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Blood, 1 August 2002, Vol. 100, No. 3, pp. 743-754
REVIEW ARTICLE
Role of factor XIII in fibrin clot formation and effects of
genetic polymorphisms
Robert A. S. Ariëns,
Thung-Shenq Lai,
John W. Weisel,
Charles S. Greenberg, and
Peter J. Grant
From the Academic Unit of Molecular Vascular Medicine,
University of Leeds School of Medicine, United Kingdom; the Department
of Medicine and the Department of Pathology, Duke University Medical
Center, Durham, NC; and the Department of Cell and Developmental
Biology, University of Pennsylvania School of Medicine, Philadelphia.
Factor XIII and fibrinogen are unusual among clotting factors in
that neither is a serine protease. Fibrin is the main protein constituent of the blood clot, which is stabilized by factor XIIIa through an amide or isopeptide bond that ligates adjacent fibrin monomers. Many of the structural and functional features of factor XIII
and fibrin(ogen) have been elucidated by protein and gene analysis,
site-directed mutagenesis, and x-ray crystallography. However, some of
the molecular aspects involved in the complex processes of insoluble
fibrin formation in vivo and in vitro remain unresolved. The findings
of a relationship between fibrinogen, factor XIII, and cardiovascular
or other thrombotic disorders have focused much attention on these 2 proteins. Of particular interest are associations between common
variations in the genes of factor XIII and altered risk profiles for
thrombosis. Although there is much debate regarding these observations,
the implications for our understanding of clot formation and
therapeutic intervention may be of major importance. In this review, we
have summarized recent findings on the structure and function of factor
XIII. This is followed by a review of the effects of genetic
polymorphisms on protein structure/function and their relationship to disease.
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