DIRECT EVIDENCE FOR HAGEMAN FACTOR (FACTOR XII) ACTIVATION BY BACTERIAL LIPOPOLYSACCHARIDES (ENDOTOXINS)

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  • David C. Morrison
    From the Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California 92037
  • Charles G. Cochrane
    From the Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California 92037

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<jats:p>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.</jats:p>

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