Synthesis and post-translational modifications of an epididymal androgen dependent protein family.
During the annual cycle of the lizard Lacerta vivipara dramatic changes in the secretory activity of the epididymis were observed. These changes and changes in morphology correlate with the plasma and epididymal testosterone concentrations. The secretory proteins contain a major group of immunorelated components referred to as LI to L1X. They consist of a group of nine proteins Mr 19,000 which can be separated according to pI 3.5 to 8.7. Post-translational modifications may be responsible for their pI diversity. All the L proteins are glycosylated (fucose, N-acetylgalactosamine and or N-acetylglucosamine) but only LVI glycosylation was inhibited with tunicamycin. Phosphorylation is unique to LV protein and none of the L proteins are sulfated. All L proteins appeared sequentially during the annual cycle and in organotypic culture when incubated in the presence of testosterone (150, 500, 1000 nM) in a time dependent manner.
Ravet
V
V
CNRS, URA 360 Laboratoire de Biologie Cellulaire, Aubière, France.
Depeiges
A
A
Morel
F
F
Dufaure
J P
JP
D000728:Androgens / Q000096:biosynthesis*; D000818:Animals; D002369:Castration; D015180:Electrophoresis, Gel, Two-Dimensional; D004822:Epididymis / Q000378:metabolism*; D005786:Gene Expression Regulation; D006031:Glycosylation; D008116:Lizards; D008297:Male; D009924:Organ Culture Techniques; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational / Q000502:physiology*
D000728:Androgens