{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T23:12:07Z","timestamp":1790896327675,"version":"4.1.0"},"reference-count":33,"publisher":"American Physiological Society","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[2006,1]]},"abstract":"<jats:p> \u03bc-calpain and calpain-3 are Ca<jats:sup>2+<\/jats:sup>-dependent proteases found in skeletal muscle. Autolysis of calpains is observed using Western blot analysis as the cleaving of the full-length proteins to shorter products. Biochemical assays suggest that \u03bc-calpain becomes proteolytically active in the presence of 2\u2013200 \u03bcM Ca<jats:sup>2+<\/jats:sup>. Although calpain-3 is poorly understood, autolysis is thought to result in its activation, which is widely thought to occur at lower intracellular Ca<jats:sup>2+<\/jats:sup> concentration levels ([Ca<jats:sup>2+<\/jats:sup>]<jats:sub>i<\/jats:sub>; \u223c1 \u03bcM) than the levels at which \u03bc-calpain activation occurs. We have demonstrated the Ca<jats:sup>2+<\/jats:sup>-dependent autolysis of the calpains in human muscle samples and rat extensor digitorum longus (EDL) muscles homogenized in solutions mimicking the intracellular environment at various [Ca<jats:sup>2+<\/jats:sup>] levels (0, 2.5, 10, and 25 \u03bcM). Autolysis of calpain-3 was found to occur across a [Ca<jats:sup>2+<\/jats:sup>] range similar to that for \u03bc-calpain, and both calpains displayed a seemingly higher Ca<jats:sup>2+<\/jats:sup> sensitivity in human than in rat muscle homogenates, with \u223c15% autolysis observed after 1-min exposure to 2.5 \u03bcM Ca<jats:sup>2+<\/jats:sup> in human muscle and almost none after 1- to 2-min exposure to the same [Ca<jats:sup>2+<\/jats:sup>]<jats:sub>i<\/jats:sub> level in rat muscle. During muscle activity, [Ca<jats:sup>2+<\/jats:sup>]<jats:sub>i<\/jats:sub> may transiently peak in the range found to autolyze \u03bc-calpain and calpain-3, so we examined the effect of two types of exhaustive cycling exercise (30-s \u201call-out\u201d cycling, n = 8; and 70% V\u0307o<jats:sub>2 peak<\/jats:sub> until fatigue, n = 3) on the amount of autolyzed \u03bc-calpain or calpain-3 in human muscle. No significant autolysis of \u03bc-calpain or calpain-3 occurred as a result of the exercise. These findings have shown that the time- and concentration-dependent changes in [Ca<jats:sup>2+<\/jats:sup>]<jats:sub>i<\/jats:sub> that occurred during concentric exercise fall near but below the level necessary to cause autolysis of calpains in vivo. <\/jats:p>","DOI":"10.1152\/ajpcell.00291.2005","type":"journal-article","created":{"date-parts":[[2005,8,18]],"date-time":"2005-08-18T00:24:57Z","timestamp":1124324697000},"page":"C116-C122","source":"Crossref","is-referenced-by-count":54,"title":["\u03bc-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans"],"prefix":"10.1152","volume":"290","author":[{"given":"Robyn M.","family":"Murphy","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rodney J.","family":"Snow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Graham D.","family":"Lamb","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"24","reference":[{"key":"R1","doi-asserted-by":"crossref","unstructured":"Allen DG. 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