Parstatin, a Novel Protease-Activated Receptor 1-Derived Inhibitor of Angiogenesis
Year: 2009
Type: article
Abstract: Angiogenesis, the process of forming new blood vessels, is a well established and clinically relevant feature of a variety of disease states. Whether blood vessels sprout in a given tissue environment depends on the balance between factors that stimulate angiogenesis and those that impede it. Potent pro-angiogenic factors such as vascular endothelial growth factor (VEGF) have been identified, validated, and successfully used in the clinic. Likewise, anti-angiogenic factors are also emerging as biologically relevant and therapeutically useful entities. PAR1 is a G protein-coupled receptor (GPCR) that participates in hemostasis and vascular development and that mediates the angiogenic activity of thrombin. PAR1 is activated through proteolytic cleavage of its first forty-one extracellular residues by a variety of proteases, most notably thrombin. However, little effort has focused on the forty-one-residue peptide fragment liberated during PAR1 activation. Tsopanoglou and colleagues have now demonstrated that this peptide, parstatin, has intriguing antiangiogenic activity, and, in a follow-up study, they demonstrate its potential pharmacological utility using a rat model of ischemic heart disease.
Source: Molecular Interventions
DOI: 10.1124/mi.9.4.4
Authors: M. B. Duncan, R. Kalluri
Institutions: Beth Israel Deaconess Medical Center, Harvard University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Awards: G2329611598, G2495637802, G2512559947, G4382730148, Regulation of Angiogenesis by Tumstatin, Matrix Microenvironment and Liver Fibrosis, G632314946, The Biology and Function of BMP-7 in the Kidney, Role of Fibroblasts in Cancer, Assembly of Type IV Collagen in Health and Disease, G9000059126
OpenAlex ID: W2043844298
