Characterization of Protease-activated Receptor-2 Immunoreactivity in Normal Human Tissues

作者：Michael R. D’Andrea, Claudia K. Derian, Didier J. Leturcq, Sherry M. Baker, Anders B. Brunmark, Ping Ling, Andrew L. Darrow, Rosemary J. Santulli, Lawrence F. Brass, Patricia Andrade‐Gordon · 发表于：Journal of Histochemistry & Cytochemistry · 年份：1998 · DOI：10.1177/002215549804600204 · 被引用次数：323 · 研究领域：Blood Coagulation and Thrombosis Mechanisms、Coagulation, Bradykinin, Polyphosphates, and Angioedema、Protease and Inhibitor Mechanisms

PAR-2 is a second member of a novel family of G-protein-coupled receptors characterized by a proteolytic cleavage of the amino terminus, thus exposing a tethered peptide ligand that autoactivates the receptor. The physiological and/or pathological role(s) of PAR-2 are still unknown. This study provides tissue-specific cellular localization of PAR-2 in normal human tissues by immunohistochemical techniques. A polyclonal antibody, PAR-2C, was raised against a peptide corresponding to the amino terminal sequence SLIGKVDGTSHVTGKGV of human PAR-2. Significant PAR-2 immunoreactivity was detected in smooth muscle of vascular and nonvascular origin and stromal cells from a variety of tissues. PAR-2 was also present in endothelial and epithelial cells independent of tissue type. Strong immunolabeling was observed throughout the gastrointestinal tract, indicating a possible function for PAR-2 in this system. In the CNS, PAR-2 was localized to many astrocytes and neurons, suggesting involvement of PAR-2 in neuronal function. A role for PAR-2 in the skin was further supported by its immunolocalization in the epidermis. PAR-2C antibody exemplifies an important tool to address the physiological role(s) of PAR-2.