Journal article

Evidence for the activation of PAR-2 by the sperm protease, acrosin: expression of the receptor on oocytes

R Smith, A Jenkins, A Lourbakos, P Thompson, V Ramakrishnan, J Tomlinson, U Deshpande, DA Johnson, R Jones, EJ Mackie, RN Pike

FEBS Letters | ELSEVIER SCIENCE BV | Published : 2000

Abstract

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 ..

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University of Melbourne Researchers