Role of monoclonal antibody J-23 in inducing acrosome reactions in capacitated mouse spermatozoa

Aarons, David; Battle, Thierry; Boettger‐Tong, Holly; Poirier, Gary R.

doi:10.1530/jrf.0.0960049

Cited by 14 publications

(8 citation statements)

References 16 publications

(26 reference statements)

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“…The decrease of the zona pellucida binding ability of human spermatozoa incubated in presence of antibodies may be explained by an effect on the acrosome reaction [44]. For example, Aarons et al [45] have reported on a monoclonal antibodyJ-23 directed against a sperm antigen that has the property to induce the acrosome reaction of capacitated mouse spermatozoa. On the other hand, Kaplan and Naz [46] have shown that a monoclonal antibody produced against a fertilization antigen inhibits ionophore-induced acrosome reaction and blocks development of the hyperactivation state of human sperm cells.…”

Section: Discussionmentioning

confidence: 99%

Human Sperm-Zona Pellucida Interaction is Inhibited by an Antiserum against a Hamster Sperm Protein1

Boué

Bherer

Lamirande

et al. 1994

Biology of Reproduction

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During epididymal transit, mammalian spermatozoa acquire new surface antigens that may participate in gamete interaction. We have previously described a 26-kDa (P26h) epididymal hamster sperm protein that we propose to be involved in fertilization. In this study, we have searched for an antigenically related protein in the human, and have found that an anti-P26h antiserum recognizes a 34-kDa (P34H) protein on Western blot of human sperm proteins. Immunostaining showed that this protein is localized on the acrosomal cap of human epididymal spermatozoa but not on testicular gametes. The effect of the anti-P26h antiserum on the fertilizing ability of human spermatozoa was evaluated by use of a human zona pellucida binding assay. Compared to the preimmune serum, the antiserum caused a highly significant decrease in the number of sperm bound per zona pellucida. This inhibition was not due to the induction of a premature acrosomal reaction nor to an effect on the motility of the spermatozoa. The antiserum recognizing the P34H human sperm protein had no effect on gamete fusion as determined by the zona-free hamster test. Our results suggest that the human spermatozoon acquires an epididymal protein that shares a common epitope(s) with the P26h hamster sperm protein. The possible involvement of this human sperm antigen in the binding to the zona pellucida is discussed.

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Section: Discussionmentioning

confidence: 99%

Human Sperm-Zona Pellucida Interaction is Inhibited by an Antiserum against a Hamster Sperm Protein1

Boué

Bherer

Lamirande

et al. 1994

Biology of Reproduction

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“…Receptor aggregation. Cross-linking of sperm surface receptors in the absence of zona pellucida components can result in acrosome exocytosis (Macek et al, 1991;McKinnon et al, 1991;Aarons et al, 1992;Tesarik and Mendoza, 1993;Lassalle and Testart, 1996).…”

Section: Induction Of the Acrosome Reactionmentioning

confidence: 99%

Modelling human sperm-egg interactions in vitro: signal transduction pathways regulating the acrosome reaction

Benoff

1998

Molecular Human Reproduction

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Recent advances in characterizing sperm surface receptors and ion channels, when combined with the rapidly expanding knowlege 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-acetyglucosaminyl 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 voltagedependent calcium channel. The resulting elevated calcium signal depolymerizes the inter-membrane actin network and activates phospholipases, leading to an acrosome reaction.

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“…Saling (1989) proposed that, if aggregation is key, then immunoaggregation of zona binding sites, in the absence of zonae, should result in acrosomal exocytosis. Recently, acrosome reactions have been induced in murine sperm with antibodies to a number of the proposed zona binding sites (Macek et al, 1991;Leyton and Saling, 1991;Aarons et al, 1991Aarons et al, , 1992. The observations presented here demonstrate that aggregation of a proteinase inhibitor bound to the human sperm head results in acrosomal exocytosis.…”

mentioning

confidence: 58%

“…In recent years evidence has accumulated that the binding site on murine sperm of one such inhibitor may participate in capacitation, zonae binding, and the acrosome reaction (Poirier et al, 1986;Robinson et al, 1987;Boettger et al, 1989;Aarons et al, 1991Aarons et al, , 1992Boettger-Tong et al, 1992). The proteinase inhibitor (SVI) involved has a molecular weight of 6,400, is produced in the seminal vesicles, and binds to the acroso-0 1993 WILEY-LISS, INC. ma1 cap region of the sperm head at ejaculation (Poirier and Jackson, 1981;Irwin et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

Binding of a murine proteinase inhibitor to the acrosome region of the human sperm head

Boettger‐Tong¹,

Aarons

Biegler

et al. 1993

Molecular Reproduction Devel

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Proteinase inhibitors are present in the various glands, tissues, and secretions of the male reproductive tract. Some of these inhibitors bind to the acrosomal region of the sperm, and their release during in vitro or in utero incubation suggests that they may play a role in capacitation. In the mouse, the binding site for a trypsin-acrosin inhibitor, the acceptor, has been implicated in capacitation, zona binding, and the acrosome reaction. This presentation demonstrates that a component, molecular weight approximately 20,000, on the human sperm head may recognize the murine inhibitor. Furthermore, the acrosome reaction can be induced in capacitated human sperm by immunoaggregation of bound murine inhibitor. The data indicate that the proteinase inhibitor binding site on the human sperm head may, as with a similar site on murine sperm, play a role in the early events of fertilization.

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Role of monoclonal antibody J-23 in inducing acrosome reactions in capacitated mouse spermatozoa

Cited by 14 publications

References 16 publications

Human Sperm-Zona Pellucida Interaction is Inhibited by an Antiserum against a Hamster Sperm Protein1

Human Sperm-Zona Pellucida Interaction is Inhibited by an Antiserum against a Hamster Sperm Protein1

Modelling human sperm-egg interactions in vitro: signal transduction pathways regulating the acrosome reaction

Binding of a murine proteinase inhibitor to the acrosome region of the human sperm head

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