Evidence for the Activation of PAR-2 by the Sperm Protease, Acrosin: Expression of the Receptor on Oocytes
Document Type
Article
Publication Date
11-10-2000
Description
Proteinase-activated receptor-2 (PAR-2) is a member of a family of G-protein-coupled, seven-transmembrane domain receptors that are activated by proteolytic cleavage. The receptor is expressed in a number of different tissues and potential physiological activators identified thus far include trypsin and mast cell tryptase. Acrosin, a trypsin-like serine proteinase found in spermatozoa of all mammals, was found to cleave a model peptide fluorescent quenched substrate representing the cleavage site of PAR-2. This substrate was cleaved with kinetics similar to those of the known PAR-2 activators, trypsin and mast cell tryptase. Acrosin was also shown to induce significant intracellular calcium responses in Chinese hamster ovary cells stably expressing intact human PAR-2, most probably due to activation of the receptor. Immunohistochemical studies using PAR-2 specific antibodies indicated that the receptor is expressed by mouse oocytes, which suggests that acrosin may play additional role(s) in the fertilization process via the activation of PAR-2 on oocytes.
Citation Information
Smith, Rosealee; Jenkins, Alison; Lourbakos, Afrodite; Thompson, Philip; Ramakrishnan, Vanitha; Tomlinson, Jim; Deshpande, Usha; Johnson, David A.; Jones, Roy; Mackie, Eleanor J.; and Pike, Robert N.. 2000. Evidence for the Activation of PAR-2 by the Sperm Protease, Acrosin: Expression of the Receptor on Oocytes. FEBS Letters. Vol.484(3). 285-290. https://doi.org/10.1016/S0014-5793(00)02146-3 PMID: 11078894 ISSN: 0014-5793