The alpha(E)C domain of human fibrinogen-420 is a stable and early plasmin cleavage product

Human fibrinogen-420, (alpha(E)betagamma)(2), was isolated from plasma and evaluated for its ability to form clots and for its susceptibility to proteolysis. Clotting parameters, including cross-linking of subunit chains, of this subclass and of the more abundant fibrinogen-340 (alphabetagamma)(2),...

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Bibliographic Details
Published in:Blood 2000-04, Vol.95 (7), p.2297-2303
Main Authors: Applegate, D, Steben, L S, Hertzberg, K M, Grieninger, G
Format: Article
Language:English
Subjects:
Animals
Blood Coagulation
Blotting, Western
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Fibrin Fibrinogen Degradation Products - metabolism
Fibrinogen - isolation & purification
Fibrinogen - metabolism
Fibrinolysin - metabolism
Humans
Mice
Myocardial Infarction - blood
Peptide Fragments - metabolism
Polymers - metabolism
Thrombin - metabolism
Transglutaminases - metabolism
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Summary:Human fibrinogen-420, (alpha(E)betagamma)(2), was isolated from plasma and evaluated for its ability to form clots and for its susceptibility to proteolysis. Clotting parameters, including cross-linking of subunit chains, of this subclass and of the more abundant fibrinogen-340 (alphabetagamma)(2), were found to be similar, suggesting little impact of the unique alpha(E)C domains of fibrinogen-420 on coagulation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of plasmic digestion patterns revealed production from fibrinogen-420 of the conventional fibrinogen degradation products, X, Y, D, and E, to be comparable to that from fibrinogen-340 in all respects except the presence of at least 2 additional cleavage products that were shown by Western blot analysis to contain the alpha(E)C domain. One was a stable fragment (alpha(E)CX) comigrating with a 34-kd yeast recombinant alpha(E)C domain, and the other was an apparent precursor. Their release occurred early, before that of fragments D and E. Two bands of the same mobility and antibody reactivity were found in Western blots of plasma collected from patients with myocardial infarction shortly after the initiation of thrombolytic therapy.
ISSN:0006-4971
DOI:10.1182/blood.v95.7.2297.007k39_2297_2303