{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,10]],"date-time":"2025-09-10T22:03:47Z","timestamp":1757541827628},"reference-count":44,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":5148,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Motil. Cytoskeleton"],"published-print":{"date-parts":[[1991,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>In this study radioimmunoassay, immunohistochemistry, Northern blot analysis, and a gel overlay technique have been used to examine the level, subcellular distribution, and potential target proteins of the S100 family of calcium\u2010modulated proteins in adult and developing rat skeletal muscles. Adult rat muscles contained high levels of S100 proteins but the particular form present was dependent on the muscle type: cardiac muscle contained exclusively S100\u03b1, slow\u2010twitch skeletal muscle fibers contained predominantly S100\u03b1, vascular smooth muscle contained both S100\u03b1 and S100\u03b2, and fast\u2010twitch skeletal muscle fibers contained low but detectable levels of S100\u03b1 and S100\u03b2. While the distribution of S100 mRNAs paralled the protein distribution in all muscles there was no direct correlation between the mRNA and protein levels in different muscle types, suggesting that S100 protein expression is differentially regulated in different muscle types. Immunohistochemical analysis of the cellular distribution of S100 proteins in adult skeletal muscles revealed that S100\u03b1 staining was associated with muscle cells, while S100\u03b2 staining was associated with nonmuscle cells. Radioimmunoassays of developing rat skeletal muscles demonstrated that all developing muscles contained low levels of S100\u03b1 at postnatal day 1 and that as development proceeded the S100\u03b1 levels increased. In contrast to adult muscle, S100\u03b1 expression as confined to fast\u2010twitch fibers in developing skeletal muscle until postnatal day 21. At postnatal day 1, developing contractile elements were S100\u03b1 positive, but no staining periodicity was detectable. At postnatal day 21, S100\u03b1 exhibited the same subcellular localization as seen in the adult: colocalization with the A\u2010band and\/or longitudinal sarcoplasmic reticulum. Comparison of the S100\u03b1\u2010binding protein profiles in fast\u2010 and slow\u2010twitch fibers of various species revealed few, if any, species\u2010 or fiber type\u2010specific S100 binding proteins. Isolated sarcoplasmic reticulum fractions and myo fibrils contained multiple S100\u03b1\u2010hinding proteins. The colocalization of S100\u03b1 and S100\u03b1\u2010binding proteins with the contractile apparatus and sarcoplasmic reticulum suggest that S100\u03b1 may regulate excitation and\/or contraction in slow\u2010twitch fibers.<\/jats:p>","DOI":"10.1002\/cm.970200408","type":"journal-article","created":{"date-parts":[[2005,2,24]],"date-time":"2005-02-24T02:53:05Z","timestamp":1109213585000},"page":"325-337","source":"Crossref","is-referenced-by-count":28,"title":["Examination of the calcium\u2010modulated protein S100\u03b1 and its target proteins in adult and developing skeletal muscle"],"prefix":"10.1002","volume":"20","author":[{"given":"Danna B.","family":"Zimmer","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"5876","DOI":"10.1016\/S0021-9258(18)60647-7","article-title":"Interaction between the microtubule\u2010associated \u03c4 protein and S100\u03b2 regulate \u03c4 phosphorylation by the Ca2+\/calmodulin\u2010dependent protein kinase II","volume":"263","author":"Baudier J.","year":"1988","journal-title":"J. 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