{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T04:25:46Z","timestamp":1790483146493,"version":"4.1.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2003,10,1]]},"abstract":"<jats:p>Endostatin is a naturally occurring proteolytic fragment of the C-terminal domain of collagen XVIII. It inhibits angiogenesis by a mechanism that appears to involve binding to HS (heparan sulphate). We have examined the molecular interaction between endostatin and HS from micro- and macrovessel endothelial cells. Two discrete panels of oligosaccharides were prepared from metabolically radiolabelled HS, using digestion with either heparinase I or III, and then examined for their endostatin affinity using a sensitive filter-binding assay. Two types of endostatin-binding regions were identified: one comprising sulphated domains of five or more disaccharides in length, enriched in 6-O-sulphate groups, and the other contained long heparinase I-resistant fragments. In the latter case, evidence from the present study suggests that the binding region encompasses a sulphated domain fragment and a transition zone of intermediate sulphation. The contribution to binding of specific O-sulphate groups was determined using selectively desulphated HS species, namely HS from Hs2st\u2212\/\u2212 mutant cells, and by comparing the compositions of endostatin-binding and non-binding oligosaccharides. The results indicate that 6-O-sulphates play a dominant role in site selectivity and 2-O-sulphates are not strictly essential.<\/jats:p>","DOI":"10.1042\/bj20030730","type":"journal-article","created":{"date-parts":[[2003,10,6]],"date-time":"2003-10-06T09:02:13Z","timestamp":1065430933000},"page":"131-139","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":37,"title":["Binding of endostatin to endothelial heparan sulphate shows a differential requirement for specific sulphates"],"prefix":"10.1042","volume":"375","author":[{"given":"Fiona H.","family":"BLACKHALL","sequence":"first","affiliation":[{"name":"Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie Hospital NHS Trust, Manchester M20 4BX, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine L. R.","family":"MERRY","sequence":"additional","affiliation":[{"name":"Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie Hospital NHS Trust, Manchester M20 4BX, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Malcolm","family":"LYON","sequence":"additional","affiliation":[{"name":"Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie Hospital NHS Trust, Manchester M20 4BX, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gordon C.","family":"JAYSON","sequence":"additional","affiliation":[{"name":"Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie Hospital NHS Trust, Manchester M20 4BX, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Judah","family":"FOLKMAN","sequence":"additional","affiliation":[{"name":"Department of Surgery, Children's Hospital, Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kashi","family":"JAVAHERIAN","sequence":"additional","affiliation":[{"name":"Department of Surgery, Children's Hospital, Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John T.","family":"GALLAGHER","sequence":"additional","affiliation":[{"name":"Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie Hospital NHS Trust, Manchester M20 4BX, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/375\/1\/131\/711532\/bj3750131.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/375\/1\/131\/711532\/bj3750131.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T12:08:36Z","timestamp":1637582916000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/375\/1\/131\/40061\/Binding-of-endostatin-to-endothelial-heparan"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,10,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2003,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20030730","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,10,1]]}}}