{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T04:38:31Z","timestamp":1785213511644,"version":"3.55.0"},"reference-count":16,"publisher":"BMJ","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Med Genet"],"published-print":{"date-parts":[[1990,9]]},"abstract":"<jats:p>The features of a baby with lethal perinatal osteogenesis imperfecta (OI II), owing to a frameshift mutation that resulted in the production of a truncated and functionless carboxy terminal propeptide of the pro alpha 1(I) chain of type I procollagen, were studied. The baby (OI26) was heterozygous for an insertion of a single uridine nucleotide after base pair 4088 of the prepro alpha 1(I) mRNA of type I procollagen. Only normal type I collagen was incorporated into the extracellular matrix of bone and dermis resulting in a type I collagen content of about 20% of control tissues. The baby was born at 35 weeks' gestation and died shortly afterwards. He was small and had the radiographical features most like those of OI IIB. The skeleton was poorly ossified. The ribs were discontinuously beaded and the femora were broad with multiple healed fractures of the diaphyses and metaphyses. Other long bones had broad metaphyses with overmodelled diaphyses. The calvarium contained many hundreds of wormian bones. Histological examination showed grossly deficient endochondral and intramembranous ossification. The bone was of a woven type without evidence of lamellar bone or Haversian systems and the osteoblasts did not mature into osteocytes. The cortex of the femur contained Haversian canals but they were surrounded by loose collagen fibres and a mosaic pattern of woven bone and islands of cartilage. We propose that OI IIB can be sub-classified into two groups, one with helical mutations and both normal and mutant type I collagen in the tissues, and the other with carboxy terminal propeptide mutations and a severe type I collagen deficiency, but without mutant collagen in the tissues.<\/jats:p>","DOI":"10.1136\/jmg.27.9.545","type":"journal-article","created":{"date-parts":[[2008,11,10]],"date-time":"2008-11-10T15:11:11Z","timestamp":1226329871000},"page":"545-551","source":"Crossref","is-referenced-by-count":18,"title":["The clinical features of osteogenesis imperfecta resulting from a non-functional carboxy terminal pro alpha 1(I) propeptide of type I procollagen and a severe deficiency of normal type I collagen in tissues."],"prefix":"10.1136","volume":"27","author":[{"given":"W G","family":"Cole","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P E","family":"Campbell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J G","family":"Rogers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J F","family":"Bateman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"239","published-online":{"date-parts":[[1990,9,1]]},"reference":[{"key":"ref_1","first-page":"237","article-title":"These features are in the genes for type I collagen","volume":"42","year":"1988","unstructured":"These features are in the genes for type I collagen. Am J Hum Genet 1988;42: 237-48.","journal-title":"Am J Hum Genet"},{"issue":"01 1","key":"ref_2","first-page":"\"the\" # \"78","article-title":"very similar to those of human type I","volume":"1","author":"Chu, M.L.; Williams, C.J.; Pepe, G.; Hirsch, J.L.; Prockop, D.J.","year":"1983","unstructured":"Chu ML, Williams CJ, Pepe G, Hirsch JL, Prockop DJ, very similar to those of human type I 01 (01 1), the classical autosomal dominant mild type of this Ramirez F. Internal deletion in a collagen gene in a peripheral lethal form of osteogenesis imperfecta. Nature 1983;304:78-80.","journal-title":"Nature; classical autosomal dominant mild type of this Ramirez F. Internal deletion in a collagen gene in a peripheral lethal form of osteogenesis imperfecta"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"7021","DOI":"10.1016\/S0021-9258(18)48196-3","article-title":"Lethal disease.20 Cultured fibroblasts from many cases of perinatal osteogenesis imperfecta due to the substitution of human OI I have decreased levels of COLlAl mRNA and reduced production of proal(I) chains.20 The arginine for glycine at residue 391 of the al(I) chain of type I collagen","volume":"262","author":"Bateman, J.F.; Chan, D.; Walker, I.D.; Rogers, J.G.; Cole, W.G.","year":"1987","unstructured":"Bateman JF, Chan D, Walker ID, Rogers JG, Cole WG. Lethal disease.20 Cultured fibroblasts from many cases of perinatal osteogenesis imperfecta due to the substitution of human OI I have decreased levels of COLlAl mRNA and reduced production of proal(I) chains.20 The arginine for glycine at residue 391 of the al(I) chain of type I collagen. J Biol Chem 1987;262:7021-7.","journal-title":"J Biol Chem"},{"key":"ref_4","first-page":"6045","article-title":"Lethal osteogenesis imperfecta resulting from a single nucleotide the cell and did not associate with normal chains.20 change in one human pro alpha","volume-title":"1(I) collagen allele. Proc Nail These reports and our findings in 0126 suggest that reduction in the amount of normal type I collagen in","volume":"83","author":"Cohn, D.H.; Byers, P.H.; Steinmann, B.; Gelinas, R.E.","year":"1986","unstructured":"Cohn DH, Byers PH, Steinmann B, Gelinas RE. Lethal osteogenesis imperfecta resulting from a single nucleotide the cell and did not associate with normal chains.20 change in one human pro alpha 1(I) collagen allele. Proc Nail These reports and our findings in 0126 suggest that reduction in the amount of normal type I collagen in Acad Sci USA 1986;83:6045-7."},{"key":"ref_5","first-page":"103","article-title":"Abnormal type I collagen metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta","volume":"217","author":"Bateman, J.F.; Mascara, T.; Chan, D.; Cole, W.G.","year":"1984","unstructured":"Bateman JF, Mascara T, Chan D, Cole WG. Abnormal type I collagen metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta. Biochemj 1984;217:103-15. homozygous frameshift mutation owing to a four base pair deletion in the COL1A2 gene was reported in a","journal-title":"Biochemj; homozygous frameshift mutation owing to a four base pair deletion in the COL1A2 gene was reported in a"},{"key":"ref_6","first-page":"699","article-title":"Collagen defects in lethal perinatal osteogenesis imperfecta","volume":"240","author":"Bateman, J.F.; Chan, D.; Mascara, T.; Rogers, J.G.; Cole, W.G.","year":"1986","unstructured":"Bateman JF, Chan D, Mascara T, Rogers JG, Cole WG. Collagen defects in lethal perinatal osteogenesis imperfecta. Biochem J 1986;240:699-708. child with a severe but viable type III form of 01.21 This mutation resulted in an abnormal proa2(I)","journal-title":"Biochem J; child with a severe but viable type III form of 01.21 This mutation resulted in an abnormal proa2(I"},{"key":"ref_7","article-title":"A frameshift mutation results in a truncated nonfunctional carboxy-terminal proal(I) propeptide of type I carboxy terminal propeptide in which the sequence of collagen in osteogenesis imperfecta","author":"Bateman, J.F.; Lamande, SR, Dahl; HHM, Chan; D, Mascara; T, Cole; W.G.","year":"1989","unstructured":"Bateman JF, Lamande SR, Dahl HHM, Chan D, Mascara T, Cole WG. A frameshift mutation results in a truncated nonfunctional carboxy-terminal proal(I) propeptide of type I carboxy terminal propeptide in which the sequence of collagen in osteogenesis imperfecta. J Biol Chem 1989;264: the last 33 amino acids was incorrect. 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Recurrence collagen in this child. The heterozygous parents had risks and prognosis in severe sporadic osteogenesis imperfecta. radiographical evidence of osteoporosis.22 In J Med Genet 1986;24:390-405.","journal-title":"radiographical evidence of osteoporosis.22 In; J Med Genet"},{"key":"ref_11","first-page":"2393","article-title":"Type III contrast, the heterozygous mutation in 0126 resulted collagen can be present on banded collagen fibrils regardless of in the loss of about half of the normal proal(I) chains, and the excess normal proa2(I) chains were not able fibril diameter","volume":"105","author":"Keene, D.R.; Sakai, L.Y.; Bachinger, H.P.; Burgeson, R.E.","year":"1987","unstructured":"Keene DR, Sakai LY, Bachinger HP, Burgeson RE. 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J Med Genet 1984;21:257-62.","journal-title":"J Med Genet"}],"container-title":["Journal of Medical Genetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1136\/jmg.27.9.545","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T08:14:01Z","timestamp":1760775241000},"score":1,"resource":{"primary":{"URL":"https:\/\/jmg.bmj.com\/lookup\/doi\/10.1136\/jmg.27.9.545"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,9]]},"references-count":16,"journal-issue":{"issue":"9","published-online":{"date-parts":[[1990,9,1]]},"published-print":{"date-parts":[[1990,9]]}},"alternative-id":["10.1136\/jmg.27.9.545"],"URL":"https:\/\/doi.org\/10.1136\/jmg.27.9.545","relation":{},"ISSN":["0022-2593","1468-6244"],"issn-type":[{"value":"0022-2593","type":"print"},{"value":"1468-6244","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,9]]}}}