The pleiotropic role of the fibrinogen gamma' chain in hemostasis.

Shirley Uitte de Willige, Kristina F Standeven, Helen Philippou, Robert A S Ariëns

Journal: Blood 2009;114(19):3994-4001

PMID: 19687509

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Abstract

A fraction of fibrinogen contains a differently spliced gamma chain called gamma', which presents itself mainly as heterodimer with the common gammaA chain as gammaA/gamma' fibrinogen. The gamma' chain differs from the gammaA 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 gammaA/gamma' fibrinogen levels with arterial and venous thrombosis have been reported, indicating that the functional effects of gammaA/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.

Address: Division of Cardiovascular & Diabetes Research, Section on Mechanisms of Thrombosis, Faculty of Medicine and Health, University of Leeds, Leeds LS2 9JT, United Kingdom. [email protected]

DOI: 10.1182/blood-2009-05-217968

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MeSH Terms: Alternative Splicing, Amino Acid Sequence, Dimerization, Factor XIII, Fibrinogens, Abnormal, Hemostasis, Humans, Microscopy, Electron, Scanning, Molecular Sequence Data, Platelet Aggregation, Protein Structure, Quaternary, Recombinant Proteins, Risk Factors, Thrombin, Thrombosis