{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T00:38:07Z","timestamp":1760747887912,"version":"build-2065373602"},"reference-count":20,"publisher":"BMJ","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Med Genet"],"published-print":{"date-parts":[[1992,2]]},"abstract":"<jats:p>The features of three babies with perinatal lethal osteogenesis imperfecta (OI II) resulting from substitutions of glycine by valine in the triple helical domain of the alpha 1(I) chain of type I collagen were studied. The babies were heterozygous for this substitution at residue 1006 in case 1 (OI35), 973 in case 2 (OI59), and 256 in case 3 (OI7B). OI35 had the most severe clinical form, OI IIC, with premature rupture of membranes, severe antepartum haemorrhage, stillbirth, severe short limbed dwarfism, and extreme osteoporosis. OI59 was a better formed baby but was also born prematurely as a result of premature rupture of membranes and severe antepartum haemorrhage. She had the radiographic features of OI IIA. OI7B was born at term and also had the radiographic features of OI IIA. Pathological examination of the skeletons of OI35 and OI59 showed grossly deficient intramembranous and endochondral ossification. Trabecular bone was sparse in the long bones and vertebrae. The trabeculae contained a cartilage core and an overlying layer of woven bone or osteoid. The diaphyses lacked cortical bone. The periosteal fibroblasts of OI35 contained grossly distended rough endoplasmic reticulum consistent with the 53% reduction in collagen secretion by cultured dermal fibroblasts. The aorta, skin, and lungs were hypoplastic in OI35 and OI59. The findings in this study show that glycine substitutions by valine in Gly-X-Y triplets, from glycine 256 to glycine 1006, of the triple helical domain of alpha 1(I) chains produce the OI II phenotype. The phenotype was most severe in the baby with the most carboxy-terminal substitution.<\/jats:p>","DOI":"10.1136\/jmg.29.2.112","type":"journal-article","created":{"date-parts":[[2008,11,10]],"date-time":"2008-11-10T15:23:16Z","timestamp":1226330596000},"page":"112-118","source":"Crossref","is-referenced-by-count":16,"title":["The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen."],"prefix":"10.1136","volume":"29","author":[{"given":"W G","family":"Cole","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E","family":"Patterson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J","family":"Bonadio","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P E","family":"Campbell","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D W","family":"Fortune","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"239","published-online":{"date-parts":[[1992,2,1]]},"reference":[{"key":"ref_1","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_2","doi-asserted-by":"crossref","first-page":"10960","DOI":"10.1016\/S0021-9258(18)60412-0","article-title":"A frameshift mutation results in a truncated non-functional carboxy-terminal propeptide of type I procollagen in osteogenesis imperfecta","volume":"264","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 non-functional carboxy-terminal propeptide of type I procollagen in osteogenesis imperfecta. J Biol Chem 1989;264: 10960-4.","journal-title":"J Biol Chem"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1136\/jmg.27.9.545","article-title":"The clinical features of osteogenesis imperfecta resulting from a non-functional carboxy terminal proal(I) propeptide of type I procollagen and a severe deficiency of normal type I collagen in tissues","volume":"27","author":"Cole, W.G.; Campbell, P.E.; Rogers, J.G.; Bateman, J.F.","year":"1990","unstructured":"Cole WG, Campbell PE, Rogers JG, Bateman JF. The clinical features of osteogenesis imperfecta resulting from a non-functional carboxy terminal proal(I) propeptide of type I procollagen and a severe deficiency of normal type I collagen in tissues. J Med Genet 1990;27:545-5 1.","journal-title":"J Med Genet"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1042\/bj2170103","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. Biochem J 1984;217:103-15.","journal-title":"Biochem J"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1042\/bj2400699","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. BiochemJ 1986;240:699-708.","journal-title":"BiochemJ"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1136\/jmg.27.4.228","article-title":"The clinical features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by arginine in the pro al(I) chain of type I procollagen","volume":"27","author":"Cole, W.G.; Chow, C.W.; Rogers, J.G.; Bateman, J.F.","year":"1990","unstructured":"Cole WG, Chow CW, Rogers JG, Bateman JF. The clinical features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by arginine in the pro al(I) chain of type I procollagen. J Med Genet 1990;27:228-35.","journal-title":"J Med Genet"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1734","DOI":"10.1016\/S0021-9258(18)89655-7","article-title":"Altered triple helical structure of type-I procollagen in lethal perinatal osteogenesis imperfecta","volume":"260","author":"Bonadio, J.F.; Holbrook, K.A.; Gelinas, R.E.; Jacob, J.; Byers, P.H.","year":"1985","unstructured":"Bonadio JF, Holbrook KA, Gelinas RE, Jacob J, Byers PH. Altered triple helical structure of type-I procollagen in lethal perinatal osteogenesis imperfecta. J Biol Chem 1985;260:1734-42.","journal-title":"J Biol Chem"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/316363a0","article-title":"Subtle structural alterations in the chains of type-I procollagen produce osteogenesis imperfecta type-II","volume":"316","author":"Bonadio, J.F.; Byers, P.H.","year":"1985","unstructured":"Bonadio JF, Byers PH. Subtle structural alterations in the chains of type-I procollagen produce osteogenesis imperfecta type-II. Nature 1985;316:363-6.","journal-title":"Nature"},{"issue":"1","key":"ref_9","first-page":"1129","article-title":"Cysteine in the triple-helical domain of one allelic product of the alpha-i (I) gene of type-I collagen produces a lethal form of osteogenesis imperfecta","volume":"259","author":"Steinmann, B.; Rao, V.H.; Vogel, A.; Bruckner, P.; Gitzelmann, R.; Byers, P.H.","year":"1986","unstructured":"Steinmann B, Rao VH, Vogel A, Bruckner P, Gitzelmann R, Byers PH. Cysteine in the triple-helical domain of one allelic product of the alpha-i (I) gene of type-I collagen produces a lethal form of osteogenesis imperfecta. J Biol Chem 1986;259:1 1129-38.","journal-title":"J Biol Chem"},{"key":"ref_10","first-page":"1206","article-title":"Osteogenesis imperfecta: the position of substitution of glycine by cysteine in the triple helical domain of the proacl (I) chains of type I collagen determines Clin Invest","volume":"84","author":"Starman, B.J.; Eyre, D.; Charbonneau, H.","year":"1989","unstructured":"Starman BJ, Eyre D, Charbonneau H, et al. Osteogenesis imperfecta: the position of substitution of glycine by cysteine in the triple helical domain of the proacl (I) chains of type I collagen determines Clin Invest 1989;84:1206-14."},{"key":"ref_11","first-page":"10083","article-title":"RNA sequence analysis of a Biol perinatal lethal osteogenesis","volume":"264","author":"Patterson, E.; Smiley, E.; Bonadio, J.","year":"1989","unstructured":"Patterson E, Smiley E, Bonadio J. RNA sequence analysis of a Biol perinatal lethal osteogenesis Chem 1989;264:10083-7.","journal-title":"Chem"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"15809","DOI":"10.1016\/S0021-9258(18)71548-2","article-title":"Characterization of point mutations in the collagen COLlA1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta","volume":"264","author":"Lamande, SR, Dahl; HHM, Cole; WG, Bateman; J.F.","year":"1989","unstructured":"Lamande SR, Dahl HHM, Cole WG, Bateman JF. Characterization of point mutations in the collagen COLlA1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta. J Biol Chem 1989;264:15809-12.","journal-title":"J Biol Chem"},{"key":"ref_13","first-page":"157","article-title":"Revised intrauterine growth curves for an Australian hospital population","volume-title":"Aust PaediatrJ1","volume":"19","author":"Kitchen, W.H.; Robinson, H.P.; Dickinson, A.J.","year":"1983","unstructured":"Kitchen WH, Robinson HP, Dickinson AJ. Revised intrauterine growth curves for an Australian hospital population. Aust PaediatrJ1 1983;19:157-61."},{"key":"ref_14","first-page":"131","article-title":"Mutagenesis of the mouse prootl(I) collagen gene: substitution of a glycine results in osteogenesis imperfecta in cultured cells and transgenic mice","volume":"332","author":"Stacey, A.; Bateman, J.F.; Choi, T.; Mascara, T.; Cole, W.G.; Jaenisch, R.","year":"1988","unstructured":"Stacey A, Bateman JF, Choi T, Mascara T, Cole WG, Jaenisch R. Mutagenesis of the mouse prootl(I) collagen gene: substitution of a glycine results in osteogenesis imperfecta in cultured cells and transgenic mice. Nature 1988;332:131-6.","journal-title":"Nature"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"18628","DOI":"10.1016\/S0021-9258(17)44798-3","article-title":"Substitution of arginine for glycine at position 847 in the triplehelical domain of type I collagen produces lethal osteogenesis imperfecta","volume":"265","author":"Wallis, G.A.; Starman, B.J.; Schwartz, M.F.; Byers, P.H.","year":"1990","unstructured":"Wallis GA, Starman BJ, Schwartz MF, Byers PH. Substitution of arginine for glycine at position 847 in the triplehelical domain of type I collagen produces lethal osteogenesis imperfecta. JBiol Chem 1990;265:18628-33.","journal-title":"JBiol Chem"},{"key":"ref_16","first-page":"1034","article-title":"Variable expression of osteogenesis imperfecta in a nuclear family is explained by somatic mosaicism for a lethal point mutation in the al (I) gene (COLlA1) of type I collagen in a parent","volume":"46","author":"Wallis, G.A.; Starman, B.J.; Zinn, A.B.; Byers, P.H.","year":"1990","unstructured":"Wallis GA, Starman BJ, Zinn AB, Byers PH. Variable expression of osteogenesis imperfecta in a nuclear family is explained by somatic mosaicism for a lethal point mutation in the al (I) gene (COLlA1) of type I collagen in a parent. Am J Hum Genet 1990;46:1034-40.","journal-title":"Am J Hum Genet"},{"key":"ref_17","first-page":"6045","article-title":"Lethal osteogenesis imperfecta resulting from a single nucleotide change","volume-title":"one human alpha 1(I) collagen allele. Proc Nati Acad Sci","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 change in one human alpha 1(I) collagen allele. Proc Nati Acad Sci USA 1986;83:6045-7."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1172\/JCI113920","article-title":"A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen","volume":"83","author":"Constantinou, C.D.; Nielsen, K.B.; Prockop, D.J.","year":"1989","unstructured":"Constantinou CD, Nielsen KB, Prockop DJ. A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen. J Clin Invest 1989; 83:574-84.","journal-title":"J Clin Invest"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"19249","DOI":"10.1016\/S0021-9258(18)37416-7","article-title":"A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away","volume":"263","author":"Vogel, B.E.; Doely, R.; Kadler, K.E.; Hojima, Y.; Engel, J.; Prockop, D.J.","year":"1988","unstructured":"Vogel BE, Doely R, Kadler KE, Hojima Y, Engel J, Prockop DJ. A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away. J Biol Chem 1988; 263:19249-55.","journal-title":"J Biol Chem"},{"key":"ref_20","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-al(I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain","volume":"266","author":"Valli, M.; Mottes, M.; Tenni, R.","year":"1991","unstructured":"Valli M, Mottes M, Tenni R, et al. A de novo G to T transversion in a pro-al(I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain. 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