{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T05:54:57Z","timestamp":1779342897764,"version":"3.51.4"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1991,10,1]]},"abstract":"<jats:p>The aim of the work was to identify and characterize the cysteine proteinases of bone tissue, as these enzymes appear necessary for bone resorption. Three cysteine-dependent proteolytic activities were separated from a homogenate of mouse calvaria by a fractionation procedure involving (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography. The first two are typical cathepsins B and L with respect to (1) their reactivity with anti-(cathepsin B) and anti-(cathepsin L) antibodies respectively, (2) their relative rate constants for inhibition by benzyloxycarbonyl-Phe-Phe-CHN2 and L-3-carboxy-trans-2,3-epoxypropionyl-L-leucylamido-(4-guanid ino)butane and (3) their enzymic properties, such as the higher activities of cathepsin L against collagen and gelatin as compared with cathepsin B, and the fact that benzyloxycarbonyl-Arg-Arg 4-methoxy-2-naphthylamide is hydrolysed only by cathepsin B. Cathepsin L was mainly recovered in its precursor form, as indicated by its apparent 40 kDa molecular mass and its relative stability at pH 7.2. The third enzyme is a cathepsin L-like proteinase with an apparent molecular mass of 70 kDa. It is immunoprecipitated by anti-(cathepsin L) antibodies, and appears as the 25 kDa band of mature cathepsin L in Western blots. It further resembles (pro)cathepsin L with regard to its activities against synthetic substrates and proteins such as collagen, and with regard to its response to various inhibitors. However, unlike (pro)cathepsin L, it is eluted as a 70 kDa protein on gel filtration (even in the presence of 1% Brij or 1 M-NaCl), it is stable at pH values as high as 9, and it exhibits stronger affinity for phenyl-Sepharose. It might thus result from a strong complex between mature cathepsin L and another entity that confers stability at alkaline pH and favours hydrophobic interactions. This 70 kDa activity was also detected in mouse muscle and long bones of Ca(2+)-deficient chicks but not in mouse liver, spleen or kidney.<\/jats:p>","DOI":"10.1042\/bj2790167","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:23:44Z","timestamp":1439241824000},"page":"167-174","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":108,"title":["Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase"],"prefix":"10.1042","volume":"279","author":[{"given":"J M","family":"Delaiss\u00e9","sequence":"first","affiliation":[{"name":"Laboratoire de Chimie Physiologique (Connective Tissue Group), Universit\u00e9 de Louvain and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Bruxelles, Belgium."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P","family":"Ledent","sequence":"additional","affiliation":[{"name":"Laboratoire de Chimie Physiologique (Connective Tissue Group), Universit\u00e9 de Louvain and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Bruxelles, Belgium."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G","family":"Vaes","sequence":"additional","affiliation":[{"name":"Laboratoire de Chimie Physiologique (Connective Tissue Group), Universit\u00e9 de Louvain and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Bruxelles, Belgium."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/279\/1\/167\/604658\/bj2790167.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/279\/1\/167\/604658\/bj2790167.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T01:00:46Z","timestamp":1637715646000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/279\/1\/167\/37191\/Collagenolytic-cysteine-proteinases-of-bone-tissue"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1991,10,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1991,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2790167","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1991,10,1]]}}}