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- W2100372506 abstract "This chapter describes the studies that examine the mechanisms by which luteinizing hormone (LH) or cyclic adenosine monophosphate (cAMP) desensitize steroidogenic response on one hand, but cause an increase in steroidogenic capacity in the same cell type under other conditions. It focuses on the effects of LH or cAMP on the degradation and synthesis of the microsomal P-450 enzymes, 17α-hydroxylase and C17–20lyase, and the relationship of changes in these activities to changes in steroidogenic capacity. The chapter provides an overview on new insights into the mechanism by which the microsomal cytochrome P-450 enzymes, 17α-hydroxylase, and C17–20lyase of Leydig cells are maintained at a constant level under normal physiological conditions. Pulsatile stimulation of Leydig cells by LH in vivo increases cAMP levels—by some yet unknown mechanism—that increases synthesis of the microsomal P-450 enzymes. In addition, cAMP increases steroid hormone production by increasing the availability of the precursor, cholesterol, for further metabolism to testosterone. The steroid products, present at elevated concentrations, can act as pseudo substrates for P-450 enzyme, and in the presence of oxygen, a P-450-pseudosubstrate-O2 complex is formed." @default.
- W2100372506 created "2016-06-24" @default.
- W2100372506 creator A5015768220 @default.
- W2100372506 creator A5059040303 @default.
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- W2100372506 date "1985-01-01" @default.
- W2100372506 modified "2023-09-27" @default.
- W2100372506 title "Regulation of Microsomal Cytochrome P-450 Enzymes and Testosterone Production in Leydig Cells" @default.
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- W2100372506 doi "https://doi.org/10.1016/b978-0-12-571141-8.50008-1" @default.
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