Characterization of the fibrin polymer structure that accelerates thrombin cleavage of plasma factor XIII.

Published

Journal Article

The effect of plasmin-derived fibrin(ogen) degradation products on alpha-thrombin cleavage of plasma Factor XIII was studied to identify the fibrin polymer structure that promotes Factor XIIIa formation. Fibrin polymers derived from fibrinogen and Fragment X enhanced the rate of thrombin cleavage of plasma Factor XIII in plasma or buffered solutions. The concentrations of fibrinogen and Fragment X that promoted half-maximal rates of Factor XIIIa formation were 5 and 40 micrograms/ml, respectively. Fragments Y, D, E, D-dimer, and photooxidized fibrinogen did not enhance thrombin cleavage of Factor XIII. Although purified Fragment D1 inhibited fibrin gelation, the soluble protofibrils promoted thrombin activation of Factor XIII. Noncrosslinked fibrin fibers failed to enhance thrombin cleavage of Factor XIII. In conclusion, soluble fibrin oligomers function to promote thrombin cleavage of plasma Factor XIII during blood clotting.

Full Text

Duke Authors

Cited Authors

  • Greenberg, CS; Achyuthan, KE; Rajagopalan, S; Pizzo, SV

Published Date

  • April 1, 1988

Published In

Volume / Issue

  • 262 / 1

Start / End Page

  • 142 - 148

PubMed ID

  • 2895608

Pubmed Central ID

  • 2895608

International Standard Serial Number (ISSN)

  • 0003-9861

Digital Object Identifier (DOI)

  • 10.1016/0003-9861(88)90176-2

Language

  • eng

Conference Location

  • United States