Characterization and androgenic regulation of major mRNAs coding for epididymal proteins in a lizard (Lacerta vivipara).
During the reproductive period (spring) under the control of testosterone the epididymis of the viviparous lizard secretes a group of major proteins with an approximate Mr of 19,000 named L protein(s). These proteins are recognized by a specific immunoserum and bind to the heads of spermatozoa. During spring, translation in reticulocyte lysate of RNA from secreting epididymis (stage 6) produced 5 immunoprecipitable bands with Mr values from 21,500 to 25,000. Such synthesis is undetectable during sexual rest in summer (stage 1). The 5 bands disappear when translation is performed in the presence of dog pancreas microsomes although a new band of Mr 19 000 becomes prominent. This suggests that synthesis of L protein involves two steps, i.e. synthesis of precursors (L preproteins) followed by a maturation process. At least 11 translation products (including L-preproteins) are involved in annual variations that follow the differentiation of the epididymal epithelial cells and their androgen dependency was studied by castration and in-vitro stimulation by testosterone. In these conditions, testosterone is able to control accumulation of RNA corresponding to L preproteins and to a translation product of Mr 29 000.
Biologie cellulaire Université de Clermont-Fd II, Aubière, France.
Y
Y
Courty
F
F
Morel
J P
JP
Dufaure
D000818:Animals; D004822:Epididymis / Q000187:drug effects / Q000378:metabolism*; D066298:In Vitro Techniques; D008116:Lizards; D008297:Male; D009919:Orchiectomy; D011506:Proteins / Q000032:analysis*; D012333:RNA, Messenger / Q000032:analysis*; D030162:Reptilian Proteins; D013739:Testosterone / Q000378:metabolism* / Q000494:pharmacology
C052269:L protein, lizard; D011506:Proteins; D012333:RNA, Messenger; D030162:Reptilian Proteins; D013739:Testosterone