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Delayed intermolecular ??-chain cross-linking by factor XIIIa in fibrinogen Asahi characterized by a ??-Met-310 to Thr substitution with an N-glycosylated ??-Asn-308
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1990
Year
Protein AssemblyMolecular BiologyCytoskeletonFibrinogen AsahiImpaired Fibrin PolymerizationChemical BiologyDelayed Gamma-dimer FormationProtein FoldingFactor XiiiaProtein MisfoldingMulti-protein AssemblyThr SubstitutionBiochemistryCross-linkBiomolecular InteractionStructural BiologyProtein BiosynthesisNatural SciencesSynthetic BiologyMedicine
In an abnormal fibrinogen with gamma-Met-310 to Thr substitution accompanied by an extra oligosaccharide attached to gamma-Asn-308, factor-XIIIa-mediated intermolecular gamma-dimer formation of fibrin was found to be markedly delayed. The delayed gamma-dimer formation was not due to impaired fibrin polymerization because the fibrinogen gamma-chain also failed to be efficiently cross-linked by factor XIIIa. Since fluorescent amine was normally incorporated into the abnormal gamma-chain by factor XIIIa, we conclude that the abnormal molecules were unable to align their gamma-chains in an anti-parallel fashion because of inaccessibility of the molecules with a profoundly perturbed conformation near the carboxyl terminal region of the gamma-chain included in the D domain.