## Abstract Heterologous protein secretion involves the coupled processes of protein synthesis, protein folding, and secretory trafficking. A more complete understanding of how these processes interrelate could help direct optimization of secretion systems. Here we provide a detailed study regardin
In vitro biosynthesis and secretion of rabbit epididymal secretory proteins: Regulation by androgens
β Scribed by Regalado, F. ;Nieto, A.
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 544 KB
- Volume
- 250
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
β¦ Synopsis
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 [3"S]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 M, 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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