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Vol. 53, Issue 2, 245-282, June 2001
Department of Physiology and Pharmacology, University of
Strathclyde, Strathclyde Institute for Biomedical Sciences,
Glasgow, United Kingdom
I. Introduction
II. Historical Perspectives
Cellular Effects of Thrombin and the
Cloning of the Thrombin Receptor, Proteinase-Activated Receptor-1
A. Cloning of a Thrombin Receptor
B. Receptor Structure and Mode of Activation
C. Thrombin/Receptor Interactions
III. Pharmacology of Proteinase-Activated Receptor-1
IV. Functional Responses to Proteinase-Activated Receptor-1
Activation
A. Platelet Aggregation
B. Endothelial Barrier Dysfunction, Chemotaxis, and Inflammation
C. Cell Growth and Division
D. Neuronal Cell Survival
E. Cardiovascular Responses
V. Proteinase-Activated Receptor-1-Mediated Cellular Signaling
A. Coupling to Heterotrimeric G-Proteins
B. Regulation of Kinase Signaling Cascades by Proteinase-Activated
Receptor-1
C. Mitogen-Activated Protein Kinase and Phosphatidyl Inositol-3
Kinase Cascades
D. G12-Dependent Proteinase-Activated Receptor-1
Signaling
VI. Desensitization of Proteinase-Activated Receptor-1
A. Phosphorylation and Internalization
B. Protein-Activated Receptor-1 Endocytosis and Trafficking
VII. Cloning of Proteinase-Activated Receptor-2
VIII. Functional Responses to Proteinase-Activated Receptor-2
Activation
A. Cardiovascular Responses
B. Proteinase-Activated Receptor-2 Involvement in Gastrointestinal
Function
C. Proteinase-Activated Receptor-2 Regulation of Skin Function
IX. Endogenous Activators of Proteinase-Activated Receptor-2
X. Pharmacology of Proteinase-Activated Receptor-2
XI. Proteinase-Activated Receptor-2-Mediated Intracellular
Signaling
XII. Proteinase-Activated Receptor-2 Desensitization
XIII. Identification and Function of Proteinase-Activated
Receptor-3 and Proteinase-Activated Receptor-4
A. Proteinase-Activated Receptor-3
B. Proteinase-Activated Receptor-4
XIV. Functional and Molecular Interactions Between
Proteinase-Activated Receptors
XV. Proteinase-Activated Receptors as Therapeutic Targets in
Disease States
A. Proteinase-Activated Receptors in Genetic Disorders
B. Proteinase-Activated Receptor-1-Mediated Thrombosis and Vascular
Remodeling
C. Cancer
D. Proteinase-Activated Receptors and Neurological Disorders
E. Proteinase-Activated Receptor-2 and Inflammatory Diseases
XVI. Future Perspectives
Acknowledgments
References
Proteinase-activated receptors are a recently described, novel family of seven-transmembrane G-protein-coupled receptors. Rather then being stimulated through ligand receptor occupancy, activation is initiated by cleavage of the N terminus of the receptor by a serine protease resulting in the generation of a new tethered ligand that interacts with the receptor within extracellular loop-2. To date, four proteinase-activated receptors (PARs) have been identified, with distinct N-terminal cleavage sites and tethered ligand pharmacology. In addition to the progress in the generation of PAR-1 antagonists, we describe the role of thrombin in such processes as wound healing and the evidence implicating PAR-1 in vascular disorders and cancer. We also identify advances in the understanding of PAR-1-mediated intracellular signaling and receptor desensitization. The cellular functions, signaling events, and desensitization processes involved in PAR-2 activation are also assessed. However, other major aspects of PAR-2 are highlighted, in particular the ability of several serine protease enzymes, in addition to trypsin, to function as activators of PAR-2. The likely physiological and pathophysiological roles for PAR-2 in skin, intestine, blood vessels, and the peripheral nervous system are considered in the context of PAR-2 activation by multiple serine proteases. The recent discovery of PAR-3 and PAR-4 as additional thrombin-sensitive PARs further highlights the complexity in assessing the effects of thrombin in several different systems, an issue that remains to be fully addressed. These discoveries have also highlighted possible PAR-PAR interactions at both functional and molecular levels. The future identification of other PARs and their modes of activation are an important future direction for this expanding field of study.
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T. Zhu, F. Sennlaub, M. H. Beauchamp, L. Fan, J. S. Joyal, D. Checchin, S. Nim, P. Lachapelle, M. Sirinyan, X. Hou, et al. Proangiogenic Effects of Protease-Activated Receptor 2 Are Tumor Necrosis Factor-{alpha} and Consecutively Tie2 Dependent Arterioscler. Thromb. Vasc. Biol., April 1, 2006; 26(4): 744 - 750. [Abstract] [Full Text] [PDF]
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