title: Delayed intermolecular gamma-chain cross-linking by factor XIIIa in fibrinogen Asahi characterized by a gamma-Met-310 to Thr substitution with an N-glycosylated gamma-Asn-308.
abstract: 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.
authors.affiliation: Division of Hemostasis and Thrombosis Research, Jichi Medical School, Tochigi, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Yamazumi
authors.forename: K
authors.initials: K
authors.lastname: Shimura
authors.forename: H
authors.initials: H
authors.lastname: Maekawa
authors.forename: S
authors.initials: S
authors.lastname: Muramatsu
authors.forename: S
authors.initials: S
authors.lastname: Terukina
authors.forename: M
authors.initials: M
authors.lastname: Matsuda
mesh_terms: D005340:Fibrinogen / Q000378:metabolism*; D015241:Fibrinogens, Abnormal / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D015394:Molecular Structure; D011487:Protein Conformation; D011503:Transglutaminases / Q000378:metabolism*; D000979:alpha-2-Antiplasmin / Q000378:metabolism
chemical_list: D015241:Fibrinogens, Abnormal; D005353:Fibronectins; D000979:alpha-2-Antiplasmin; C059379:fibrinogen Asahi; C027539:fibrinopeptides gamma; D005340:Fibrinogen; D011503:Transglutaminases