{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T09:12:42Z","timestamp":1762161162076},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1984,7,1]]},"abstract":"<jats:p>The occurrence of endogenous substrate proteins for Ca2+-dependent protein kinase, augmented by either phospholipid or calmodulin, and for cyclic AMP-dependent protein kinase was examined in homogenates and subcellular fractions of mouse pancreatic islets. Islet protein phosphorylation was enhanced by Ca2+-calmodulin; the major endogenous substrates in the homogenate were two proteins of Mr 53000 and 100000. The Mr-100000 phosphoprotein was localized to a 27000g-supernatant fraction, whereas the Mr-53000 phosphoprotein was present in a 27000g particulate fraction of mouse islets. In the presence of Ca2+, phosphatidylserine stimulated phosphorylation of 15 proteins, of Mr 17000-190000, in a 27000g-supernatant fraction. No effects of Ca2+ plus phosphatidylserine were observed in a 27000g particulate fraction of mouse islets. Examination of cyclic AMP-dependent protein phosphorylation revealed five substrate proteins, of Mr 23000-72000, present in the 27000g supernatant of mouse islets. No common substrates for either the two Ca2+-dependent phosphorylation systems or for the cyclic AMP-dependent and the Ca2+-calmodulin-dependent phosphorylation systems were noted. On the other hand, the actions of the cyclic AMP-sensitive and the Ca2+-phospholipid-sensitive systems may be overlapping, since two common substrates for them were noted in the 27000g-supernatant fraction. The results are consistent with the hypothesis that protein phosphorylation may play a role in the regulation of insulin secretion by Ca2+ and cyclic AMP. The extensive stimulatory effect of phosphatidylserine furthermore suggests that the Ca2+-phospholipid-sensitive protein kinase may prove to be a prominent phosphorylation system in pancreatic islets.<\/jats:p>","DOI":"10.1042\/bj2210247","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:42:48Z","timestamp":1439239368000},"page":"247-253","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Endogenous substrate proteins for Ca2+-calmodulin-dependent, Ca2+-phospholipid-dependent and cyclic AMP-dependent protein kinases in mouse pancreatic islets"],"prefix":"10.1042","volume":"221","author":[{"given":"P","family":"Thams","sequence":"first","affiliation":[]},{"given":"K","family":"Capito","sequence":"additional","affiliation":[]},{"given":"C J","family":"Hedeskov","sequence":"additional","affiliation":[]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/221\/1\/247\/581851\/bj2210247.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/221\/1\/247\/581851\/bj2210247.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T13:52:03Z","timestamp":1637848323000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/221\/1\/247\/16075\/Endogenous-substrate-proteins-for-Ca2-calmodulin"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1984,7,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1984,7,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2210247","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1984,7,1]]}}}