Isolation and characterization of specific rat epididymal proteins

Garberi, Juan C.; Kohane, A. C.; Cameo, Mónica S.; Blaquier, Jörge A.

doi:10.1016/0303-7207(79)90077-7

Cited by 91 publications

(58 citation statements)

References 28 publications

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“…A tight association with spermatozoa heads (Garberi et al, 1979;Cameo et al, 19861, and data suggesting the existence of a specific receptor (Brooks and Tiver, 1983;Wong and Tsang, 1982) have so far not been confirmed.…”

Section: Localization Of Crisp-1 In Different Tissuesmentioning

confidence: 93%

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: 93%

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

View full text Add to dashboard Cite

show abstract

“…CRISP1, the first identified member of the Cysteine-RIch Secretory Protein (CRISP) family, is an androgen-dependent glycoprotein synthetized by the epididymis in the rat (Cameo and Blaquier 1976;Garberi et al 1979Garberi et al , 1982, mouse (Mizuki and Kasahara 1992;Haendler et al 1993), human (Hayashi et al 1996;Kratzschmar et al 1996), and monkey (Sivashanmugam et al 1999;Ellerman et al 2010). This secretory protein associates with two different affinities with the surface of spermatozoa during epididymal maturation (Kohane et al 1980a, b).…”

Section: Crisp1mentioning

confidence: 97%

Acrosome Reaction as a Preparation for Gamete Fusion

Cuasnicú

Ros

Muñoz

et al. 2016

Sperm Acrosome Biogenesis and Function During Fertilization

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The acrosome reaction (AR) is a universal requisite for sperm-egg fusion. However, whereas through the animal kingdom fusion of spermatozoa with the egg plasma membrane occurs via the inner acrosomal membrane exposed after the AR, in eutherian mammals, gamete fusion takes place through a specialized region of the acrosome known as the equatorial segment (ES) which becomes fusogenic only after the AR is completed. This chapter focuses on the different molecular mechanisms involved in the acquisition of the fusogenicity of the ES after the AR. We provide an update of the knowledge about the proteins proposed to have a role in this process either by modifying cytoskeletal and/or membrane molecules or by relocalizing to the ES after the AR to subsequently participate in gamete fusion.

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“…The family of androgen-dependent proteins in the epididymis has been re ported under various designations, such as, androgen-controlled specific proteins (22), acidic epididymal glycoproteins (23), specific epididymal proteins (24), for ward motility proteins (25) or surface glycoproteins of spermatozoa (26). These proteins are acidic glycoprotein, and secreted mainly from the principal cells in the epithelium of the caput epididymis and attach to the surface of spermatozoa for their maturation.…”

Section: Discussionmentioning

confidence: 99%

Purification and Partial Characterization of Rat Epididymal Retinoic Acid-binding Protein, and Its Immunohistochemical Localization.

Nishiwaki

Kato

Okuno

et al. 1991

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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SummaryTwo types of retinoic acid-binding proteins, designated as epididymal retinoic acid-binding protein (ERABP) types A and B, have been purified to homogeneity from rat genital organs. ERABP types A and B had molecular weights of 19,000 and 18,500 and isoelectric points of 5.72 and 5.90, respectively. The absorption spectrum of ERABP complex with retinoic acid had two peaks at 277 and 354 nm, and showed similar uncorrected fluorescence spectra to that of cellular retinoic acid binding protein (CRABP). These ERABPs were identified as major androgen-dependent epididymal proteins by amino acid sequences anal yses. Furthermore, immunohistochemical examinations revealed that the ERABPs exist in the epithelium of the proximal portion of the epididymis and in the lumen of epididymal canal and seminal tract leading from the epididymis. The existence of ERABP strongly suggests that retinoic acid might be involved in the maturation of spermatozoa.

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Isolation and characterization of specific rat epididymal proteins

Cited by 91 publications

References 28 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

Acrosome Reaction as a Preparation for Gamete Fusion

Purification and Partial Characterization of Rat Epididymal Retinoic Acid-binding Protein, and Its Immunohistochemical Localization.

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