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Previous Volume 333:494-497 August 24, 1995 Number 8 Next

	Since this article has no abstract, we have provided an extract of the first 100 words of the full text and any section headings.

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Thrombin (factor IIa) is a serine protease that performs a number of functions in blood coagulation.¹ Among its most important actions is converting fibrinogen into fibrin monomers, which polymerize to form the fibrin clot. Thrombin participates in the activation of factors V, VIII, and XIII, as well as of platelets.² By binding to thrombomodulin on vascular endothelial cells, it forms a complex that activates protein C, thereby limiting the extent of an emerging clot.³ Cleavage of thrombin's inactive zymogen precursor, prothrombin (factor II), is required to generate functionally active thrombin.

Acquired inhibitors of certain coagulation factors are relatively common, but . . . [Full Text of this Article]

Case Report

Methods

Enzyme Immunoassays

Immunoblotting

Results

Discussion

Source Information

From the Departments of Laboratory Medicine (A.R.L.S., R.H., G.S., W.C.), Pharmacology (B.S.S.), and Pathology (R.P.), University of Washington Medical Center, Seattle.

Address reprint requests to Dr. La Spada at the Department of Laboratory Medicine, Box 357110, University of Washington Medical Center, 1959 N.E. Pacific St., Seattle, WA 98195.

References

This article has been cited by other articles:

• Madoiwa, S., Nakamura, Y., Mimuro, J., Furusawa, S., Koyama, T., Sugo, T., Matsuda, M., Sakata, Y. (2001). Autoantibody against prothrombin aberrantly alters the proenzyme to facilitate formation of a complex with its physiological inhibitor antithrombin III without thrombin conversion. Blood 97: 3783-3789 [Abstract] [Full Text]