Distribution of Seminal Antigens and Enzymes in the Rabbit Ductus Epididymidis

Wl, Johnson; Ag, Hunter

doi:10.2527/jas1979.491143x

Cited by 7 publications

(1 citation statement)

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“…Several methods have been used to demonstrate the presence of epididymal secretory proteins on spermatozoa. These include coincident migration of epididymal and sperm proteins on polyacrylamide gels [Cameo and Blaquier, 1976;Brooks and Higgins, 1980;Jones et al, 1980b;Gonzalez Echeverria et al, 19821, immunochemical techniques [Barker and Amann, 1970;Killian and Amann, 1973;Lea et al, 1978;Kohane et al, 1979Kohane et al, , 1980aJohnson and Hunter, 1979;Moore, 1980Moore, , 1981Bayard et al, 1981;Dravland and Joshi, 19811, radiolabeling of sperm surface proteins [Voglmayr et al, 1980[Voglmayr et al, , 1982Jones et al, 1981b1, and binding of '251-labeled proteins to sperm [Voglmayr et al, 1980, 19821. Each of these methods suffers from several drawbacks. For instance, when using '*'I-labeled epididymal luminal fluid proteins for binding studies, the origin (eg , testicular fluid, epididymis, bloodstream, loss from spermatozoa) of any particular luminal fluid protein is not known.…”

Section: Discussionmentioning

confidence: 99%

Selective binding of specific rat epididymal secretory proteins to spermatozoa and erythrocytes

Brooks¹

1983

Gamete Research

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Tissue pieces from the caput epididymidis of the rat were incubated in vitro with (35S) methionine to produce radioactive secretory proteins. The radioactive secretory proteins so formed were tested for their ability to bind to washed rat spermatozoa collected from the rete testis and cauda epididymidis, and to rat erythrocytes. The sperm and erythrocytes bound approximately 5% of the total radioactive protein. Binding was protein‐specific in that only selected proteins became associated with the cells. Binding was not cell‐specific, however, since testicular spermatozoa, caudal spermatozoa, and erythrocytes all bound the same proteins to a similar degree.

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Section: Discussionmentioning

confidence: 99%

Selective binding of specific rat epididymal secretory proteins to spermatozoa and erythrocytes

Brooks¹

1983

Gamete Research

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A cytochemical study on surface charges and lectin‐binding sites in epididymal and ejaculated spermatozoa of Macaca fascicularis

Dadoune

Reger

1984

Anat. Rec.

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Changes in electronegative and electropositive surface charges and in lectin receptors (concanavalin A and wheat germ agglutinin) were investigated on sperm plasma membranes of the monkey (Macaca fascicularis) during epididymal transit and after ejaculation. Electronegative charges at pH 1.8, which were uniformly distributed on the whole plasma membrane of caput epididymal spermatozoa, increased mainly on the postacrosomal cap and the tail during epididymal passage. Electropositive charges at pH 9 were simultaneously found on the whole cell surface of caput epididymal spermatozoa with a stronger labeling on the acrosomal apex, the postacrosomal cap, and the tail. These charges disappeared during passage through the epididymis corpus. The surface distribution of lectin receptors varied inversely during epididymal transit with an increase in concanavalin A receptors and a decrease in wheat germ agglutinin receptors. These data show that changes in the monkey sperm plasma membrane during epididymal maturation occur in the distal corpus of the epididymis.

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Changes in binding of a 27‐kilodalton chimpanzee cauda epididymal protein glycoprotein component to chimpanzee sperm

1987

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Motility patterns of caput epididymal chimpanzee sperm, caput epididymal chimpanzee sperm incubated in vitro with chimpanzee cauda epididymal fluid, and cauda epididymal chimpanzee sperm were assessed quantitatively. Sperm recovered from the caput epididymis showed no motility, whereas sperm recovered from cauda epididymis showed progressive forward motility. After incubation in cauda fluid, approximately 25% of caput epididymal sperm showed some motile activity. Electrophoretic analysis of 125I-labeled sperm plasma membrane preparations revealed that the surface of caput epididymal sperm, incubated in cauda fluid, was modified by the appearance of a major protein-glycoprotein surface component with an apparent molecular weight of 27 kilodaltons (kD). THis 27-kD component was not detected on caput epididymal sperm incubated in buffer or in caput fluid. However, it was present in cauda fluid and on cauda epididymal sperm. Binding to caput epididymal sperm was cell specific in that chimpanzee erythrocytes incubated in cauda fluid did not bind this 27-kD cauda fluid component. Motility patterns of ejaculated chimpanzee sperm and of ejaculated chimpanzee sperm incubated in the uterus of adult female chimpanzees also were assessed quantitatively. Ejaculated sperm showed progressive forward motility, whereas in utero incubated ejaculated sperm showed hyperactivated motility typical of capacitated sperm. Electrophoretic analysis of 125I-labeled sperm plasma membrane preparations revealed the loss of a 27-kD component from the surface of ejaculated sperm after in utero incubation. No significant change in the 125I-distribution pattern was detectable when ejaculated sperm were incubated in buffer. These results suggest that the lumenal fluid component, which becomes adsorbed to the surface of chimpanzee sperm during maturation in the epididymis and which is removed from the surface of mature chimpanzee sperm in the female reproductive tract, affects sperm motility.

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Distribution of Seminal Antigens and Enzymes in the Rabbit Ductus Epididymidis

Cited by 7 publications

References 0 publications

Selective binding of specific rat epididymal secretory proteins to spermatozoa and erythrocytes

Selective binding of specific rat epididymal secretory proteins to spermatozoa and erythrocytes

A cytochemical study on surface charges and lectin‐binding sites in epididymal and ejaculated spermatozoa of Macaca fascicularis

Changes in binding of a 27‐kilodalton chimpanzee cauda epididymal protein glycoprotein component to chimpanzee sperm

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