{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T13:24:20Z","timestamp":1776432260328,"version":"3.51.2"},"reference-count":18,"publisher":"BMJ","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Med Genet"],"published-print":{"date-parts":[[1989,6]]},"abstract":"<jats:p>We report a family in which dominant osteogenesis imperfecta segregates with a COL1A2 haplotype and is associated with a structural defect in the helical region of the type I procollagen molecule. All affected subjects had short stature, dentinogenesis imperfecta, and myopia; however, great differences were observed in the number of fractures and in the degree of bone deformity. Identical biochemical changes were found in the type I collagen molecules synthesised by fibroblasts of subjects with severe or minimal bone fragility. These results confirm that mutations in the triple helical region of alpha 2(I) chains produce a milder phenotype than analogous mutations in the alpha 1(I) chains, but indicate that, in addition to defects in the type I collagen molecule, other factors may modulate the degree of bone involvement in osteogenesis imperfecta.<\/jats:p>","DOI":"10.1136\/jmg.26.6.358","type":"journal-article","created":{"date-parts":[[2008,11,10]],"date-time":"2008-11-10T15:11:11Z","timestamp":1226329871000},"page":"358-362","source":"Crossref","is-referenced-by-count":30,"title":["Clinical variability of osteogenesis imperfecta linked to COL1A2 and associated with a structural defect in the type I collagen molecule."],"prefix":"10.1136","volume":"26","author":[{"given":"A","family":"Superti-Furga","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F","family":"Pistone","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C","family":"Romano","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B","family":"Steinmann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"239","published-online":{"date-parts":[[1989,6,1]]},"reference":[{"key":"ref_1","first-page":"237","article-title":"Perinatal lethal osteogenesis imperfecta (OI type II): a biochemically heterogeneous disorder usually due to new mutations in the genes for type I collagen","volume":"42","author":"Byers, P.H.; Tsipouras, P.; Bonadio, J.F.; Starman, B.J.; Schwartz, R.C.","year":"1988","unstructured":"Byers PH, Tsipouras P, Bonadio JF, Starman BJ, Schwartz RC. Perinatal lethal osteogenesis imperfecta (OI type II): a biochemically heterogeneous disorder usually due to new mutations in the genes for type I collagen. Am J Hum Genet 1988;42:237-48.","journal-title":"Am J Hum Genet"},{"key":"ref_2","first-page":"69","article-title":"Osteogenesis imperfecta is linked to both type I collagen structural genes","volume":"i:","author":"Sykes, B.; Ogilvie, D.; Wordsworth, P.; Anderson, J.; Jones, N.","year":"1986","unstructured":"Sykes B, Ogilvie D, Wordsworth P, Anderson J, Jones N. Osteogenesis imperfecta is linked to both type I collagen structural genes. Lancet 1986;i:69-72.","journal-title":"Lancet"},{"key":"ref_3","first-page":"47","article-title":"Imperfect collagenesis in osteogenesis imperfecta","volume":"543","author":"Steinmann, B.; Superti-Furga, A.; Royce, P.M.","year":"1988","unstructured":"Steinmann B, Superti-Furga A, Royce PM. Imperfect collagenesis in osteogenesis imperfecta. Ann NY Acad Sci 1988;543: 47-61.","journal-title":"Ann NY Acad Sci"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/BF00291667","article-title":"Homozygous osteogenesis imperfecta unlinked to collagen I genes","volume":"78","author":"Aitchison, K.; Ogilvie, D.; Honeyman, M.; Thompson, E.; Sykes, B.","year":"1988","unstructured":"Aitchison K, Ogilvie D, Honeyman M, Thompson E, Sykes B. Homozygous osteogenesis imperfecta unlinked to collagen I genes. Hum Genet 1988;78:233-6.","journal-title":"Hum Genet"},{"key":"ref_5","first-page":"55","article-title":"Cysteine in al chains of human type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta","volume-title":"Development and diseases of cartilage and bone matrix. UCLA Symp Mol Cell Biol","volume":"46","author":"N, De Vries; W, De Wet","year":"1987","unstructured":"De Vries N, De Wet W. Cysteine in al chains of human type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta. In: Sen A, Thornhill T, eds. Development and diseases of cartilage and bone matrix. UCLA Symp Mol Cell Biol. New York: Alan R Liss, 1987;46:55-64."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"14094","DOI":"10.1016\/S0021-9258(18)89861-1","article-title":"A heterozygous defect for structurally altered proa2 chain of type I procollagen in a mild variant of osteogenesis imperfecta","volume":"259","author":"Sippola, M.; Kaffe, S.; Prockop, D.J.","year":"1984","unstructured":"Sippola M, Kaffe S, Prockop DJ. A heterozygous defect for structurally altered proa2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. J Biol Chem 1984;259: 14094-100.","journal-title":"J Biol Chem"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"11407","DOI":"10.1016\/S0021-9258(18)37971-7","article-title":"A 19-base pair deletion in the proa2(I) gene of type I procollagen that causes in-frame splicing from exon 10 to exon 12 in a proband with atypical osteogenesis imperfecta and in his asymptomatic mother","volume":"263","author":"Kuivaniemi, H.; Sabol, C.; Tromp, G.; Sippola-Thiele, M.; Prockop, D.J.","year":"1988","unstructured":"Kuivaniemi H, Sabol C, Tromp G, Sippola-Thiele M, Prockop DJ. A 19-base pair deletion in the proa2(I) gene of type I procollagen that causes in-frame splicing from exon 10 to exon 12 in a proband with atypical osteogenesis imperfecta and in his asymptomatic mother. J Biol Chem 1988;263:11407-13.","journal-title":"J Biol Chem"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"6226","DOI":"10.1016\/S0021-9258(18)68776-9","article-title":"Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3AI alleles affecting structure, stability and processing of type III procoliagen","volume":"263","author":"Superti-Furga, A.; Gugler, E.; Gitzelmann, R.; Steinmann, B.","year":"1988","unstructured":"Superti-Furga A, Gugler E, Gitzelmann R, Steinmann B. Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3AI alleles affecting structure, stability and processing of type III procoliagen. J Biol Chem 1988;263: 6226-32.","journal-title":"J Biol Chem"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/0006-291X(88)90497-4","article-title":"Impaired secretion of type III procoliagen in Ehlers-Danlos syndrome type IV: correction of the defect by incubation at reduced temperature and demonstration of subtle alterations in the triple-helical region of the molecule","volume":"150","author":"Superti-Furga, A.; Steinmann, B.","year":"1988","unstructured":"Superti-Furga A, Steinmann B. Impaired secretion of type III procoliagen in Ehlers-Danlos syndrome type IV: correction of the defect by incubation at reduced temperature and demonstration of subtle alterations in the triple-helical region of the molecule. Biochem Biophys Res Commun 1988;150:140-7.","journal-title":"Biochem Biophys Res Commun"},{"key":"ref_10","first-page":"1","article-title":"Fetal DNA analysis","volume-title":"genetic diseases-a practical approach","author":"Old, J.M.","year":"1986","unstructured":"Old JM. Fetal DNA analysis. In: Davies KE, ed. Human genetic diseases-a practical approach. Oxford: IRL Press, 1986:1-17."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1042\/bj2520633","article-title":"Structure of a full-length cDNA clone for the preproa2(I) chain of human type I procollagen","volume":"252","author":"Kuivaniemi, H.; Tromp, G.; Chu, M.L.; Prockop, D.J.","year":"1988","unstructured":"Kuivaniemi H, Tromp G, Chu ML, Prockop DJ. Structure of a full-length cDNA clone for the preproa2(I) chain of human type I procollagen. Biochem J 1988;252:633-40.","journal-title":"Biochem J"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1111\/j.1749-6632.1988.tb55319.x","article-title":"Delayed triple-helix formation of abnormal type I collagen is corrected by reduced temperature-studies on a family with variable expression of osteogenesis imperfecta","volume":"543","author":"Superti-Furga, A.; Royce, P.M.; Pistone, F.M.; Romano, C.; Steinmann, B.","year":"1988","unstructured":"Superti-Furga A, Royce PM, Pistone FM, Romano C, Steinmann B. Delayed triple-helix formation of abnormal type I collagen is corrected by reduced temperature-studies on a family with variable expression of osteogenesis imperfecta. Ann NY Acad Sci 1988;543:85-92.","journal-title":"Ann NY Acad Sci"},{"key":"ref_13","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, D.O.; Senn, A.S.; Danks, D.M.","year":"1979","unstructured":"Sillence DO, Senn AS, Danks DM. Genetic heterogeneity in osteogenesis imperfecta. J Med Genet 1979;16:101-16.","journal-title":"J Med Genet"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1172\/JCI112735","article-title":"Osteogenesis imperfecta type IV: biochemical confirmation of genetic linkage to the proa2(I) gene of type I collagen","volume":"78","author":"Wenstrup, R.J.; Tsipouras, P.; Byers, P.H.","year":"1986","unstructured":"Wenstrup RJ, Tsipouras P, Byers PH. Osteogenesis imperfecta type IV: biochemical confirmation of genetic linkage to the proa2(I) gene of type I collagen. J Clin Invest 1986;78:1449-55.","journal-title":"J Clin Invest"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"7734","DOI":"10.1016\/S0021-9258(18)68560-6","article-title":"Arginine for glycine substitution in the triple-helical domain of the products of one a2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype","volume":"263","author":"Wenstrup, R.J.; Cohn, D.H.; Cohen, T.; Byers, P.H.","year":"1988","unstructured":"Wenstrup RJ, Cohn DH, Cohen T, Byers PH. Arginine for glycine substitution in the triple-helical domain of the products of one a2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype. 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London: Butterworths, 1983;111-25."}],"container-title":["Journal of Medical Genetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1136\/jmg.26.6.358","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,5]],"date-time":"2025-10-05T18:45:51Z","timestamp":1759689951000},"score":1,"resource":{"primary":{"URL":"https:\/\/jmg.bmj.com\/lookup\/doi\/10.1136\/jmg.26.6.358"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,6]]},"references-count":18,"journal-issue":{"issue":"6","published-online":{"date-parts":[[1989,6,1]]},"published-print":{"date-parts":[[1989,6]]}},"alternative-id":["10.1136\/jmg.26.6.358"],"URL":"https:\/\/doi.org\/10.1136\/jmg.26.6.358","relation":{},"ISSN":["0022-2593","1468-6244"],"issn-type":[{"value":"0022-2593","type":"print"},{"value":"1468-6244","type":"electronic"}],"subject":[],"published":{"date-parts":[[1989,6]]}}}