{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T09:53:22Z","timestamp":1792058002569,"version":"4.4.0"},"reference-count":93,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2005,5,1]],"date-time":"2005-05-01T00:00:00Z","timestamp":1114905600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2005,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Collagen XVIII is a component of basement membranes (BMs) with the structural properties of both a collagen and a proteoglycan. Proteolytic cleavage within its C\u2010terminal domain releases a fragment, endostatin, which has been reported to have anti\u2010angiogenesis effects. Molecular studies demonstrated binding of the endostatin domain to heparan sulfate and to BM components like laminin and perlecan, but the functional role of these interactions in vivo remains unknown. Insights into the physiological function of collagen XVIII\/endostatin have recently been obtained through the identification of inactivating mutations in the human collagen XVIII\/endostatin gene (\n                    <jats:italic>COL18A1<\/jats:italic>\n                    ) in patients with Knobloch syndrome, characterized by age\u2010dependent vitreoretinal degeneration and occipital encephalocele. That collagen XVIII\/endostatin has an essential role in ocular development and the maintenance of visual function is further demonstrated by the ocular abnormalities seen in mice lacking collagen XVIII\/endostatin. Age\u2010dependent loss of vision in these mutant mice is associated with pathological accumulation of deposits under the retinal pigment epithelium, as seen in early stages of age\u2010related macular degeneration in humans. In addition, recent evidence suggests that lack of collagen XVIII\/endostatin predisposes to hydrocephalus formation. These recent findings demonstrate an important role for collagen XVIII\/endostatin in cell\u2010matrix interactions in certain tissues that may be compensated for in other tissues expressing this collagen.\u2014Marneros, A. G., Olsen, B. R. Physiological role of collagen XVIII and endostatin.\n                    <jats:italic>FASEB J<\/jats:italic>\n                    . 19, 716\u2013728 (2005)\n                  <\/jats:p>","DOI":"10.1096\/fj.04-2134rev","type":"journal-article","created":{"date-parts":[[2005,4,27]],"date-time":"2005-04-27T16:10:37Z","timestamp":1114618237000},"page":"716-728","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":211,"title":["Physiological role of collagen XVIII and endostatin"],"prefix":"10.1096","volume":"19","author":[{"given":"Alexander G.","family":"Marneros","sequence":"first","affiliation":[{"name":"Department of Cell Biology Harvard Medical School  Boston Massachusetts USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bjorn R.","family":"Olsen","sequence":"additional","affiliation":[{"name":"Department of Cell Biology Harvard Medical School  Boston Massachusetts USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,5]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.matbio.2003.10.006"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.19.8763"},{"key":"e_1_2_11_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/21.7.1535"},{"key":"e_1_2_11_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.10.4234"},{"key":"e_1_2_11_6_1","doi-asserted-by":"crossref","first-page":"13929","DOI":"10.1016\/S0021-9258(17)36737-6","article-title":"Primary structure of the \u03b11 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the \u03b11 (XVIII) chain with its homologue, the \u03b11 (XV) collagen chain","volume":"269","author":"Rehn M.","year":"1994","journal-title":"J. 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