{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T11:09:03Z","timestamp":1790507343853,"version":"4.1.0"},"reference-count":48,"publisher":"Oxford University Press (OUP)","issue":"7","license":[{"start":{"date-parts":[[1992,7,1]],"date-time":"1992-07-01T00:00:00Z","timestamp":709948800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["AM-38370"],"award-info":[{"award-number":["AM-38370"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["AR-39870"],"award-info":[{"award-number":["AR-39870"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["AR-40926"],"award-info":[{"award-number":["AR-40926"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["AR-30426"],"award-info":[{"award-number":["AR-30426"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"name":"March of Dimes, the Saint Vincent Hospital Research Council"},{"name":"Northeast Osteogenesis Imperfecta Foundation"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1992,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>This study compares the synthesis of mutant type I collagen in cultured dermal fibroblasts and trabecular osteoblasts that were isolated from a patient with moderately severe osteogenesis imperfecta (type IV). Previous study of this patient's dermal fibroblasts revealed a 2000 dalton deletion located in cyanogen bromide peptide 4 of \u03b12(D-collagen. The phenotype of the bone cell cultures was defined by a 3\u20134 day logarithmic phase doubling time, predominantly type I collagen production over type III and alkaline phosphatase activity 13.5 times dermal fibroblast levels. The current study revealed that both fibroblasts and osteoblasts synthesized a normal and a shortened \u03b12(I) chain, each as the product of separate alleles. Following pepsin treatment of the procollagens, a shortened \u03b11(I) chain was also seen in both cell types. Cyanogen bromide peptide mapping of osteoblast \u03b1-chains demonstrated the same deletions in the cyanogen bromide peptide 4 as observed in the fibroblast cyanogen bromide maps. PAGE analysis of oligonucleotide-specific cDNA that was reverse transcribed from RNA isolated from fibroblasts and osteoblasts also demonstrated the presence of two bands, one the normal size of \u03b12(I) cDNA and a second species that was smaller by 54 base pairs. Sequencing of polymerase chain reaction-amplified cDNA fragments revealed an in-frame deletion of exon 12. This finding was confirmed by the RNase protection method. Genomic DNA sequencing detected a T\u2192G point mutation in the second position of the 5\u2032 splice donor site of intron 12. Therefore, in this patient with osteogenesis imperfecta there was no qualitative alteration in the osteoblast-specific expression of this mutant \u03b12(I)-collagen allele compared to dermal fibroblasts.<\/jats:p>","DOI":"10.1002\/jbmr.5650070709","type":"journal-article","created":{"date-parts":[[2010,2,3]],"date-time":"2010-02-03T17:08:31Z","timestamp":1265216911000},"page":"793-805","source":"Crossref","is-referenced-by-count":10,"title":["Expression of mutant \u03b1(I)-procollagen in osteoblast and fibroblast cultures from a proband with osteogenesis imperfecta type IV"],"prefix":"10.1093","volume":"7","author":[{"given":"Stewart D.","family":"Chipman","sequence":"first","affiliation":[{"name":"Bone Metabolism Research Laboratory, Division of Geriatric Medicine and Gerontology, Johns Hopkins University School of Medicine, Baltimore, Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jay R.","family":"Shapiro","sequence":"additional","affiliation":[{"name":"Bone Metabolism Research Laboratory, Division of Geriatric Medicine and Gerontology, Johns Hopkins University School of Medicine, Baltimore, Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monique B.","family":"McKinstry","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, University of Connecticut Health Science Center, Farmington"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mary Louise","family":"Stover","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, University of Connecticut Health Science Center, Farmington"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip","family":"Branson","sequence":"additional","affiliation":[{"name":"Department of Orthopedic Surgery, Princeton Hospital, Princeton, West Virginia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David W.","family":"Rowe","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, University of Connecticut Health Science Center, Farmington"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[1992,7,1]]},"reference":[{"key":"2024013113110470300_bib1","first-page":"49","volume-title":"Collagen, Vol. 5, Pathobiochemistry","author":"Shapiro","year":"1992"},{"key":"2024013113110470300_bib2","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1136\/jmg.16.2.101","article-title":"Genetic heterogeneity in osteogenesis imperfecta","volume":"16","author":"Sillence","year":"1979","journal-title":"J Med Genet"},{"key":"2024013113110470300_bib3","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/0168-9525(90)90235-X","article-title":"Brittle bones \u2014 fragile molecules: Disorders of collagen gene structure and expression","volume":"6","author":"Byers","year":"1990","journal-title":"Trends Genet"},{"key":"2024013113110470300_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1749-6632.1988.tb55311.x","article-title":"Osteogenesis imperfecta nosology and genetics","volume":"543","author":"Sillence","year":"1989","journal-title":"Ann NY Acad Sci"},{"key":"2024013113110470300_bib5","first-page":"197","article-title":"A cysteine for glycine substitution at position 1017 in an \u03b11(I) chain of type I collagen in a patient with mild dominantly inherited osteogenesis imperfecta","volume":"5","author":"Labhard","year":"1988","journal-title":"Mol Biol Med"},{"key":"2024013113110470300_bib6","doi-asserted-by":"crossref","first-page":"8398","DOI":"10.1016\/S0021-9258(18)68491-1","article-title":"Heterozygosity for a large deletion in the \u03b12(I) collagen gene has a dramatic effect on type I collagen secretion and produces perinatal lethal osteogenesis imperfecta","volume":"263","author":"Willing","year":"1988","journal-title":"J Biol Chem"},{"key":"2024013113110470300_bib7","doi-asserted-by":"crossref","first-page":"3002","DOI":"10.1016\/S0021-9258(19)81713-1","article-title":"A single base mutation that converts glycine 907 of the \u03b12(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. 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