(Circulation. 2003;107:654.)
© 2003 American Heart Association, Inc.
Editorial |
From the University of Vermont, Departments of Biochemistry and Medicine, Burlington, Vt.
Correspondence to Kenneth G. Mann, PhD, University of Vermont, Departments of Biochemistry and Medicine, C-401 Given Building, 89 Beaumont Avenue, Burlington, VT 05405-0068. E-mail kenneth.mann@uvm.edu
Key Words: Editorials factor VII-activating protease coagulation fibrinolysis thrombosis
An extract of the first 250 words of the full text is provided, because this article has no abstract. |
The mechanistic description of a biological process first involves the development of an inventory of constituents that are presumed essential for the expression of the function. Although initially based on pathology, more frequently this inventory is developed by in vitro tests on the biochemistry, cell biology, or molecular genetics of a process. Elaborate schemes describing physiological reaction systems are frequently developed on the basis of these in vitro-developed inventories; however, it is becoming commonplace knowledge that the ultimate test of biological relevance, ie, a clinical phenotype, does not exist. In the coagulation system, this is evident in descriptions of the "intrinsic pathway" of coagulation, which take the view that surface contact activation of factor XII is the initial process.1,2 However, defects in the contact pathway produce no hemorrhagic phenotype.3 More recently, the use of transgenic animal models has provided a powerful tool for pathological phenotype recognition.4,5
See p 667
In the present issue of Circulation, the article titled "Marburg I Polymorphism of Factor VII-Activating Protease: A Prominent Risk Predictor of Carotid Stenosis" by Willeit and colleagues6 provides important observations that appear to require the inclusion of a novel serine protease, the factor VII-activated protease (FSAP), into the inventory of molecules associated with the coagulation/fibrinolytic process. FSAP was identified by a number of investigators and isolated either because of its affinity for immobilized hyaluronic acid7 or its presence in commercial prothrombin complex concentrates.8 The protein contains domain structures frequently associated with coagulation and fibrinolytic enzymes, including three "EGF"- like domains,
Related Article:
Circulation 2003 107: 667-670.
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