Interaction of Proteins of Epididymal Origin with Spermatozoa

Kohane, A. C.; Echeverría, Fernanda M. C. González; Piñeiro, Lucrecia; Blaquier, Jörge A.

doi:10.1095/biolreprod23.4.737

Cited by 138 publications

(82 citation statements)

References 30 publications

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“…Rat CRISP1 (rCRISP1) is synthesized in an androgen-dependent manner by the proximal segments of the epididymis, and associates with the sperm surface during epididymal maturation (Kohane et al, 1980a;Kohane et al, 1980b). Originally localized in the dorsal region of the sperm head, rCRISP1 migrates to the equatorial segment as the acrosome reaction occurs (Rochwerger and Cuasnicu, 1992).…”

Section: Epididymal Crisp1mentioning

confidence: 99%

Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction

Cohen¹,

Busso²,

Ros³

et al. 2008

Int. J. Dev. Biol.

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Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. CRISP1 (cysteine-rich secretory protein 1) is an epididymal protein thought to participate in gamete fusion through its binding to egg-complementary sites. Structure-function studies using recombinant fragments of CRISP1 as well as synthetic peptides reveal that its egg-binding ability resides in a 12 amino acid region corresponding to an evolutionary conserved motif of the CRISP family, named Signature 2 (S2). Further experiments analyzing both the ability of other CRISP proteins to bind to the rat egg and the amino acid sequence of their S2 regions show that the amino acid sequence of the S2 is needed for CRISP1 to interact with the egg. CRISP1 appears to be involved in the first step of sperm binding to the zona pellucida, identifying a novel role for this protein in fertilization. The observation that sperm testicular CRISP2 is also able to bind to the egg surface suggests a role for this protein in gamete fusion. Subsequent experiments confirmed the participation of CRISP2 in this step of fertilization and revealed that CRISP1 and CRISP2 interact with common egg surface binding sites. Together, these results suggest a functional cooperation between CRISP1 and CRISP2 to ensure the success of fertilization. These observations contribute to a better understanding of the molecular mechanisms underlying mammalian fertilization.

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Section: Epididymal Crisp1mentioning

confidence: 99%

Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction

Cohen¹,

Busso²,

Ros³

et al. 2008

Int. J. Dev. Biol.

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“…Previous results had indicated that about 70 % of the total protein DE associated with cauda epididymal spermatozoa was lost from the cells when these were capacitated for 4 h in utero (Kohane et al, 1980 It is accepted that the postacrosomal region of the sperm plasma membrane is a specialized structure through which fusion with the oocyte membrane is started (Bedford and Cooper, 1978 ;Salgi and Phillips, 1980). In addition, it is also well established that a considerable degree of species specificity is retained by this step of membrane fusion in many mammals (Hanada and Chang, 1972 (Tezon et al, 1982).…”

mentioning

confidence: 99%

On the role of epididymal factors in sperm fertility

Blaquier¹,

Cameo²,

Cuasnicú³

et al. 1988

Reprod. Nutr. Dévelop.

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Notwithstanding our improved descriptive knowledge of events occurring to mammalian sperm during epididymal maturation, the nature of the mechanisms involved in the development of such primary functions as forward motility (Bedford, 1975) and zona pellucida recognition (Saling, 1982) remain obscure.This review attempts to summarize the latest information produced by our laboratory in relation to the interaction of epididymal products with spermatozoa and the bearing that this interaction might have on sperm function.Our interest has been primarily focused on androgen-induced secretory epididymal proteins that associate to sperm during epididymal transit and that our group has described in rats (Cameo and Blaquier, 1976), hamsters (Gonzalez Echeverria, Cuasnic6 and Blaquier, 1982) and humans (Tezón et al., 1985b).Immature hamster sperm, obtained from the proximal segments of the epididymis, were used as a model to induce in vitro modifications of their functions (Cuasnicu et al., 1984a). Exposure of these spermatozoa to a preparation enriched with androgen-induced secretory proteins EP2-EP3 (Gonzalez Echeverria, was able to induce a significant increase in homologous zona pellucida binding (Cuasnicu et al., 1984b). Since zona binding seemed to be one of the functions developed by sperm during epididymal transit (Cuasnic6 et al., 1984a;Saling, 1982), our results were interpreted as reflecting the in vitro advancement of the maturational stage of these spermatozoa which was caused by the added epididymal preparation. Similarly, we were also able to show that immature sperm gained in fertilizing ability when pre-treated in vitro with the epididymal extract prior to in vivo or in vitro insemination (Gonzalez Echeverria et al., 1984).Our latest results confirm these preliminary findings and support the role of epididymal proteins in sperm maturation. Briefly, our studies show that the preparation of the epididymal proteins mentioned above, in which EP2-EP3 represented 16 % of the total protein, had a biological activity such that, on the average, treated sperm fertilized twice as many oocytes as their untreated controls (Gonzalez Echeverria et al., 1984 (Gwatkin, 1977)

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“…Current evidence suggests that specific secretory proteins in the epididymis play an important role in the development of motility (Acott and Hoskins, 1978) and surface properties of spermatozoa during their post-testicular maturation stage (Kohane et al, 1980 ;Jones et al, 1980 b ;Voglmayr et al, 1980 ;Orgebin-Crist et al, 1981). It has been demonstrated in rats and rabbits that different proteins are synthesized and secreted in different morphological regions of the epididymis and that some of these proteins are regulated specifically by androgen (Lea et al, 1978 ;Brooks and Higgins, 1980 ;Faye et al, 1980 ;Moore, 1980 ;Jones et al, 1980Jones et al, a, 1981.…”

mentioning

confidence: 99%

Identification of androgen-dependent proteins synthesized in vitro by the ram epididymis

Jones¹,

Fournier-Delpech²,

Sm³

1982

Reprod. Nutr. Dévelop.

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Interaction of Proteins of Epididymal Origin with Spermatozoa

Abstract: The present work was devoted to the study of certain aspects of the interaction of rat specific epididymal proteins (SEP) with spermatozoa.

Cited by 138 publications

References 30 publications

Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction

Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction

On the role of epididymal factors in sperm fertility

Identification of androgen-dependent proteins synthesized in vitro by the ram epididymis

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