Subscribe to RSS
DOI: 10.1160/TH04-05-0275
The factor VII activating protease G511E (Marburg) variant and cardiovascular risk
Financial support: NPHSII was supported by the British Medical Research Council, the US National Institute of Health (grant NHLBI 33014) and Du Pont Pharma, Wilmington, USA. PJT, SEH, EH and KSR are supported by the British Heart Foundation (PG2000/015;RG 98/011). HI is part-supported by the Coronary Thrombosis Trust.Publication History
Received
05 May 2004
Accepted after resubmission
19 August 2004
Publication Date:
04 December 2017 (online)
Summary
A previous study had shown a strong relationship between a variant in factor VII activating protease (FSAP G511E) and advanced carotid atheroma. In-vitro, the variant has reduced fibrinolytic but normal pro-coagulant activity, which may constitute a prothrombotic state. The current study has addressed risk for coronary heart disease in a prospective study of cardio-vascular disorders (Northwick Park Heart Study II). An interactive effect upon risk was found between the 511E allele and elevated levels of cholesterol and triglyceride. Fibrinogen could substitute for triglyceride levels in this risk-interaction analysis. The findings support the proposal that the FSAP 511E allele exacerbates atherosclerosis or its clinical sequelae.
-
References
- 1 Choi-Miura N-H, Tobe T, Sumiya J-I. et al. Purification and characterization of a novel hyaluronan-binding protein (PHBP) from human plasma: it has three EGF, a kringle and a serine protease domain, similar to hepatocyte growth factor activator. J Biochem 1996; 119: 1157-65.
- 2 Hunfeld A, Etscheid M, Konig H. et al. Detection of a novel plasma serine protease during purification of vitamin K-dependent coagulation factors. FEBS Lett 1999; 456: 290-4.
- 3 Romisch J, Feussne A, Vermolen S. A protease isolated from human plasma activating factor VII independent of tissue factor. Blood Coagul Fibrinolysis 1999; 10: 471-9.
- 4 Romisch J, Vermolen S, Feussner A. et al. The factor VII activating protease cleaves singlechain plasminogen activators. Haemostasis 1999; 29: 292-9.
- 5 Kannemeier C, Al-Fakhri N, Preissner KT. et al. Factor VII-activating protease (FSAP) inhibits growth factor-mediated cell proliferation and migration of vascular smooth muscle cells. FASEB J 2004; 18: 728-30.
- 6 Kannemeier C, Feussner A, Stohr HA. et al. Factor VII and single-chain plasminogen activator-activating protease: activation and autoactivation of the proenzyme. Eur J Biochem 2001; 268: 3789-96.
- 7 Romisch J, Feussner A, Stohr HA. et al. Quantitation of the factor VIIand singlechain plasminogen activator-activating protease in plasmas of healthy subjects. Blood Coagul Fibrinolysis 2001; 12: 376-86.
- 8 Romisch J. Factor VII activating protease (FSAP): A novel protease in hemostasis. Biol Chem 2002; 383: 1119-24.
- 9 Romisch J, Feussner A, Nerlich C. et al. The frequent Marburg I polymorphism impairs the pro-urokinase activating potency of the factor VII activating protease (FSAP). Blood Coagul Fibrinolysis 2002; 13: 433-41.
- 10 Willeit J, Kiechl S, Weimer T. et al. Marburg I polymorphism of factor VII-activating protease: a prominent risk predictor of carotid stenosis. Circulation 2003; 107: 667-70.
- 11 Miller GJ, Bauer KA, Barzeger S. et al. Increased activation of the haemostatic system in men at high risk of fatal coronary heart disease. Thromb Haemost 1996; 75: 767-71.
- 12 Silveira A, Karpe F, Blomback M. et al. Activation of coagulation factor VII during alimentary lipemia. Arterioscler Thromb 1994; 14: 60-9.