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Evidence for the activation of PAR‐2 by the sperm protease, acrosin: expression of the receptor on oocytes
Author(s) -
Smith Rosealee,
Jenkins Alison,
Lourbakos Afrodite,
Thompson Philip,
Ramakrishnan Vanitha,
Tomlinson Jim,
Deshpande Usha,
Johnson David A.,
Jones Roy,
Mackie Eleanor J.,
Pike Robert N.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02146-3
Subject(s) - acrosin , protease activated receptor 2 , chinese hamster ovary cell , trypsin , receptor , protease , microbiology and biotechnology , serine protease , chemistry , cleavage (geology) , protease activated receptor , hamster , mast cell , biology , biochemistry , sperm , acrosome , enzyme , enzyme linked receptor , immunology , paleontology , botany , thrombin , platelet , fracture (geology)
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.