{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T13:37:50Z","timestamp":1768743470551,"version":"3.49.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1990,5,1]]},"abstract":"<jats:p>The culture of skin fibroblasts in the presence of 0.01% (w\/v) dextran sulphate results in complete proteolytic processing of procollagen to collagen. Processing occurs predominantly via a pN-collagen intermediate, suggesting that C-propeptide cleavage occurs early during the processing pathway. The processed collagen is associated with the cell-layer fraction. This method of inducing procollagen processing was evaluated for use in detecting procollagen processing abnormalities in heritable connective-tissue diseases. Abnormal type I procollagen processing was clearly demonstrated in two cases with known defects of pN-propeptide cleavage. In one, the cleavage deficiency was due to diminished N-proteinase activity (dermatosparaxis) and in the other case (Ehler's-Danlos syndrome type VIIA) the cleavage site was deleted. In a case of osteogenesis imperfecta (type II) the slow electrophoretic migration of type I collagen alpha-chains due to over-modification of lysine was readily demonstrated. Inefficient procollagen processing was also evident in this patient, as had been previously reported [de Wet, Pihlanjaniemi, Myers, Kelly &amp; Prockop (1983) J. Biol. Chem. 258, 7721-7728]. Thus this method of culture in the presence of dextran sulphate provides a simple and rapid procedure for the detection of procollagen processing defects and electrophoretic abnormalities.<\/jats:p>","DOI":"10.1042\/bj2670573","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:15:42Z","timestamp":1439241342000},"page":"573-577","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":44,"title":["Assessment of procollagen processing defects by fibroblasts cultured in the presence of dextran sulphate"],"prefix":"10.1042","volume":"267","author":[{"given":"J F","family":"Bateman","sequence":"first","affiliation":[{"name":"University of Melbourne, Department of Paediatrics, Royal Children's Hospital, Parkville, Vic. 3052, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S B","family":"Golub","sequence":"additional","affiliation":[{"name":"University of Melbourne, Department of Paediatrics, Royal Children's Hospital, Parkville, Vic. 3052, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/267\/3\/573\/599964\/bj2670573.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/267\/3\/573\/599964\/bj2670573.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T19:14:26Z","timestamp":1637867666000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/267\/3\/573\/36609\/Assessment-of-procollagen-processing-defects-by"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,5,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1990,5,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2670573","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,5,1]]}}}