The Proteins of Bovine Spermatozoa From the Caput and Cauda Epididymidis

Lavon, U.; Volcani, R.; Danon, D.

doi:10.1530/jrf.0.0240219

Cited by 33 publications

(10 citation statements)

References 33 publications

(31 reference statements)

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“…The eluted proteins probably represent species adhering to the outer surface of the membrane. Furthermore, it is possible that the epididymal proteins are related to the new protein bands which appear in epididymal spermatozoa during the course of maturation (Lavon, Volcani & Danon, 1971).…”

Section: Discussionmentioning

confidence: 99%

Androgen-Controlled Specific Proteins in Rat Epididymis

Cameo¹,

Blaquier²

1976

Journal of Endocrinology

220

131

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The pattern of proteins in the soluble fraction of the cytoplasm of the rat epididymis was studied by acrylamide gel electrophoresis. The components of five distinct bands, labelled A, B, C, D and E, were found to be sensitive to changes in androgen in the blood. Castration for 14 days produced a sharp decrease in the colour intensity of bands B-E when stained with Amido black. After 21 days of castration, bands D and E were undetectable, bands B and C were severely diminished and band A was more intense. Seven days of replacement with testosterone (1 mg/day) induced a return towards a normal pattern. The degree of restoration was inversely proportional to the duration of castration. Quantitation by densitometry showed that the relative contributions of bands B-E to the region A-E were 61% in the control rat, only 27% after 21 days of castration and 35% when testosterone was given between days 14 and 21 of castration. The components of bands A-E are presumed to be proteins since the electrophoretic pattern was altered by digestion with pronase but not by ribonuclease, phospholipase C or neuraminidase. Epididymides from castrated and androgen-treated castrated rats were incubated with 14C- and 3H-labelled mixed amino acids respectively. After co-electrophoresis the ratio 3H: 14C rose from a baseline of 2-5 in band B, 32 in band C and 7 in bands D and E. Molecular weights were estimated as 27900 for B, 23100 for C and 34400 for D. Band A had the same electrophoretic mobility as serum albumin. Bands B and C were also present in testicular cytosol. Bands D and E were only found in the epididymis, localized mainly within the lumen of the tubules. Bands B-E increased with age during sexual maturation, bands D and E became detectable in the 20-day-old rats. Preliminary evidence indicates that the proteins in bands C, D and E can be removed from caput spermatozoa by washing.

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Section: Discussionmentioning

confidence: 99%

Androgen-Controlled Specific Proteins in Rat Epididymis

Cameo¹,

Blaquier²

1976

Journal of Endocrinology

220

131

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“…Epididymal protein changes after epididymal isolation 27 In the present study, DNA and its associated proteins comprised about 50 % of the TEP. Dawson & Scott (1964) and Lavon et al (1971) reported that the DNA content in sperm cells does not change significantly during the maturation process in the epididymal duct. This suggests that the change of DNA and associated protein level in the different portions of the bull epididymis reported here was mainly caused by the differences in the epididymal tissue.…”

Section: Discussionmentioning

confidence: 99%

“…The various protein fractions were extracted according to the method described by Lavon, Volcani & Danon (1971); lipoprotein was extracted with OT N-NaOH, acid-soluble protein with OT N-HC1, keratin-like basic protein with OT N-HC1 after treatment with 3 % mercaptoethanol, and the DNA and its associated proteins with 3 % NaOH. Protein levels in each extraction fraction were determined by the Folin reagent method (Lowry, Rosebrough, Farr & Randall, 1951).…”

Section: Methodsmentioning

confidence: 99%

Effect of Epididymal Isolation on the Protein Component of Bull Epididymal Tissue

Huang¹,

Turner²,

Johnson³

1975

Reproduction

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Four fractions of protein from intact and 'isolated' bull epididymides were extracted. The total extractable protein was increased by isolation mainly due to increases in the lipoprotein and DNA-protein fractions. Changes of lipoprotein may be associated with the increase of lipid which also occurs in isolated tissue. This may reflect the increase of pentose cycle activity and lipogenesis due to the absence of spermatozoa in the epididymal tubules. Changes of DNA-protein may indicate a change of protein metabolism. Electrophoresis of protein fractions showed that individual proteins may be changed by the zonal origin of the epididymal tissue and the presence or absence of spermatozoa in the epididymal tubules.

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“…Specific protein components are secreted by the epididymis (Lavon, Volcani & Danon, 1971;Killian & Amann, 1973; Koskimies & Kormano, 1975) and the protein composition of epididymal fluid is altered dramatically by castration (Jones & Glover, 1973). However, the role played by epididymal proteins in the development of sperm fertilizing ability is not understood.…”

Section: Introductionmentioning

confidence: 99%

Effects of castration on specific glycoprotein secretions of the epididymis in the rabbit and hamster

Moore¹

1981

Reproduction

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Summary. Mature male rabbits and hamsters were bilaterally castrated and their epididymides were examined, at 2, 4, 7, 9 and 14 days after operation, for the presence of several glycoproteins by using monospecific antisera and indirect immunoperoxidase labelling. In the rabbit, there was a reduction in the glycoprotein reaction product in the epithelium of the proximal caput epididymidis by 2\p=n-\4days after castration, and the staining was weak or absent by 7\p=n-\9 days. Compared with controls, there was also a marked decrease in the intensity of reaction product to glycoprotein in the lumen of the proximal and distal corpus epididymidis 2\p=n-\4 days after castration although spermatozoa still filled the duct in this region. Glycoprotein was present in the distal cauda epididymidis at 14 days but staining diminished as spermatozoa were cleared from the tract. In the hamster, epididymal glycoproteins were apparently less critically dependent on androgens than those in the rabbit, reaching a weak but constant level in the proximal region by 7\p=n-\9 days after castration and remaining at the same intensity in the distal cauda epididymidis throughout the study.These results suggest that the secretion of specific glycoproteins by the mammalian epididymis is related to androgen levels and to sperm maturation.

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The Proteins of Bovine Spermatozoa From the Caput and Cauda Epididymidis

Cited by 33 publications

References 33 publications

Androgen-Controlled Specific Proteins in Rat Epididymis

Androgen-Controlled Specific Proteins in Rat Epididymis

Effect of Epididymal Isolation on the Protein Component of Bull Epididymal Tissue

Effects of castration on specific glycoprotein secretions of the epididymis in the rabbit and hamster

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