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Abstract
In a previous paper we suggested that gp273, the ligand
molecule for sperm egg interaction in the bivalve mollusc
Unio elongatulus has functional carbohydrate
epitopes in common with a human zona pellucida
glycoprotein, probably ZP3. We demonstrated that 1)
anti-gp273 purified IgG that recognizes a carbohydrate
gp273 epitope including a Lewisa-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 signalling receptors since exposure of
spermatozoa to this glycoprotein results in significant
stimulation of PKC activity. Since the PKC inihibitor,
BIM, 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.
Key words:
Acrosome reaction
Fertilization
Kinases
Signal transduction
Sperm
This article has been cited by other articles:
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S. Canovas, P. Coy, and E. Gomez First Steps in the Development of a Functional Assay for Human Sperm Using Pig Oocytes J Androl, March 1, 2007; 28(2): 273 - 281. [Abstract] [Full Text] [PDF] |
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