The G534E polymorphism of the gene encoding the factor VII-activating protease is associated with cardiovascular risk due to increased neointima formation

J Exp Med. 2006 Dec 25;203(13):2801-7. doi: 10.1084/jem.20052546. Epub 2006 Dec 4.

Abstract

The G534E polymorphism (Marburg I [MI]) of factor VII-activating protease (FSAP) is associated with carotid stenosis and cardiovascular disease. We have previously demonstrated that FSAP is present in atherosclerotic plaques and it is a potent inhibitor of vascular smooth muscle proliferation and migration in vitro. The effect of wild-type (WT)- and MI-FSAP on neointima formation in the mouse femoral artery after wire-induced injury was investigated. Local application of WT-FSAP led to a 70% reduction in the neointima formation, and this effect was dependent on the protease activity of FSAP. MI-FSAP did not inhibit neointima formation in vivo. This is due to a reduced proteolytic activity of MI-FSAP, compared to WT-FSAP, toward platelet-derived growth factor BB, a key mediator of neointima development. The inability of MI-FSAP to inhibit vascular smooth muscle accumulation explains the observed linkage between the MI-polymorphism and increased cardiovascular risk. Hence, FSAP has a protective function in the vasculature, and analysis of MI polymorphism is likely to be clinically relevant in restenosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Amino Acid Chloromethyl Ketones / pharmacology
  • Animals
  • Becaplermin
  • Catalysis
  • Cell Proliferation / drug effects
  • Coronary Restenosis / genetics*
  • Coronary Restenosis / prevention & control
  • Extracellular Signal-Regulated MAP Kinases / metabolism
  • Female
  • Gene Expression
  • Heparin / metabolism
  • Humans
  • Intercellular Signaling Peptides and Proteins / pharmacology
  • Liver / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Myocytes, Smooth Muscle / cytology
  • Myocytes, Smooth Muscle / drug effects
  • Myocytes, Smooth Muscle / metabolism
  • Phosphorylation
  • Platelet-Derived Growth Factor / metabolism
  • Platelet-Derived Growth Factor / pharmacology
  • Polymorphism, Genetic*
  • Protein Binding
  • Proto-Oncogene Proteins c-sis
  • Serine Endopeptidases / genetics*
  • Serine Endopeptidases / metabolism
  • Serine Endopeptidases / pharmacology
  • Serine Proteinase Inhibitors / pharmacology
  • Tunica Intima / drug effects
  • Tunica Intima / metabolism*
  • Tunica Intima / pathology
  • Urokinase-Type Plasminogen Activator / metabolism
  • von Willebrand Factor / metabolism

Substances

  • Actins
  • Amino Acid Chloromethyl Ketones
  • Intercellular Signaling Peptides and Proteins
  • Platelet-Derived Growth Factor
  • Proto-Oncogene Proteins c-sis
  • Serine Proteinase Inhibitors
  • von Willebrand Factor
  • Becaplermin
  • Heparin
  • Extracellular Signal-Regulated MAP Kinases
  • HABP2 protein, human
  • Serine Endopeptidases
  • Urokinase-Type Plasminogen Activator
  • phenylalanyl-prolyl-arginine-chloromethyl ketone