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 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The biosynthesis and secretion of epididymal proteins were studied in an in vitro system using explants from rabbit epididymis cultured in a defined medium. Epididymal explants actively incorporated [35S]methionine into cellular proteins, about 7% of them being secreted into the medium. SDS-PAGE of the labeled proteins secreted to the medium showed regional differences in their synthesis and secretion along the epididymal tract. Castration resulted in the inhibition of the synthesis and secretion of at least two polypeptides of Mr 150,000 and 21,000, but at the same time induced the appearance of other polypeptides. Immunoprecipitations with a specific antibody indicated that the variations in the amounts of the secreted 21 kDa component were associated with differences in its rate of synthesis. Epididymis from immature rabbits synthesized some polypeptides that are repressed in the adult state. The results suggest a dual effect of testosterone on rabbit epididymal secretory proteins.
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PMID:In vitro biosynthesis and secretion of rabbit epididymal secretory proteins: regulation by androgens. 273 56

Androgen dependent epididymal proteins act as antigen to produce autoantibodies and affect normal fertility. In the present study, epididymal proteins were analyzed during the time of sexual maturation and their androgen dependency was studied in male albino mice. Epididymis of 21 days (Pre-pubertal), 45 days (Pubertal), 60 days (Post-pubertal), orchidectomized (15 days after surgery) and orchidectomized with testosterone-treated (15 days after treatment) mice were dissected out and analyzed. Caput, corpus and cauda epididymidis were separated and the protein extract was prepared with 0.1 M PBS for 10% SDS-PAGE analysis. Testosterone assay was performed in the experimental groups except the testosterone treated group. The electrophoretic analysis of proteins in caput, corpus and cauda epididymidis of orchidectomized animals showed the disappearance of several proteins as compared to the adult. However, the disappeared proteins started to reappear in testosterone treated animals. The results suggest that removal of testis depletes the testosterone level and causes significant alteration in epididymal proteins. These proteins need further investigation for the purpose of immunocontraception by using them as antigens.
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PMID:Analysis of epididymal proteins during sexual maturation in male albino mice. 1181 49

Epididymis provides a safe environment in which stored-spermatozoa could survive for days before ejaculation. In vitro studies suggested that epididymal proteins seem to be implicated in sperm survival during coincubation with cultured epididymal cells. This study was basically designed to confirm if secretory proteins from bovine epididymal cell cultures provide sperm protection against rapid loss of sperm motility in vitro. Bovine spermatozoa were incubated in conditioned media (CM), which were prepared from cultured cauda epididymal cell (CEC). Motion parameters were recorded using a computer-assisted sperm analyzer. Sperm-free protein extracts from CM were fractionated by ultrafiltration through a 10-kDa cut off membrane. A significantly positive effect on sperm motility was observed when spermatozoa were incubated in CM (54 +/- 4%) and CM > 10 kDa (57 +/- 4%) compared to CM < 10-kDa fraction (30 +/- 3%) or fresh media (34 +/- 3%), after a 6-hr incubation period. This beneficial effect on sperm motility was abolished when the CM > 10-kDa fraction was heat-treated at 100 degrees C for 10 min. The CM > 10 kDa fraction provides factors that remained active even though spermatozoa were washed twice after a 2-hr preincubation period. To identify potential beneficial factors, bovine spermatozoa were incubated with radiolabeled proteins obtained using (35)S-methionine in culture medium. SDS-PAGE analysis of proteins extracted from CM-preincubated spermatozoa revealed the presence of a 42-kDa protein strongly associated to the sperm surface. This 42-kDa spot was trypsin-digested and identified by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) as a protein homologue to a 35-kDa bovine estrogen-sulfotransferase. This protein can play a role in epididymal biology and sperm function. Taken together, these results suggest that specific epididymal proteins can be implicated in the sperm protection in vitro, and can be characterized in our cell culture system.
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PMID:Characterization of secretory proteins from cultured cauda epididymal cells that significantly sustain bovine sperm motility in vitro. 1241 53