TRPM8 in mouse sperm detects temperature changes and may influence the acrosome reaction

2011 ◽  
Vol 226 (6) ◽  
pp. 1620-1631 ◽  
Author(s):  
Pablo Martínez-López ◽  
Claudia L. Treviño ◽  
José Luis de la Vega-Beltrán ◽  
Gerardo De Blas ◽  
Esteban Monroy ◽  
...  
Keyword(s):  
Acrosome Reaction ◽  
Temperature Changes ◽  
Mouse Sperm

scholarly journals Evidence that aggregation of mouse sperm receptors by ZP3 triggers the acrosome reaction.

1989 ◽  
Vol 108 (6) ◽  
pp. 2163-2168 ◽  
Author(s):  
L Leyton ◽  
P Saling
Keyword(s):  
Acrosome Reaction ◽  
Specific Binding ◽  
Polyclonal Antibodies ◽  
Subsequent Treatment ◽  
Mouse Sperm ◽  
Fab Fragments ◽  
Sperm Binding ◽  
Extracellular Signal ◽  
Acrosomal Exocytosis ◽  
Rabbit Igg

In the mouse, considerable evidence indicates that initial sperm binding to the zona pellucida (ZP) is mediated by ZP3. In addition, this same glycoprotein is also responsible for inducing the acrosome reaction (AR). Whereas the O-linked oligosaccharides of ZP3 appear to mediate sperm-ZP binding, the portion of ZP3 bearing AR activity has not been defined. To try to understand the bifunctional role of ZP3 (binding and AR inducing activities), we have examined the hypothesis that ZP3 aggregates sperm receptor molecules. By analogy with findings in a variety of other extracellular signal transducing systems, including receptors for growth factors and insulin, this aggregation event could initiate the cascade resulting in the AR. To test this hypothesis, we have generated monospecific polyclonal antibodies against ZP2 and against ZP3, and examined the effects of these probes on capacitated sperm incubated in the absence or presence of various ZP protein preparations. For some experiments, we have used proteolytic fragments of ZP3, a preparation known to retain specific binding, but not AR-inducing, activity. We show here that capacitated mouse sperm, incubated with ZP glycopeptides, displayed ARs when incubated subsequently with anti-ZP3 IgG; ARs did not occur when parallel sperm samples were incubated with anti-ZP2 IgG or with anti-ZP3 Fab fragments. When capacitated sperm were treated successively, with (a) ZP3 glycopeptides, (b) anti-ZP3 Fab fragments, and (c) goat anti-rabbit IgG, ARs occurred in the majority of sperm. An alternative approach to examine this hypothesis used ZP proteins obtained from tubal eggs treated previously with bioactive phorbol diester (12-O-tetradecanoyl phorbol-13-acetate [TPA]). This preparation arrests capacitated sperm in an intermediate state of the AR. We demonstrate here that these sperm can be induced to undergo a complete AR by subsequent treatment with anti-ZP3 IgG. Together, these findings are consistent with the hypothesis under examination, and suggest that the aggregation of sperm molecules recognized by ZP3 glycopeptides or by TPA-treated ZP is sufficient to trigger the events that occur during acrosomal exocytosis.

scholarly journals Soluble adenylyl cyclase inhibition prevents human sperm functions essential for fertilization

2021 ◽  
Author(s):  
Melanie Balbach ◽  
Lubna Ghanem ◽  
Thomas Rossetti ◽  
Navpreet Kaur ◽  
Carla Ritagliati ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
Acrosome Reaction ◽  
Human Sperm ◽  
Comprehensive Analysis ◽  
Multiple Points ◽  
Soluble Adenylyl Cyclase ◽  
Mouse Sperm ◽  
On Demand ◽  
Sperm Functions

AbstractSoluble adenylyl cyclase (sAC: ADCY10) is essential for activating dormant sperm. Studies of freshly dissected mouse sperm identified sAC as needed for initiating capacitation and activating motility. We now use an improved sAC inhibitor, TDI-10229, for a comprehensive analysis of sAC function in human sperm. Unlike dissected mouse sperm, human sperm are collected post-ejaculation, after sAC activity has already been stimulated. Even in ejaculated human sperm, TDI-10229 interrupts stimulated motility and capacitation, and it prevents acrosome reaction in capacitated sperm. At present, there are no non-hormonal, pharmacological methods for contraception. Because sAC activity is required post-ejaculation at multiple points during the sperm’s journey to fertilize the oocyte, sAC inhibitors define candidates for non-hormonal, on-demand contraceptives suitable for delivery via intravaginal devices in females.

Mouse sperm patch-clamp recordings reveal single Cl− channels sensitive to niflumic acid, a blocker of the sperm acrosome reaction

FEBS Letters ◽  
1998 ◽  
Vol 426 (1) ◽  
pp. 47-51 ◽  
Author(s):  
F Espinosa ◽  
J.L de la Vega-Beltrán ◽  
I López-González ◽  
R Delgado ◽  
P Labarca ◽  
...  
Keyword(s):  
Patch Clamp ◽  
Acrosome Reaction ◽  
Niflumic Acid ◽  
Mouse Sperm ◽  
Cl Channels ◽  
Sperm Acrosome Reaction ◽  
Sperm Acrosome

Relationship between the M42 antigen of mouse sperm and the acrosome reaction induced by ZP3

1989 ◽  
Vol 132 (1) ◽  
pp. 174-178 ◽  
Author(s):  
Lisette Leyton ◽  
Athy Robinson ◽  
Patricia Saling
Keyword(s):  
Acrosome Reaction ◽  
Mouse Sperm

Interactions between gametes leading to fertilization: the sperm's eye view

1995 ◽  
Vol 7 (4) ◽  
pp. 927 ◽  
Author(s):  
BT Storey
Keyword(s):  
Plasma Membrane ◽  
Acrosome Reaction ◽  
Mammalian Species ◽  
Sperm Chromatin ◽  
Peptide Backbone ◽  
Mouse Sperm ◽  
Gamete Interactions ◽  
Sperm Plasma Membrane ◽  
Sperm Penetration ◽  
Strong Candidate

Sexual reproduction requires that the gamete carrying the male-derived haploid chromatin join with the gamete carrying the female-derived haploid chromatin during fertilization to produce the diploid zygote. To accomplish this feat, the sperm must not only meet the egg, it must recognize the egg and be recognized in turn by the egg, and in the end must enter and be engulfed by the egg. In this selective overview of gamete interactions that lead to fertilization, encounters of three kinds, followed by the finale of gamete fusion, are considered from the sperm's viewpoint, with particular emphasis on the mammalian species with the mouse as the principal model. The first encounter is with the zona pellucida of the egg, to whose surface the sperm must bind. Mouse sperm appear to have four binding sites for zona ligands. Three interact with sugar moieties of the oligosaccharide chains of the mouse zona glycoprotein ZP3; the fourth binds a peptide backbone arginine. Capacitation is not required for this encounter, but is obligate for the second encounter--induction of the acrosome reaction in the bound sperm. The acrosome reaction is an exocytotic process that makes available the enzymatic machinery needed for sperm penetration the zona which is the end point of a sequence of reactions directed by intracellular signalling systems. In mouse sperm, these systems are presumed to be activated by ligands on ZP3 binding to ligand-specific sperm receptors with consequent aggregation of receptors. No receptor has been identified with certainty, nor have candidates for putative ZP3 ligands been identified. Completion of the acrosome reaction allows the sperm to penetrate the zona and, bind to the egg plasma membrane, thereby completing the third encounter. In the mouse, a 94-kDa protein appears essential for this binding. In the guinea-pig, a sperm plasma membrane protein (formerly PH-30, now fertilin), is a strong candidate for the mediator of the fusion process by which the egg engulfs the sperm. Decondensation of the sperm chromatin reverses the remarkable packing of DNA organized by sperm protamines. Mitochondrial DNA is also engulfed by the egg; the question of whether this DNA makes a small finite, or null, contribution to cytosolic inheritance is still in debate. The puzzles attending these encounters are presented as reminders of the intricacy and fascination, as well as of the vital necessity, of gamete interaction.

QSOX2, a FAD-Dependent Sulfhydryl Oxidase, Can Agglutinate Mouse Sperm and Inhibit Acrosome Reaction.

2011 ◽  
Vol 85 (Suppl_1) ◽  
pp. 503-503
Author(s):  
Sheng-Hsiang Li ◽  
Chung-Hao Lu ◽  
Hsiao-Ho Chang ◽  
Robert Kuo-Kuang Lee
Keyword(s):  
Acrosome Reaction ◽  
Sulfhydryl Oxidase ◽  
Mouse Sperm

scholarly journals Epididymal Maturation and the Acrosome Reaction in Mouse Sperm: Response to Zona Pellucida Develops Coincident with Modification of M42 Antigen1

1988 ◽  
Vol 38 (1) ◽  
pp. 221-233 ◽  
Author(s):  
Katherine A. Lakoski ◽  
Christopher P. Carron ◽  
Christine L. Cabot ◽  
Patricia M. Saling
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Mouse Sperm ◽  
Epididymal Maturation
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