{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T10:53:59Z","timestamp":1761216839997},"reference-count":57,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2004,10,8]],"date-time":"2004-10-08T00:00:00Z","timestamp":1097193600000},"content-version":"vor","delay-in-days":6674,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Annals of Neurology"],"published-print":{"date-parts":[[1986,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Human muscle sarcoplasmic reticulum (SR) yields three major protein bands. The percent distribution of the mean values of the bands from 15 normal human muscles was 55.4, 14.6, and 30.0 for the 100, 55, and 45\u2010kDa mass proteins, respectively. A mean distribution similar to that in normal muscle SR was found in preparations from 7 patients with polymyositis and from 7 patients with myotonic dystrophy. In 12 preparations from patients with Duchenne dystrophy, the protein distribution differed from that of preparations from normal muscle. The 100\u2010kDa mass protein band was decreased, whereas the 55\u2010 and 45\u2010kDa mass bands were increased. Protease inhibitors pepstatin A, antipain, and leupeptin, as well as ethyleneglycol\u2010<jats:italic>bis<\/jats:italic>(aminoethyl ether)\u2010N,N,N\u2032,N\u2032\u2010tetraacetic acid or ethylenediaminetetraacetic acid, significantly reduced this change. However, some of the changes cannot be prevented by the addition of inhibitors and must be expressed in vivo. Neither protease inhibitors nor chelators affected SR preparations from normal muscle. We found a five\u2010 to ten\u2010fold increase in calcium\u2010activated neutral protease activity in Duchenne dystrophic muscles that degraded the calcium\u2010adenosinetriphosphatase of SR. The active protease was identified as the cytoplasmic calpain II. The increased activity in Duchenne muscles may explain many reported abnormalities.<\/jats:p>","DOI":"10.1002\/ana.410200109","type":"journal-article","created":{"date-parts":[[2005,1,1]],"date-time":"2005-01-01T17:32:11Z","timestamp":1104600731000},"page":"50-56","source":"Crossref","is-referenced-by-count":23,"title":["Membrane defects in duchenne dystrophy: Protease affecting sarcoplasmic reticulum"],"prefix":"10.1002","volume":"20","author":[{"given":"B\u00e9la","family":"Nagy","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Frederick J.","family":"Samaha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,10,8]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1002\/mus.880030102"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1113\/jphysiol.1961.sp006771"},{"key":"e_1_2_1_4_2","doi-asserted-by":"crossref","first-page":"11267","DOI":"10.1016\/S0021-9258(17)44413-9","article-title":"Staining of the Ca2+\u2010binding proteins, calsequestrin, calmodulin, troponin C, and S\u2010100 with the cationic carbocyanine dye \u201cStains\u2010All.\u201d","volume":"258","author":"Campbell KP","year":"1983","journal-title":"J Biol Chem"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1093\/brain\/102.1.147"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-510X(84)90084-4"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00261a019"},{"key":"e_1_2_1_8_2","first-page":"103","article-title":"High creatine phosphokinase activity of sera of progressive muscular dystrophy","volume":"46","author":"Ebashi S","year":"1959","journal-title":"J Biochem"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/214843a0"},{"key":"e_1_2_1_10_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.ph.44.030182.001501"},{"key":"e_1_2_1_11_2","doi-asserted-by":"crossref","first-page":"7835","DOI":"10.1016\/S0021-9258(19)44598-5","article-title":"Interaction of divalent cations with the 55,000 dalton protein component of the sarcoplasmic reticulum","volume":"247","author":"Ikemoto N","year":"1972","journal-title":"J Biol Chem"},{"key":"e_1_2_1_12_2","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1016\/S0021-9258(19)42738-5","article-title":"Studies on a metal binding protein of the sarcoplasmic reticulum","volume":"249","author":"Ikemoto N","year":"1974","journal-title":"J Biol Chem"},{"key":"e_1_2_1_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(71)90415-2"},{"key":"e_1_2_1_14_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a132558"},{"key":"e_1_2_1_15_2","doi-asserted-by":"publisher","DOI":"10.1038\/279344a0"},{"key":"e_1_2_1_16_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a135018"},{"key":"e_1_2_1_17_2","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the pholin phenol reagent","volume":"193","author":"Lowry OH","year":"1951","journal-title":"J Biol Chem"},{"key":"e_1_2_1_18_2","doi-asserted-by":"crossref","first-page":"4508","DOI":"10.1016\/S0021-9258(19)63820-2","article-title":"Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum","volume":"245","author":"MacLennan DH","year":"1970","journal-title":"J Biol Chem"},{"key":"e_1_2_1_19_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.68.6.1231"},{"key":"e_1_2_1_20_2","doi-asserted-by":"publisher","DOI":"10.3181\/00379727-127-32813"},{"key":"e_1_2_1_21_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(80)81326-3"},{"key":"e_1_2_1_22_2","doi-asserted-by":"crossref","first-page":"7203","DOI":"10.1016\/S0021-9258(18)34557-5","article-title":"Rabbit skeletal muscle calcium\u2010dependent protease requiring millimolar Ca2+","volume":"257","author":"Mellgren RL","year":"1982","journal-title":"J Biol Chem"},{"key":"e_1_2_1_23_2","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1515\/znc-1973-3-414","article-title":"Tryptic fragmentation of the calcium transport system in the sarcoplasmic reticulum","volume":"28","author":"Migala A","year":"1973","journal-title":"Z Naturforsch [C]"},{"key":"e_1_2_1_24_2","doi-asserted-by":"publisher","DOI":"10.1212\/WNL.25.12.1111"},{"key":"e_1_2_1_25_2","doi-asserted-by":"publisher","DOI":"10.1016\/0968-0004(83)90165-2"},{"key":"e_1_2_1_26_2","first-page":"407","volume-title":"Advances in Enzyme Regulation","author":"Murachi T","year":"1981"},{"key":"e_1_2_1_27_2","first-page":"166a","article-title":"Comparison of tryptic fragments of rabbit and human muscle sarcoplasmic reticulum. A model for dystrophic muscle sarcoplasmic reticulum","volume":"41","author":"Nagy B","year":"1983","journal-title":"Biophys J"},{"key":"e_1_2_1_28_2","first-page":"145","article-title":"Increased protease activity in Duchenne dystrophic muscles decreases Ca2+ ATPase in sarcoplasmic reticulum preparations","volume":"16","author":"Nagy B","year":"1984","journal-title":"Ann Neurol"},{"key":"e_1_2_1_29_2","first-page":"401","article-title":"Biochemical studies on normal and diseased human muscle sarcoplasmic reticulum: increased protease effects in muscle diseases","volume":"16","author":"Nagy B","year":"1984","journal-title":"Ann Neurol"},{"key":"e_1_2_1_30_2","first-page":"828","article-title":"Duchenne dystrophic muscles possess increased protease activity affecting the calcium\u2010adenosine triphosphatase of sarcoplasmic reticulum","volume":"12","author":"Nagy B","year":"1984","journal-title":"IRCS Med Sci"},{"key":"e_1_2_1_31_2","first-page":"643","article-title":"Identity of calcium\u2010activated neutral proteases from rabbit cardiac and skeletal muscle","volume":"79","author":"Ohsumi M","year":"1984","journal-title":"Comp Biochem Physiol [C]"},{"key":"e_1_2_1_32_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00637a017"},{"key":"e_1_2_1_33_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(81)91619-3"},{"key":"e_1_2_1_34_2","doi-asserted-by":"publisher","DOI":"10.1042\/bst0080690"},{"key":"e_1_2_1_35_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.81.1.53"},{"key":"e_1_2_1_36_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.81.21.6714"},{"key":"e_1_2_1_37_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-2944(69)90040-4"},{"key":"e_1_2_1_38_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2090635"},{"key":"e_1_2_1_39_2","doi-asserted-by":"publisher","DOI":"10.1002\/mus.880030103"},{"key":"e_1_2_1_40_2","doi-asserted-by":"publisher","DOI":"10.1212\/WNL.31.7.916"},{"key":"e_1_2_1_41_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM196901232800403"},{"key":"e_1_2_1_42_2","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1152\/ajplegacy.1962.202.5.815","article-title":"Effects of activity on contractions of normal and dystrophic mouse muscles","volume":"202","author":"Sandow A","year":"1962","journal-title":"Am J Physiol"},{"key":"e_1_2_1_43_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2736(77)90271-1"},{"key":"e_1_2_1_44_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00687539"},{"key":"e_1_2_1_45_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.860127"},{"key":"e_1_2_1_46_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00687741"},{"key":"e_1_2_1_47_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(73)90098-5"},{"key":"e_1_2_1_48_2","first-page":"303","article-title":"Aldolase in the serum and tissues of tumor bearing animals","volume":"9","author":"Sibley JA","year":"1949","journal-title":"J Natl Cancer Inst"},{"key":"e_1_2_1_49_2","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/S0021-9258(18)57031-9","article-title":"Determination of aldolase in animal tissues","volume":"177","author":"Sibley JA","year":"1949","journal-title":"J Biol Chem"},{"key":"e_1_2_1_50_2","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1016\/S0021-9258(17)33841-3","article-title":"Isolation and characterization of tryptic fragments of adenosine triphosphatase of sarcoplasmic reticulum","volume":"251","author":"Stewart PS","year":"1976","journal-title":"J Biol Chem"},{"key":"e_1_2_1_51_2","doi-asserted-by":"publisher","DOI":"10.1002\/mus.880030410"},{"key":"e_1_2_1_52_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a133656"},{"key":"e_1_2_1_53_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a133455"},{"key":"e_1_2_1_54_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.178.4063.871"},{"key":"e_1_2_1_55_2","doi-asserted-by":"crossref","first-page":"4406","DOI":"10.1016\/S0021-9258(18)94333-4","article-title":"The reliability of molecular weight determination of dodecyl sulfate\u2010polyacrylamide gel electrophoresis","volume":"244","author":"Weber K","year":"1969","journal-title":"J Biol Chem"},{"key":"e_1_2_1_56_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-87966-1_60"},{"key":"e_1_2_1_57_2","doi-asserted-by":"publisher","DOI":"10.1212\/WNL.28.5.447"},{"key":"e_1_2_1_58_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(84)80173-4"}],"container-title":["Annals of Neurology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fana.410200109","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/ana.410200109","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,21]],"date-time":"2023-10-21T10:20:22Z","timestamp":1697883622000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/ana.410200109"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1986,7]]},"references-count":57,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1986,7]]}},"alternative-id":["10.1002\/ana.410200109"],"URL":"https:\/\/doi.org\/10.1002\/ana.410200109","archive":["Portico"],"relation":{},"ISSN":["0364-5134","1531-8249"],"issn-type":[{"value":"0364-5134","type":"print"},{"value":"1531-8249","type":"electronic"}],"subject":[],"published":{"date-parts":[[1986,7]]}}}