Molecular Human Reproduction, Vol 4, 453-471, Copyright © 1998 by Oxford University Press
S Benoff
Recent advances in characterizing sperm surface receptors and ion channels,
when combined with the rapidly expanding knowledge of interactions among
second messenger systems in somatic cells, permit formulation of a
tentative molecular mechanism for the regulation of the human sperm
acrosome reaction. As spermatozoa pass through the cumulus mass,
progesterone binds to its sperm surface receptor, alkalinizes the sperm
head cytosol and potentiates changes in intracellular ionized calcium.
Primary binding of spermatozoa to egg involves receptors for mannosyl,
N-acetylglucosaminyl and, possibly, fucosyl residues of the glycosylated
zona protein, ZP3. These receptors aggregate on multivalent ligand binding,
migrate to the equatorial region along an actin filament network formed
between the plasma and acrosomal membranes during capacitation, and
activate a G protein/protein kinase A/protein kinase C second messenger
system and a secondary proteolysis signal. Binding of a receptor tyrosine
kinase to ZP3 amino acid residues simultaneous with the sugar recognition
event triggers tyrosine phosphorylation signalling. All signals combine to
open a voltage-dependent calcium channel. The resulting elevated calcium
signal depolymerizes the inter-membrane actin network and activates
phospholipases, leading to an acrosome reaction.
REVIEW, ACADEMIC
Modelling human sperm-egg interactions in vitro: signal transduction pathways regulating the acrosome reaction
Department of Obstetrics and Gynecology, North Shore University Hospital-New York University Medical College, Manhasset 11030, USA.
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