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 Blood, 5 November 2009, Vol. 114, No. 19, pp. 3994-4001.
Prepublished online as a Blood First Edition Paper on August 17, 2009; DOI 10.1182/blood-2009-05-217968.

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REVIEW ARTICLE

The pleiotropic role of the fibrinogen {gamma}' chain in hemostasis

Shirley Uitte de Willige1, Kristina F. Standeven1, Helen Philippou1, and Robert A. S. Ariëns1

1 Division of Cardiovascular & Diabetes Research, Section on Mechanisms of Thrombosis, Faculty of Medicine and Health, University of Leeds, Leeds, United Kingdom

A fraction of fibrinogen contains a differently spliced {gamma} chain called {gamma}', which presents itself mainly as heterodimer with the common {gamma}A chain as {gamma}A/{gamma}' fibrinogen. The {gamma}' chain differs from the {gamma}A chain in its C-terminus and has important functional implications for fibrinogen. The presence of the {gamma}' chain modulates thrombin and FXIII activity, influences clot architecture, and eliminates a platelet-binding site. Associations of {gamma}A/{gamma}' fibrinogen levels with arterial and venous thrombosis have been reported, indicating that the functional effects of {gamma}A/{gamma}' fibrinogen may contribute to the pathology of thrombosis. This review summarizes the key biologic aspects of this interesting variant of fibrinogen and discusses inconsistencies in current reports.


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