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  • Title: Evidence for the activation of PAR-2 by the sperm protease, acrosin: expression of the receptor on oocytes.
    Author: Smith R, Jenkins A, Lourbakos A, Thompson P, Ramakrishnan V, Tomlinson J, Deshpande U, Johnson DA, Jones R, Mackie EJ, Pike RN.
    Journal: FEBS Lett; 2000 Nov 10; 484(3):285-90. PubMed ID: 11078894.
    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 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.
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