{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,22]],"date-time":"2026-01-22T12:19:46Z","timestamp":1769084386426,"version":"3.49.0"},"reference-count":32,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2001,6,1]],"date-time":"2001-06-01T00:00:00Z","timestamp":991353600000},"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":[[2001,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>RNA and type I collagen were analyzed from cultured skin fibroblasts of a Beagle puppy with fractures consistent with type III osteogenesis imperfecta (OI). In a nonisotopic RNAse cleavage assay (NIRCA), the proband's RNA had a unique cleavage pattern in the region of COL1A2 encoding the C-propeptide. DNA sequence analyses identified a mutation in which nucleotides 3991-3994 (\u201cCTAG\u201d) were replaced with \u201cTGTCATTGG.\u201d The first seven bases of the inserted sequence were identical to nucleotides 4002-4008 of the normal canine COL1A2 sequence. The resulting frameshift changed 30 amino acids and introduced a premature stop codon. Reverse-transcription polymerase chain reaction (RT-PCR) with primers flanking the mutation site amplified two complementary DNA (cDNA) fragments for the proband and a single product for the control. Restriction enzyme digestions also were consistent with a heterozygous mutation in the proband. Type I procollagen labeled with [3H]proline was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Increased density of pC-\u03b12(I) suggested comigration with the similarly sized pro-\u03b12(I) derived from the mutant allele. Furthermore, \u03b1-chains were overhydroxylated and the ratio of \u03b11(I):\u03b12(I) was 3.2:1, consistent with the presence of \u03b11(I) homotrimers. Analyses of COL1A2 and type I collagen were both consistent with the described heterozygous mutation affecting the pro-\u03b12(I) C-propeptide and confirmed a diagnosis of OI.<\/jats:p>","DOI":"10.1359\/jbmr.2001.16.6.1147","type":"journal-article","created":{"date-parts":[[2006,4,27]],"date-time":"2006-04-27T04:23:56Z","timestamp":1146111836000},"page":"1147-1153","source":"Crossref","is-referenced-by-count":35,"title":["Canine COL1A2 Mutation Resulting in C-Terminal Truncation of Pro-\u03b12(I) and Severe Osteogenesis Imperfecta"],"prefix":"10.1093","volume":"16","author":[{"given":"Bonnie G.","family":"Campbell","sequence":"first","affiliation":[{"name":"Present address: Department of Veterinary Clinical Sciences, College of Veterinary Medicine, Washington State University, Pullman, Washington, USA"},{"name":"Department of Biomedical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joyce A. 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Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, New York, USA"},{"name":"Department of Biomedical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ronald R.","family":"Minor","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2009,12,2]]},"reference":[{"key":"2024020714130337100_bib1","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1093\/nar\/25.1.181","article-title":"The human type I collagen mutation database","volume":"25","author":"Dalgleish","year":"1997","journal-title":"Nucleic Acids Res"},{"key":"2024020714130337100_bib2","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1093\/nar\/26.1.253","article-title":"The human collagen mutation database 1998","volume":"26","author":"Dalgleish","year":"1998","journal-title":"Nucleic Acids Res"},{"key":"2024020714130337100_bib3","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/S0934-8832(11)80077-6","article-title":"Self-assembly into fibrils of a homotrimer of type I collagen","volume":"12","author":"McBride","year":"1992","journal-title":"Matrix"},{"key":"2024020714130337100_bib4","doi-asserted-by":"crossref","first-page":"10960","DOI":"10.1016\/S0021-9258(18)60412-0","article-title":"A frameshift mutation results in a truncated nonfunctional carboxyl-terminal pro alpha 1(I) propeptide of type I collagen in osteogenesis imperfecta","volume":"264","author":"Bateman","year":"1989","journal-title":"J Biol Chem"},{"key":"2024020714130337100_bib5","doi-asserted-by":"crossref","first-page":"18218","DOI":"10.1016\/S0021-9258(17)46833-5","article-title":"Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta","volume":"268","author":"Chessler","year":"1993","journal-title":"J Biol Chem"},{"key":"2024020714130337100_bib6","doi-asserted-by":"crossref","first-page":"15192","DOI":"10.1016\/S0021-9258(17)43792-6","article-title":"The molecular defect in a nonlethal variant of osteogenesis imperfecta. 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