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Factor XI activation in a revised model of blood coagulation.

Abstract
Coagulation factor XI is activated in vitro by factor XIIa in the presence of high molecular weight kininogen (HMWK) and a negatively charged surface. Factor XII deficiency is not associated with bleeding, which suggests that another mechanism for factor XI activation exists in vivo. A revised model of coagulation is proposed in which factor XI is activated by thrombin. In the absence of cofactors, thrombin is more effective (kcat/Km = 1.6 x 10(5)) than factor XIIa (1.7 x 10(4)) in activating factor XI. Dextran sulfate enhances activation of factor XI by thrombin 2000-fold; part of this effect is due to autoactivation of factor XI by activated factor XI.
AuthorsD Gailani, G J Broze Jr
JournalScience (New York, N.Y.) (Science) Vol. 253 Issue 5022 Pg. 909-12 (Aug 23 1991) ISSN: 0036-8075 [Print] United States
PMID1652157 (Publication Type: Comparative Study, Journal Article)
Chemical References
  • Chromogenic Compounds
  • Kininogens
  • Macromolecular Substances
  • Oligopeptides
  • Receptors, Cell Surface
  • Receptors, Thrombin
  • Recombinant Proteins
  • S 2366
  • Factor XI
  • Dextran Sulfate
  • Factor XIIa
  • Thrombin
  • Pyrrolidonecarboxylic Acid
Topics
  • Blood Coagulation
  • Chromogenic Compounds (metabolism)
  • Dextran Sulfate (pharmacology)
  • Factor XI (chemistry, metabolism)
  • Factor XIIa (pharmacology)
  • Hemostasis (physiology)
  • Kininogens (pharmacology)
  • Macromolecular Substances
  • Models, Biological
  • Oligopeptides (metabolism)
  • Pyrrolidonecarboxylic Acid (analogs & derivatives)
  • Receptors, Cell Surface (pharmacology)
  • Receptors, Thrombin
  • Recombinant Proteins (pharmacology)
  • Thrombin (pharmacology)

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