Rat epididymis‐specific sperm maturation antigens. I. Evidence that the 26 kD 4E9 antigen found on rat caudal epididymal sperm tail is derived from a protein secreted by the epididymis

Moore, Abby; Ensrud, Kathy M.; White, Thomas W.; Frethem, Chris; Hamilton, David W.

doi:10.1002/mrd.1080370209

Cited by 38 publications

(35 citation statements)

References 37 publications

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“…Other results published recently (Moore et al, 1994) suggest an association with the tail region of spermatozoa. Too few data are available about mouse CRISP-1 at present to clarify the situation.…”

Section: Localization Of Crisp-1 In Different Tissuesmentioning

confidence: 87%

Mouse androgen‐dependent epididymal glycoprotein crisp‐1 (DE/AEG): Isolation, biochemical characterization, and expression in recombinant form

Eberspaecher¹,

Roosterman²,

Krätzschmar³

et al. 1995

Molecular Reproduction Devel

100

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In the rat, the secretory glycoprotein DE/AEG is one of the main constituents of the epididymal fluid. We have recently reported the cloning of the cDNA for the related cysteine-rich secretory protein-1 (CRISP-1) from murine epididymis (Haendler et al., 1993; Endocrinology 133:192-198). The protein has now been isolated from the same organ and its N-terminal amino acid sequence has been determined. CRISP-1 exhibited an isoelectric point of approximately 6.8. High levels of CRISP-1 antigen were detected in the corpus and cauda of the epididymis, vas deferens, seminal vesicle, prostate, and in the salivary gland by immunohistochemistry. A quantitative analysis of the cauda epididymal fluid by sandwich ELISA revealed that CRISP-1 represented approximately 15% of the total protein. For heterologous expression, the CRISP-1 coding sequence was introduced into the pMPSV/CMV vector before transfection of baby hamster kidney (BHK) cells and selection with puromycin and neomycin. Expression in insect cells was achieved by co-transfection of Sf9 cells with a transfer vector and baculovirus DNA. Recombinant CRISP-1 was isolated in quantities sufficient for structural analysis. Ethyl maleimide treatment showed that all 16 cysteines were engaged in disulfide bonds. Proteolytic digestion demonstrated that the six cysteines localized in the N-terminal moiety formed three bonds with each other, suggesting the existence of two discrete domains in the protein.

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Section: Localization Of Crisp-1 In Different Tissuesmentioning

confidence: 87%

Mouse androgen‐dependent epididymal glycoprotein crisp‐1 (DE/AEG): Isolation, biochemical characterization, and expression in recombinant form

Eberspaecher¹,

Roosterman²,

Krätzschmar³

et al. 1995

Molecular Reproduction Devel

100

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“…Some of the surface differences demonstrated by spermatozoa as they migrate through the epididymis have been shown to result from the binding of epididymal secretory proteins to the sperm surface, by using approaches such as: coincident migration of epididymal and sperm proteins on polyacrylamide gels (Rankin et al 1989, Srivastava & Olson 1991, Srivastav 2000; radiolabelling techniques using both in vitro and in vivo binding of labelled epididymal proteins to spermatozoa (Moore et al 1994); direct binding of protein to spermatozoa (Fournier-Delpech et al 1997); and immunochemical techniques (Xu et al 1997, Gatti et al 2000 in several species, including both non-human primates (Frö hlich & Young 1996) and human (Tezon et al 1985, Focarelli et al 1998, Martin Ruiz et al 1998, Liu et al 2000.…”

Section: Discussionmentioning

confidence: 99%

Partial characterization, sperm association and significance of N- and O-linked glycoproteins in epididymal fluid of rhesus monkeys (Macaca mulatta)

Srivastav

Singh²,

Chandra³

et al. 2004

Reproduction

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The present study investigated regional modifications of glycosylation status, sperm association and functional significance of N-and O-linked glycoproteins in epididymal luminal fluid of the rhesus monkey (Macaca mulatta). The predominant glycoproteins of the epididymal luminal fluid that increase in the extent of glycosylation or unmasking of exposed epitopes in a region-specific, maturation-dependent manner, included those of 150, 116, 68, 64, 58 (N-and O-linked) and 170 kDa (O-linked). The higher expression of 40 (N-linked), 38 (N-and O-linked) and 60, 56 and 33 kDa (O-linked) glycoproteins in the proximal caput epididymal fluid was followed by alteration or reorganization of 60, 38 and 33 kDa (O-linked) glycoproteins in the distal segments of the epididymis. The association of epididymal fluid glycoproteins with maturing spermatozoa was identified by generating polyclonal antiserum against monkey caudal sperm membrane in female albino rabbits. The antiserum crossreacted strongly with 58 and 33 kDa epididymal fluid glycoproteins of monkeys and also reacted with 116, 68, 58, 56 and 33 kDa glycoproteins from Triton X-100 extracts of human spermatozoa, indicating the presence of antigenically related components in both species. The functional significance of epididymal fluid glycoproteins in sperm functions was investigated by raising antiserum against a heavily glycosylated 58 kDa glycoprotein (MEF1) of caudal epididymal fluid, which crossreacted with the Triton X-100 extracts of epididymal spermatozoa of monkey and ejaculated human spermatozoa on immunoblots. In an in vitro micro-sperm agglutination assay, anti-MEF1 serum agglutinated both rat caudal epididymal spermatozoa and human spermatozoa. MEF1 seemed to be involved in fertilization as demonstrated by inhibition of fertility (100%) in female albino rabbits and rats immunized with this protein. A sperm-agglutinating 58 kDa glycoprotein of rhesus monkey epididymis with functional significance in fertility was identified, thus indicating that it is a potential candidate for contraceptive vaccine development.

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“…Specifically, rat (protein E) and mouse CRISP1 irreversibly associate with the sperm plasma membrane during epididymal transit. 56,72,73 and remain localized to the fusogenic region of the sperm head after the acrosome reaction. 52 A similar localization was observed on human sperm, 44,74 and CRISP1 antibodies were capable of significantly reducing the number of penetrating human sperm in the hamster oocyte penetration assay.…”

Section: 71mentioning

confidence: 99%

The role of cysteine-rich secretory proteins in male fertility

Koppers¹,

Reddy²,

O'Bryan³

2010

Asian J Androl

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The cysteine-rich secretory proteins (CRISPs) are a subgroup of the CRISP, antigen 5 and Pr-1 (CAP) protein superfamily, and are found only in vertebrates. They show a strong expression bias to the mammalian male reproductive tract and the venom of poisonous reptiles. Within the male reproductive tract CRISPs have been implicated in many aspects of male germ cell biology spanning haploid germ cell development, epididymal maturation, capacitation, motility and the actual processes of fertilization. At a structural level, CRISPs are composed of two domains, a CAP domain, which has been implicated in cell-cell adhesion, and a CRISP domain, which has been shown to regulate several classes of ion channels across multiple species. Herein, we will review the current literature on the role of CRISPs in male fertility, and by inference to related non-mammalian protein, infer potential biochemical functions.

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Rat epididymis‐specific sperm maturation antigens. I. Evidence that the 26 kD 4E9 antigen found on rat caudal epididymal sperm tail is derived from a protein secreted by the epididymis

Cited by 38 publications

References 37 publications

Mouse androgen‐dependent epididymal glycoprotein crisp‐1 (DE/AEG): Isolation, biochemical characterization, and expression in recombinant form

Mouse androgen‐dependent epididymal glycoprotein crisp‐1 (DE/AEG): Isolation, biochemical characterization, and expression in recombinant form

Partial characterization, sperm association and significance of N- and O-linked glycoproteins in epididymal fluid of rhesus monkeys (Macaca mulatta)

The role of cysteine-rich secretory proteins in male fertility

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