{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T09:35:32Z","timestamp":1790847332730,"version":"4.1.0"},"reference-count":57,"publisher":"Oxford University Press (OUP)","issue":"7","license":[{"start":{"date-parts":[[1995,7,1]],"date-time":"1995-07-01T00:00:00Z","timestamp":804556800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1995,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>In previous work, we compared the steady-state levels of specific matrix components in human bone cells derived from patients with osteogenesis imperfecta (OI) to those of age-matched controls. A remarkable finding was the observation that there was a reduction not only in the total levels of collagen, but also in osteonectin and three proteoglycans (a large chondroitin sulfate proteoglycan, biglycan, and decorin). This pattern was observed in patients with and without detectable collagen defects. More recent analysis of extracellular matrix composition have yielded that, compared with age-matched controls, bone cells from OI patients produced higher steady-state levels of fibronectin and thrombospondin. The percentage of these two proteins incorporated into the cell layer pool was also higher in OI than in age-matched controls. In addition, the steady-state levels of hyaluronan and a heparan sulfate proteoglycan were analyzed in both OI and age-matched controls. Although the total (medium + cell layer) steady-state levels of hyaluronan were reduced by 1\/3, the percentage of the hyaluronan in the cell layer pool of patients with OI increased between 100\u2013250% of age-matched control. Thus the matrix elaborated by human OI bone cells is not only quantitatively different but also qualitatively distinct from that of age-matched controls. Not only have specific bone cell matrix components (collagen, osteonectin, the large chondroitin sulfate proteoglycan, biglycan, and decorin) been found to be present in reduced levels in OI bone cells, but some matrix components (thrombospondin, fibronectin, and hyaluronan) have also been found to be present in elevated levels in the matrix of OI cells. These results suggest that putative mutations in type I collagen (present in OI bone cells) give rise to an altered gene expression of other matrix components.<\/jats:p>","DOI":"10.1002\/jbmr.5650100718","type":"journal-article","created":{"date-parts":[[2010,2,3]],"date-time":"2010-02-03T16:09:42Z","timestamp":1265213382000},"page":"1122-1129","source":"Crossref","is-referenced-by-count":51,"title":["Extracellular matrix stoichiometry in osteoblasts from patients with osteogenesis imperfecta"],"prefix":"10.1093","volume":"10","author":[{"given":"Neal S.","family":"Fedarko","sequence":"first","affiliation":[{"name":"Bone Metabolism Research Laboratory, Division of Geriatric Medicine and Gerontology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland"},{"name":"Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pamela Gehron","family":"Robey","sequence":"additional","affiliation":[{"name":"Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich K.","family":"Vetter","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, Humboldt University of Berlin, Berlin, Germany"},{"name":"Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[1995,7,1]]},"reference":[{"key":"2024013114213794900_bib1","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0079-6603(08)60249-4","article-title":"Collagen genes: Mutations affecting collagen structure and expression","volume":"47","author":"Cole","year":"1992","journal-title":"Prog Nucleic Acid Res Mol Biol"},{"key":"2024013114213794900_bib2","first-page":"A216","article-title":"Two cysteine substitutions in the type I procollagen genes (COLIA1 and COLIA2) that cause lethal osteogenesis imperfecta: The location of glycine substitutions does not in any simple way predict their effects on protein function or phenotype","volume":"47","author":"Fertala","year":"1990","journal-title":"Am J Hum Genet"},{"key":"2024013114213794900_bib3","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1146\/annurev.me.43.020192.001413","article-title":"Osteogenesis imperfecta","volume":"43","author":"Byers","year":"1992","journal-title":"Ann Rev Med"},{"key":"2024013114213794900_bib4","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1097\/00019616-199305000-00003","article-title":"Osteogenesis imperfecta: type I collagen and skeletal formation","volume":"3","author":"Shapiro","year":"1993","journal-title":"Endocrinologist"},{"key":"2024013114213794900_bib5","doi-asserted-by":"crossref","first-page":"2590","DOI":"10.1016\/S0021-9258(18)52286-9","article-title":"The effects of different cysteine for glycine substitutions with \u03b12(I) chains","volume":"266","author":"Wenstrup","year":"1991","journal-title":"J Biol Chem"},{"key":"2024013114213794900_bib6","doi-asserted-by":"crossref","first-page":"1872","DOI":"10.1016\/S0021-9258(18)52374-7","article-title":"A de novo G to T transversion in a pro-\u03b11(I) collagen gene for a moderate case of osteogenesis imperfecta","volume":"266","author":"Valli","year":"1991","journal-title":"J Biol Chem"},{"key":"2024013114213794900_bib7","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1111\/j.1749-6632.1990.tb17985.x","article-title":"Characterization of point mutations in type I collagen by RNA\/RNA hybrid analysis","volume":"580","author":"Marini","year":"1990","journal-title":"Ann NY Acad Sci"},{"key":"2024013114213794900_bib8","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/03008209309061961","article-title":"A cysteine for glycine substitution at position 175 in an \u03b11(I) chain of type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta","volume":"29","author":"Wirtz","year":"1993","journal-title":"Conn Tiss Res"},{"key":"2024013114213794900_bib9","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1136\/jmg.30.6.492","article-title":"Osteogenesis imperfecta type III: mutations in the type I collagen structural genes, COLIA1 and COLIA2, are not necessarily responsible","volume":"30","author":"Wallis","year":"1993","journal-title":"J Med Genet"},{"key":"2024013114213794900_bib10","doi-asserted-by":"crossref","first-page":"25162","DOI":"10.1016\/S0021-9258(19)74583-9","article-title":"Two additional cases of osteogenesis imperfecta with substitutions for glycine in the alpha 2(I) collagen chain. 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