In a previous article, we suggested that gp273, the ligand molecule for sperm-egg interaction in the bivalve mollusk Unio elongatulus has functional carbohydrate epitopes in common with a human zona pellucida glycoprotein, probably ZP3. We demonstrated that: 1) anti-gp273-purified immunoglobulin G (IgG), which recognizes a carbohydrate gp273 epitope including a Lewis a-like structure, interacts with a zona pellucida protein; 2) human sperm specifically bind to gp273; and 3) binding is reversed by anti-gp273 IgG. In the present study, we confirm this suggestion by demonstrating that heat-solubilized zonae pellucidae reverse gp273-human sperm binding, that gp273-binding sites are restricted to the acrosomal region, and that gp273 induces the acrosome reaction in human sperm. We also demonstrated that gp273-binding sites on human sperm function as signaling receptors because exposure of spermatozoa to this glycoprotein results in significant stimulation of protein kinase C (PKC) activity. Because the PKC inhibitor, bisindolylmaleimide I, reverses both PKC activation and the acrosome reaction, this kinase is a key component of the signal transduction pathway activated by gp273 and leading to the exocytotic event.
Gp273, the Ligand Molecule for Sperm-Egg Interaction in the Bivalve Mollusk, Unio elongatulus, Binds to and Induces Acrosome Reaction in Human Spermatozoa through a Protein Kinase C-Dependent Pathway / Delle Monache, S.; Flori, F.; Della Giovampaola, C.; Capone, A.; La Sala, Giovanni Battista; Rosati, F.; Colonna, R.; Tatone, C.; Focarelli, Riccardo. - In: BIOLOGY OF REPRODUCTION. - ISSN 0006-3363. - 69:6(2003), pp. 1779-1784. [10.1095/biolreprod.103.019976]
Gp273, the Ligand Molecule for Sperm-Egg Interaction in the Bivalve Mollusk, Unio elongatulus, Binds to and Induces Acrosome Reaction in Human Spermatozoa through a Protein Kinase C-Dependent Pathway
LA SALA, Giovanni Battista;
2003
Abstract
In a previous article, we suggested that gp273, the ligand molecule for sperm-egg interaction in the bivalve mollusk Unio elongatulus has functional carbohydrate epitopes in common with a human zona pellucida glycoprotein, probably ZP3. We demonstrated that: 1) anti-gp273-purified immunoglobulin G (IgG), which recognizes a carbohydrate gp273 epitope including a Lewis a-like structure, interacts with a zona pellucida protein; 2) human sperm specifically bind to gp273; and 3) binding is reversed by anti-gp273 IgG. In the present study, we confirm this suggestion by demonstrating that heat-solubilized zonae pellucidae reverse gp273-human sperm binding, that gp273-binding sites are restricted to the acrosomal region, and that gp273 induces the acrosome reaction in human sperm. We also demonstrated that gp273-binding sites on human sperm function as signaling receptors because exposure of spermatozoa to this glycoprotein results in significant stimulation of protein kinase C (PKC) activity. Because the PKC inhibitor, bisindolylmaleimide I, reverses both PKC activation and the acrosome reaction, this kinase is a key component of the signal transduction pathway activated by gp273 and leading to the exocytotic event.File | Dimensione | Formato | |
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