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  • Title: A new type of Ser substitution for gamma Arg-275 in fibrinogen Kamogawa I characterized by impaired fibrin assembly.
    Author: Mimuro J, Kawata Y, Niwa K, Muramatsu S, Madoiwa S, Takano H, Sugo T, Sakata Y, Sugimoto T, Nose K, Matsuda M.
    Journal: Thromb Haemost; 1999 Jun; 81(6):940-4. PubMed ID: 10404772.
    Abstract:
    A new type of substitution, Arg to Ser at gamma275, has been found in a heterozygous dysfibrinogen derived from a 23-year-old woman with no major bleeding or thrombosis. By sequence analyses of the affected gamma-chain and its gene. we found a single amino acid substitution of gamma Arg-275 to Ser in an aberrant gamma (274-302) residue peptide isolated from lysyl endopeptidase-digests of the patient's fibrinogen. In agreement with this amino acid substitution, we identified a single nucleotide exchange of A for C at position 5728 in the gamma-chain gene creating a codon (AGC) encoding Ser instead of the codon (CGC) encoding Arg at position gamma 275. Like two other known types of mutants with a His or Cys substitution at this position, the functional abnormality was characterized by delayed fibrin polymerization, most likely due to impaired abutting of two D domains of adjacent fibrin monomers in the same strand of fibrin protofibrils. The structural derangement that affects the D:D association may not be so severe as compared with those of Cys and His mutants, possessing an additional disulfide-linked Cys molecule and an imidazole ring at the mutation site, respectively.
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