":"2013","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.pmbts.2017.02.005","article-title":"Biochemical and Biological Attributes of Matrix Metalloproteinases","volume":"147","author":"Cui","year":"2017","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.meatsci.2016.04.025","article-title":"The role of matrix metalloproteinases in muscle and adipose tissue development and meat quality: A review","volume":"119","author":"Christensen","year":"2016","journal-title":"Meat Sci."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.semcancer.2010.05.002","article-title":"Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion","volume":"20","author":"Bourboulia","year":"2019","journal-title":"Semin. Cancer Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.yexcr.2007.06.007","article-title":"Tissue inhibitor of metalloproteinase-2 (TIMP-2) regulates myogenesis and \u03b21 integrin expression in vitro","volume":"314","author":"Lluri","year":"2008","journal-title":"Exp. Cell Res."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1152\/physrev.00031.2003","article-title":"Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading","volume":"84","year":"2004","journal-title":"Physiol. Rev."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s00401-004-0941-0","article-title":"Increased mRNA expression of tissue inhibitors of metalloproteinase-1 and -2 in Duchenne muscular dystrophy","volume":"109","author":"Zwirner","year":"2005","journal-title":"Acta Neuropathol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.bcp.2016.05.005","article-title":"Adipose extracellular matrix remodelling in obesity and insulin resistance","volume":"119","author":"Lin","year":"2016","journal-title":"Biochem. Pharmacol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"16146","DOI":"10.1074\/jbc.M610161200","article-title":"Regulation of ADAMTS9 secretion and enzymatic activity by its propeptide","volume":"282","author":"Koo","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1152\/japplphysiol.01160.2006","article-title":"Effects of short-term vibration and hypoxia during high-intensity cycling exercise on circulating levels of angiogenic regulators in humans","volume":"103","author":"Suhr","year":"2007","journal-title":"J. Appl. Physiol."},{"key":"ref_92","first-page":"70","article-title":"Extracellular Matrix, Proteases and Physical Exercise","volume":"2019","author":"Suhr","year":"2019","journal-title":"Ger. J. Sports Med. \/Dtsch. Z. fur Sportmed."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2346","DOI":"10.1152\/japplphysiol.00822.2006","article-title":"A single bout of exercise activates matrix metalloproteinase in human skeletal muscle","volume":"102","author":"Rullman","year":"2007","journal-title":"J. Appl. Physiol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1111\/iep.12237","article-title":"Physical training improves visceral adipose tissue health by remodelling extracellular matrix in rats with estrogen absence: A gene expression analysis","volume":"98","author":"Duarte","year":"2017","journal-title":"Int. J. Exp. Pathol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1080\/17461391.2018.1526974","article-title":"Age-specific response of skeletal muscle extracellular matrix to acute resistance exercise: A pilot study","volume":"19","author":"Wessner","year":"2019","journal-title":"Eur. J. Sport Sci."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/11\/3845\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:33:32Z","timestamp":1760175212000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/11\/3845"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,5,28]]},"references-count":95,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2020,6]]}},"alternative-id":["ijms21113845"],"URL":"https:\/\/doi.org\/10.3390\/ijms21113845","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,5,28]]}}}