Research Article
DIRECT EVIDENCE FOR HAGEMAN FACTOR (FACTOR XII) ACTIVATION BY BACTERIAL LIPOPOLYSACCHARIDES (ENDOTOXINS)
David C. Morrison, Charles G. Cochrane
Published:
September 01, 1974
DOI:
License:
Copyright © 1974 by The Rockefeller University Press
Abstract
Purified precursor Hageman factor has been demonstrated to bind to soluble bacterial lipopolysaccharide (LPS, endotoxin) isolated from Escherichia coli 0111:B4, and this complex has been shown to have the capacity to convert prekallikrein to its active form. In addition, LPS-activated Hageman factor substantially reduces clotting times in XII-deficient plasma. The capacity to activate Hageman factor has been demonstrated to reside in the lipid A region of the LPS molecule. Activation of Hageman factor by LPS contrasts with fluid-phase activation (e.g., by kallikrein or trypsin) in that no cleavage to lower molecular weight fragments occurs. High concentrations of LPS inhibit the activity of Hageman factor, probably by a direct LPS-Hageman factor interaction.