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2002 | 49 | 2 | 443-450
Article title

A novel Gly to Arg substitution at position 388 of the α1 chain of type I collagen in lethal form of osteogenesis imperfecta.

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EN
Abstracts
EN
Cultured skin fibroblasts from a proband with a lethal form of osteogenesis imperfecta produce two forms of type I collagen chains, with normal and delayed electrophoretic migration; collagen of the proband's mother was normal. Peptide mapping experiments localized the structural defect in the proband to α1(I) CB8 peptide in which residues 123 to 402 are spaned. Direct sequencing of amplified cDNA covering this region revealed a G to A single base change in one allele of the α1(I) chain, that converted glycine 388 to arginine. Restriction enzyme digestion of the RT-PCR product was consistent with a heterozygous COL1A1 mutation. The novel mutation conforms to the linear gradient of clinical severity for the α1(I) chain and results in reduced thermal stability by 3°C and intracellular retention of abnormal molecules.
Keywords
Publisher

Year
Volume
49
Issue
2
Pages
443-450
Physical description
Dates
published
2002
received
2002-02-13
revised
2002-05-14
accepted
2002-06-05
Contributors
author
  • Department of Medical Chemistry, Medical Academy of Białystok, Białystok, Poland
  • Department of Gynaecological Endocrinology, Medical Academy of Białystok, Białystok, Poland
  • Department of Genetics, Medical Academy of Białystok, Białystok, Poland
  • Department of Molecular Biology, Medical Academy of Białystok, Białystok, Poland
  • Department of Medical Chemistry, Medical Academy of Białystok, Białystok, 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.
  • Bonadio J, Holbrook KA, Gelinas RE, Jacob J, Byers PH. (1985) Altered triple helical structure of type I procollagen in lethal perinatal osteogenesis imperfecta. J Biol Chem.; 260: 1734-42.
  • Byers PH. (1990) Brittle bones-fragile molecules: disorders of collagen gene structure and expression. Trends Genet.; 6: 293-300.
  • Chomczynski P, Sacchi N. (1987) Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem.; 162: 156-9.
  • Cohen-Solal L, Zolezzi F, Pignatti PF, Mottes M. (1996) Intrafamilial variable expressivity of osteogenesis imperfecta due to mosaicism for a lethal G382R substitution in the COL1A1 gene. Mol Cell Probes.; 10: 219-25.
  • Cole WG. (1994) Collagen genes: mutations affecting collagen structure and expression. Prog Nucleic Acid Res Mol Biol.; 47: 29-80.
  • Deak SB, Scholz PM, Amenta PS, Constantinou CD, Levi-Minzi SA, Gonzales-Lavin L, Mackenzie JW. (1991) The substitution of arginine for glycine 85 in the α1(I) procollagen chain results in mild osteogenesis imperfecta. J Biol Chem.; 266: 21827-32.
  • 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.
  • Gat-Yablonski G, Ries L, Lev D, Goldman B, Friedman E. (1997) A missense mutation in Col1A1 in Jewish Israeli patient with mild osteogenesis imperfecta, detected by DGGE. Hum Genet.; 101: 22-5.
  • Kuivaniemi H, Tromp G, Prockop DJ. (1991) Mutations in collagen genes: causes of rare and some common diseases in humans. FASEB J.; 5: 2052-60.
  • Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
  • Laskey RA, Mills AD. (1975) Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem.; 56: 335-41.
  • Mackay K, Byers PH, Dalgleish R. (1993) An RT-PCR-SSCP screening strategy for detection of mutations in the gene encoding the α1 chain of type I collagen: application to four patients with osteogenesis imperfecta. Hum Mol Genet.; 2: 1155-60.
  • Mackay K, De Paepe A, Nuytinck L, Dalgleish R. (1994) Substitution of glycine-172 by arginine in the alpha 1 chain of type I collagen in a patient with osteogenesis imperfecta, type III. Hum Mutat.; 3: 324-6.
  • Prockop DJ. (1992) Mutations in collagen genes as a cause of connective-tissue diseases. N Engl J Med.; 326: 540-6.
  • Pruchno CJ, Cohn DH, Wallis GA, Willing MC, Starman BJ, Zhang X, Byers PH. (1991) Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen. Hum Genet.; 87: 33-40.
  • Redford-Badwal DA, Stover ML, Valli M, McKinstry MB, Rowe DW. (1996) Nuclear retention of COL1A1 messenger RNA identifies null alleles causing mild osteogenesis imperfecta. J Clin Invest.; 97: 1035-40.
  • Sanger F, Nicklin S, Coulson AR. (1977) DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci U S A.; 74: 5463-7.
  • Sillence DO, Senn A, Danks DM. (1979) Genetic heterogeneity in osteogenesis imperfecta. J Med Genet.; 16: 101-16.
  • Sztrolovics R, Glorieux FH, Travers R, van der Rest M, Roughley BJ. (1994) Osteogenesis imperfecta: comparison of molecular defects with bone histological changes. Bone.; 15: 321-8.
  • Trummer T, Brenner R, Just W, Vogel W, Kennerknecht I. (2001) Recurrent mutations in the COL1A2 gene in patients with osteogenesis imperfecta. Clin Genet.; 59: 338-43.
  • Ward LM, Lalic L, Roughley PJ, Glorieux FH. (2001) Thirty-three novel COL1A1 and COL1A2 mutations in patients with osteogenesis imperfecta types I-IV. Hum Mutat.; 17: 434-9.
  • Wenstrup RJ, Shrago AW, Lever LW, Phillips CL, Byers PH, Cohn DH. (1991) Effect of different cysteine for glycine substitutions within α2(I) chain. J Biol Chem.; 266: 2590-4.
  • Westerhausen A, Kishi J, Prockop DJ. (1990) Mutations that substitute serine for glycine α1-598 and glycine α1-631 in type I procollagen. J Biol Chem.; 265: 13995-4000.
  • Wilcox W, Scott L, Cohn D. (1994) A N-terminal glycine to cysteine mutation in the collagen COL1A1 gene produces moderately severe osteogenesis imperfecta. Am J Hum Genet.; 55S: A367.
  • 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-abpv49i2p443kz
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