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2002 | 49 | 2 | 433-441
Article title

Mutations in type I collagen genes resulting in osteogenesis imperfecta in humans.

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EN
Abstracts
EN
Osteogenesis imperfecta (OI), commonly known as "brittle bone disease", is a dominant autosomal disorder characterized by bone fragility and abnormalities of connective tissue. Biochemical and molecular genetic studies have shown that the vast majority of affected individuals have mutations in either the COL1A1 or COL1A2 genes that encode the chains of type I procollagen. OI is associated with a wide spectrum of phenotypes varying from mild to severe and lethal conditions. The mild forms are usually caused by mutations which inactivate one allele of COL1A1 gene and result in a reduced amount of normal type I collagen, while the severe and lethal forms result from dominant negative mutations in COL1A1 or COL1A2 which produce structural defects in the collagen molecule. The most common mutations are substitutions of glycine residues, which are crucial to formation and function of the collagen triple helix, by larger amino acids. Although type I collagen is the major structural protein of both bone and skin, the mutations in type I collagen genes cause a bone disease. Some reports showed that the mutant collagen can be expressed differently in bone and in skin. Since most mutations identified in OI are dominant negative, the gene therapy requires a fundamentally different approach from that used for genetic-recessive disorders. The antisense therapy, by reducing the expression of mutant genes, is able to change a structural mutation into a null mutation, and thus convert severe forms of the disease into mild OI type I.
Publisher

Year
Volume
49
Issue
2
Pages
433-441
Physical description
Dates
published
2002
revised
2002-02-15
received
2002-02-7
accepted
2002-04-22
Contributors
  • Department of Medical Chemistry, Medical Academy of Białystok, 15-230 Białystok 8, Poland
References
  • Baker AT, Ramshaw JAM, Chan D, Cole WG, Bateman JF. (1989) Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of α1(I)-chain glycine-to-arginine substitutions. Biochem J.; 261: 253-7.
  • Chessler SD, Wallis GA, Byers PH. (1993) Mutations in the carboxyl-terminal propeptide of the proα1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta. J Biol Chem.; 268: 18218-25.
  • Cohen-Solal L, Zylberberg L, Sangalli A, Gomez Lira M, Mottes M. (1994) Substitution of aspartic acid for glycine 700 in the α2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone. J Biol Chem.; 269: 14751-8.
  • Cole WG. (1994) Collagen genes: mutations affecting collagen structure and expression. Prog Nucleic Acid Res Mol Biol.; 47: 29-80.
  • Dalgleish R. (1998) The human type I collagen mutation database. Nucleic Acids Res.; 26: 253-5.
  • Dawson P, Marini JC. (2000) Hammerhead ribozymes selectively suppress mutant type I collagen mRNA in osteogenesis imperfecta fibroblasts. Nucleic Acids Res.; 28: 4013-20.
  • Fedarko NS, Robey PG, Vetter UK. (1995) Extracellular matrix stechiometry in osteoblasts from patients with osteogenesis imperfecta. J Bone Miner Res.; 10: 1122-9.
  • Forlino A, Porter FD, Lee EJ, Westphal H, Marini JC. (1999) Use of the Cre/lox recombination system to develop a non-lethal knock-in murine model for osteogenesis imperfecta with an α1(I) G349C substitution. JBiol Chem.; 274: 37923-31.
  • Galicka A, Wolczynski S, Gindzienski A. (2002) Comparative studies of osteoblast and fibroblast type I collagen in a patient with osteogenesis imperfecta type IV. J Pathol.; 196: 235-7.
  • Galicka A, Wolczynski S, Anchim T, Surazynski A, Lesniewicz R, Palka J. (2001) Defects of type I procollagen metabolism correlated with decrease of prolidase activity in a case of lethal osteogenesis imperfecta. Eur J Biochem.; 268: 2172-8.
  • Glorieux FH, Rauch F, Plotkin H, Ward L, Travers R, Roughley PJ, Lalic L, Glorieux DF, Fassier F, Bishop N. (2000) Osteogenesis imperfecta type V: a new form of brittle bone disease. J Bone Min Res.; 15: 1650-8.
  • Grassi G, Forlino A, Marini JC. (1997) Cleavage of collagen RNA transcripts by hammerhead ribozymes in vitro is mutation-specific and shows competitive binding effects. Nucleic Acids Res.; 25: 3451-38.
  • Kielty CM, Hopkinson I, Grant ME. (1993) Collagen: the collagen family: structure, assembly, and organization in the extracellular matrix. In Connective tissue and its heritable disorders: Molecular, genetic and medical aspects. Royce PM, Steinmann B. eds, pp 103-47, Wiley-Liss New York.
  • Lehmann HW, Rimek D, Bodo M, Brenner RE, Vetter U, Worsdorfer O, Karbowski A, Muller PK. (1995) Hydroxylation of collagen type I: evidence that both lysyl and prolyl residues are overhydroxylated in osteogenesis imperfecta. Eur J Clin Invest.; 25: 306-10.
  • Marini JC, Lewis MB, Wang Q, Chen KJ, Orrison BM. (1993) Serine for glycine substitution in type I collagen in two cases of type IV osteogenesis imperfecta (OI): additional evidence for a regional model of OI pathophysiology. J Biol Chem.; 268: 2667-73.
  • Mundlos S, Chan D, Weng YM, Sillence DO, Cole WG, Bateman JF. (1996) Multiexon deletions in the type I collagen COL1A2 gene in osteogenesis imperfecta type IB. Molecules containing the shortened α2(I) chains show differential incorporation into the bone and skin extracellular matrix. J Biol Chem.; 271: 21068-74.
  • Niyibizi Ch, Bonadio J, Byers PH, Eyre DR. (1992) Incorporation of type I collagen molecules that contain a mutant α2(I) chain (Gly580→Asp) into bone matrix in a lethal case of osteogenesis imperfecta. J Biol Chem.; 267: 23108-12.
  • Prockop DJ, Kivirikko KL. (1984) Heritable diseases of collagen. N Engl J Med.; 311: 376-86.
  • Raughunath M, Bruckner P, Steinmann B. (1994) Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta. J Mol Biol.; 236: 940-9.
  • Sarafova AP, Choi H, Forlino A, Gajko A, Cabral WA, Tosi L, Reing CM, Marini JC. (1998) Three novel type I collagen mutations in osteogenesis imperfecta type IV probands are associated with discrepancies between electrophoretic migration of osteoblast and fibroblast collagen. Hum Mut.; 11: 395-403.
  • Scott JE. (1988) Proteoglycan-fibrillar collagen interactions. Biochem J.; 252: 313-23.
  • Sillence DO, Senn A, Danks DM. (1979) Genetic heterogeneity in osteogenesis imperfecta. JMed Genet.; 16: 101-16.
  • Starman BJ, Eyre D, Charbonneau H, Harrylock M, Weis MA, Weiss L, Graham JM. Byers PH. (1989) The position of substitution for glycine by cysteine in the triple helical domain of the proα1(I) chains of type I collagen determines the clinical phenotype. J Clin Invest.; 84: 1206-14.
  • Sykes B. (1985) The molecular genetics of collagen. BioEssays; 3: 112-7.
  • Tenni R, Cetta G, Dyne K, Rossi A, Quacci D, Lenzi L, Castellani AA. (1988) Type I procollagen in the severe non-lethal form of osteogenesis imperfecta. Defective pro-α1(I) chains in a patient with abnormal proteoglycan metabolism and mineral deposits in the dermis. Hum Genet.; 79: 245-50.
  • Valli M, Zolezzi F, Mottes M, Antoniazzi F, Stanzial F, Tenni R, Pignatti P, Cetta G. (1993) Gly85 to Val substitution in proα1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion. Eur J Biochem.; 217: 77-82.
  • Vogel BE, Doelz R, Kadler KE, Hojima Y, Engel J, Prockop DJ. (1988) A substitution of cysteine for glycine 748 of the α1 chain produces a kink at this site in the procollagen molecule and an altered N-proteinase cleveage site over 225 nm away. J Biol Chem.; 263: 19249-55.
  • Wang Q, Marini JC. (1996) Antisense oligodeoxynucleotides selectively suppress expression of the mutant α2(I) collagen allele in type IV osteogenesis imperfecta fibroblasts. A molecular approach to therapeutics of dominant negative disorders. J Clin Invest.; 97: 448-54.
  • Ward L, Rauch F, Travers R, Lalic L, Alos N, Lalic R, Roughley PJ, Glorieux FH. (2000) Osteogenesis imperfecta type VI: a form of brittle bone disease with a mineralization defect. J Bone Min Res.; 15: M116.
  • Willing MC, Deschenes SP, Slayton RL, Roberts EJ. (1996) Premature chain termination is a unifying mechanism for COL1A1 null alleles in osteogenesis imperfecta type I cell strains. Am J Hum Genet.; 59: 799-809.
  • Zhuang J, Tromp G, Kuivaniemi H, Castells S, Prockop DJ. (1996) Substitution of arginine for glycine at position 154 of the α1 chain of type I collagen in a variant of osteogenesis imperfecta: comparison to previous cases with the same mutation. Am J Med Genet.; 61: 111-6.
  • Zlotogora J. (1998) Germ line mosaicism. Hum Genet.; 102: 381-6.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv49i2p433kz
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