Evidence for the requirement of proteolysis in LH stimulated cyclic AMP production and steroidogenesis in Leydig cells.
We have investigated the effect of protease activity on cyclic AMP production and steroidogenesis in rat testis, mouse testis and mouse tumour Leydig (MA10) cells. LH-, dibutyryl cyclic AMP-, and forskolin-stimulated steroidogenesis, but not 22R(OH) cholesterol conversion to pregnenolone, was inhibited by protease inhibitors. In mouse Leydig cells, LH but not forskolin or cholera toxin stimulated cyclic AMP production was inhibited by protease inhibitors. These results suggest that steroidogenesis in Leydig cells requires proteolysis before the conversion of cholesterol to pregnenolone. In the mouse but not rat Leydig cells, LH-stimulated cyclic AMP production is also dependent on proteolysis.
West
A P
AP
Department of Biochemistry, Royal Free Hospital School of Medicine, University of London, U.K.
Phipp
L H
LH
Cooke
B A
BA
D000818:Animals; D003994:Bucladesine / Q000494:pharmacology; D005576:Colforsin / Q000494:pharmacology; D000242:Cyclic AMP / Q000096:biosynthesis*; D010450:Endopeptidases / Q000502:physiology*; D066298:In Vitro Techniques; D007985:Leydig Cells / Q000502:physiology*; D007986:Luteinizing Hormone / Q000494:pharmacology*; D008297:Male; D051379:Mice; D011284:Pregnenolone / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D013739:Testosterone / Q000096:biosynthesis*; D014407:Tumor Cells, Cultured
D011480:Protease Inhibitors; D005576:Colforsin; D013739:Testosterone; D003994:Bucladesine; D011284:Pregnenolone; D007986:Luteinizing Hormone; D000242:Cyclic AMP; D010450:Endopeptidases