Biochemical composition of human vas deferens

Setty, B.S.; Chowdhury, S.R.; Jehan, Q

doi:10.1016/0010-7824(74)90045-6

Cited by 6 publications

(2 citation statements)

References 12 publications

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“…Its epithelial cells, in the proximal region, contain an abundance of rough endoplasmic reticulum and an extensive array of Golgi complexes (Flickinger, 1973;Hamilton, 1975). There is also some evidence that a large number of enzymes and other substances are present in the secretions of vas deferens of various mammalian species (Setty et al, 1974). How¬ ever, knowledge of the extent to which the vas deferens is dependent on androgens for its normal function is limited.…”

Section: Introductionmentioning

confidence: 99%

Preliminary characterization, androgen-dependence and ontogeny of an abundant protein from mouse vas deferens

Taragnat¹,

Berger²,

Jean³

1988

Reproduction

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Polyacrylamide gel electrophoresis analysis revealed that the vas deferens of adult mouse contains a major protein. Mouse vas deferens protein is a basic glycoprotein with a molecular weight of 34,800 +/- 300. The protein represents 17 +/- 0.7% and 42 +/- 2.4% of soluble proteins from homogenate and luminal fluid respectively, an estimate based on densitometric scanning of polyacrylamide gels. The protein originated from the vas deferens since it was not detected in blood plasma or in sexual organs and it was still present after ligation of the epididymis. Changes in androgen status of the animal markedly affected the vas deferens protein. After castration a progressive decrease in the protein was observed and its relative percentage dropped to 2 +/- 0.4% after 45 days. The concentration of the protein returned to precastration levels after 2 weeks of testosterone treatment but oestradiol, progesterone and corticosterone were ineffective in this respect. The vas deferens protein was not synthesized in significant amounts until animals were 20 days old and its concentration increased rapidly from 20 to 30 days in concert with the pubertal increase of androgens in the vas deferens.

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Section: Introductionmentioning

confidence: 99%

Preliminary characterization, androgen-dependence and ontogeny of an abundant protein from mouse vas deferens

Taragnat¹,

Berger²,

Jean³

1988

Reproduction

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“…However, since in vasectomized men spermatozoa do survive in the distal region of the vas without loosing their fertilizing capacity (Risley 1963), the vas is probably a physiologically active organ involved in sperm maturation and survival (Orgebin-Crist 1969;Young 1970;Handton 19'75). There is some evidence that the vas deferens is involved in a variety of functions such as the metabolism of sex steroids (Hamilton & Fawcett 1970;Dupuy et al 1979;Kumari et al 1980;Seethalakhsmi et al 1982;Setty et al 1983) which can be transferred into the prostatic circulation in both the dog and man (Pierrepoint et al 1980), and the secretion and resorption of fluid and various substances (Setty et al 1974). At ejaculation, certain components of the epididymal, ampullar, prostatic and vesicular fluids are added to the plasma membrane of spermatozoa (Balerna et al 1984;Russel et al 1984).…”

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confidence: 99%

Identification and androgen‐dependence of proteins in the mouse vas deferens

1986

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Proteins from 'luminal fluid' or from a homogenate of whole vas deferens were analysed by polyacrylamide gel electrophoresis under denaturing conditions. Four major bands with apparent molecular weights of 34.5, 36, 38 and 180 Kilodaltons (K) were observed in homogenates. In 'luminal fluid' the same protein pattern was observed except that 38 K band was missing. These four major bands probably originated from the vas deferens as they were not detected in plasma and were still present after ligation between the epididymis and vas deferens. After castration, there was a specific reduction of the 34.5 K MW protein band in both homogenate and 'luminal fluid'. When the androgen-dependence of proteins was investigated using radioactive methionine, the protein spectra from normal and castrated males showed that about 10 polypeptides were differentially induced or repressed by androgens. The synthesis of some proteins (MW's 24, 36 and 180 K) was decreased by castration while the synthesis of several others (MW's between 27 and 82 K) was increased. Most of these androgen-dependent proteins were detectable at 10 days of age.

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Tissue and Species Specificity of Mouse Ductus Deferens Protein

TARAGNAT,

BERGER,

JEAN

1990

Journal of Andrology

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The ductus deferens of the mouse contains a major protein with a molecular weight of 34.5 kd called mouse vas deferens protein (MVDP). Immunofluorescence histochemistry and immunoblotting with monoclonal antibodies have been used to investigate the localization, tissue, and species distribution, androgen‐regulation, and developmental expression of this protein. Consistent positive immunoreaction was achieved in the ductus deferens epithelium, and immunofluorescence revealed that spermatozoa from the deferent duct were coated with MVDP. Western blot analysis showed the organ specificity of MVDP, which could not be detected in several organs in the mouse. Furthermore, MVDP appeared to be species specific since the proteins extracted from the ductus deferens of man, rat, guinea‐pig, rabbit, and hamster did not react with the anti‐MVDP probe. MVDP, whose expression is regulated by testosterone, was detectable at 20 days of age and its concentration increased rapidly from 20–30 days.

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Biochemical composition of human vas deferens

Cited by 6 publications

References 12 publications

Preliminary characterization, androgen-dependence and ontogeny of an abundant protein from mouse vas deferens

Preliminary characterization, androgen-dependence and ontogeny of an abundant protein from mouse vas deferens

Identification and androgen‐dependence of proteins in the mouse vas deferens

Tissue and Species Specificity of Mouse Ductus Deferens Protein

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