Monoclonal antibody recognizing an apparent peptide epitope of human seminal plasma glycoprotein and exhibiting sperm immobilizing activity

Batova, Iglika N.; Kameda, K.; Hasegawa, Akiko; Koyama, Koji; Tsuji, Yoshiyuki; Isojima, Shinzo

doi:10.1016/0165-0378(90)90035-5

Cited by 9 publications

(11 citation statements)

References 17 publications

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“…Wright et al [50] have shown that an antibody against a human sperm protein, SP-10, blocks sperm-egg interactions. Human proteins that inhibit fertilization in vitro have been identified and several genes have been isolated [40,[51][52][53]. The appearance of this P34H sperm antigen in the proximal region of the human epididymis and the fact that it appears to be involved in the zona pellucida binding ability of the male gamete make this sperm protein an interesting candidate for understanding the physiological importance of human sperm transit through the epididymis.…”

Section: Discussionmentioning

confidence: 98%

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: 98%

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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“…In point of fact, at present, only a few polyclonal or monoclonal antibodies against human sperm proteins have been shown to impair fertilization [45][46][47][48][49][50][51][52][53]. When tested, the origin of the corresponding antigen was shown to be the testes except for the antigen described by Batova et al [48].…”

Section: Discussionmentioning

confidence: 96%

“…When tested, the origin of the corresponding antigen was shown to be the testes except for the antigen described by Batova et al [48]. Two of these antibodies have been shown to act at the ZP level [51][52], while four others inhibited sperm-oocyte binding and/or egg penetration [46][47][48][49][50][51][52][53].…”

Section: Discussionmentioning

confidence: 99%

FLB1, a Human Protein of Epididymal Origin that is Involved in the Sperm-Oocyte Recognition Process

Boué

Duquenne

Lassalle

et al. 1995

Biology of Reproduction

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CA6 antibody was selected out of a monoclonal antibody library raised against human sperm proteins primarily for its ability to recognize an epididymal antigen and to modify sperm adhesion to zona-free hamster oocytes. In the present study, CA6 was shown to decrease sperm binding to zona-free hamster and human oocytes by 40-92% and 38-48%, respectively. The corresponding protein, which was referred to as FLB1, was found to be secreted by the epididymis and to bind specifically to a human, macaque, and rodent subacrosomal sperm region. Western blotting revealed a molecular mass of 94 kDa in human epididymal extracts and of 100 kDa in human, macaque, mouse, rat, and hamster sperm, suggesting further modifications after its binding to sperm. An equivalent protein was not observed in human liver, ovary, testis, plasma, or epidermis. Two-dimensional electrophoresis showed that FLB1 is formed of two subunits with the same 47-kDa molecular mass and slightly different pI (5.8, 5.9). Microsequencing of the protein revealed a partial homology with human cytokeratins 1 and 10. These results suggest that FLB1 is an epididymis-specific cytokeratin-like protein that is involved in the sperm-oocyte recognition process.

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“…The earlier work on proteins involved the raising of polyclonal or monoclonal antibodies against human ejaculated spermatozoa [2,4], because coating proteins should be adherent to them; against proteins eluted from the ejaculated sperm surface [48], because eluted sperm proteins can promote zona binding [29]; and against human seminal fluid proteins (e.g. [31]), because secreted epididymal sperm-coating proteins are found in seminal plasma.…”

Section: Epididymal Proteins Involved In Sperm Maturationmentioning

confidence: 99%

Recent advances in sperm maturation in the human epididymis

Cooper¹

2002

Androl.

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A B S T R A C TAs spermatozoa move through the human epididymis they encounter a varied environment with respect to the proteins with which they come into contact. In the proximal epididymis sperm are subjected to the action of enzymes and exposure to proteins involved in membrane modification. In the middle region another set of proteins and enzymes predominates; those associated with sterol transport could modify the sperm membrane to permit the uptake of GPI-anchored zona binding proteins P34H and CD52. More distally sperm encounter increasing activities of lytic enzymes, proteins involved in both zona binding and oocyte fusion, the major maturation antigen CD52, antimicrobial activity and decapacitation factors, that help them to survive before ejaculation. Adherence of the proteins to different domains (e.g. anterior acrosome or equatorial acrosomal segment) may depend on the nature of the protein, the lipid composition of the particular membrane and the ionic environment in the epididymal lumen. The eventual location on a capacitated sperm (acrosomal membrane) or acrosome-reacted sperm (equatorial region) may dictate their role in, for example, zona-binding (P34H) or oocyte-binding (gp20). Both proteins and membranes may be modified during epididymal transit by the enzymes which may add to or remove carbohydrates and peptides from the sperm surface.

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Monoclonal antibody recognizing an apparent peptide epitope of human seminal plasma glycoprotein and exhibiting sperm immobilizing activity

Cited by 9 publications

References 17 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

FLB1, a Human Protein of Epididymal Origin that is Involved in the Sperm-Oocyte Recognition Process

Recent advances in sperm maturation in the human epididymis

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