{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T02:29:52Z","timestamp":1788834592825,"version":"build-2803163510"},"reference-count":168,"publisher":"Wiley","issue":"23-24","license":[{"start":{"date-parts":[[2022,8,8]],"date-time":"2022-08-08T00:00:00Z","timestamp":1659916800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001602","name":"Science Foundation Ireland","doi-asserted-by":"publisher","award":["SFI\u201112\/RI\/2346\/3"],"award-info":[{"award-number":["SFI\u201112\/RI\/2346\/3"]}],"id":[{"id":"10.13039\/501100001602","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteomics"],"published-print":{"date-parts":[[2022,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The X\u2010linked inherited neuromuscular disorder Duchenne muscular dystrophy is characterised by primary abnormalities in the membrane cytoskeletal component dystrophin. The almost complete absence of the Dp427\u2010M isoform of dystrophin in skeletal muscles renders contractile fibres more susceptible to progressive degeneration and a leaky sarcolemma membrane. This in turn results in abnormal calcium homeostasis, enhanced proteolysis and impaired excitation\u2013contraction coupling. Biochemical and mass spectrometry\u2010based proteomic studies of both patient biopsy specimens and genetic animal models of dystrophinopathy have demonstrated significant changes in the concentration and\/or physiological function of essential calcium\u2010regulatory proteins in dystrophin\u2010lacking voluntary muscles. Abnormalities include dystrophinopathy\u2010associated changes in voltage sensing receptors, calcium release channels, calcium pumps and calcium binding proteins. This review article provides an overview of the importance of the sarcolemmal dystrophin\u2010glycoprotein complex and the wider dystrophin complexome in skeletal muscle and its linkage to depolarisation\u2010induced calcium\u2010release mechanisms and the excitation\u2013contraction\u2013relaxation cycle. Besides chronic inflammation, fat substitution and reactive myofibrosis, a major pathobiochemical hallmark of X\u2010linked muscular dystrophy is represented by the chronic influx of calcium ions through the damaged plasmalemma in conjunction with abnormal intracellular calcium fluxes and buffering. Impaired calcium handling proteins should therefore be included in an improved biomarker signature of Duchenne muscular dystrophy.<\/jats:p>","DOI":"10.1002\/pmic.202200003","type":"journal-article","created":{"date-parts":[[2022,7,28]],"date-time":"2022-07-28T22:08:44Z","timestamp":1659046124000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Proteomic profiling of impaired excitation\u2013contraction coupling and abnormal calcium handling in muscular dystrophy"],"prefix":"10.1002","volume":"22","author":[{"given":"Paul","family":"Dowling","sequence":"first","affiliation":[{"name":"Department of Biology, Maynooth University National University of Ireland  Maynooth, Co. Kildare Ireland"},{"name":"Kathleen Lonsdale Institute for Human Health Research Maynooth University  Maynooth, Co. 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