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- W2027794920 abstract "Prostaglandin synthesis by rat testicular tissue was observed to be gonadotrophin and adrenal dependent, and to have the same distribution in the gonad as the steroidogenic enzymes. The synthesis was increased by 5-HT, but decreased by melatonin. Lipid peroxidation increases with age, FSH treament, linoleic and arachidonic acid and melatonin, but was decreased by serotonin, c-AMP, LH, prolactin and ephinephrine. Testicular lysosomes were labilized by LH, adrenal demedullation, testosterone, Vit. A and acetylcholine, but were stabilized by c-AMP, epinephrine and cortisol. Contractility of rat seminiferous tubules was observed to be prostaglandin dependent, stimulated by 5-HT, and inhibited by melatonin and c-AMP. Evidence was obtained indicating that a phospholipase A2 is present in rat testicular lysosomes, and that it is liberated by radiation, heat or certain chemicals. This enzyme hydrolyses PUFA from membrane phospholipids, the former of which are converted into prostaglandins. The prostaglandins appear to initially stimulate contractility of seminiferous tubules, but at higher concentrations they stimulate adenyl cyclase, which increases c-AMP levels in the tubules thereby inhibiting contractility and cellular division. The process of prostaglandin synthesis also produced malonaldehyde, and endoperoxides that contribute to alterations in steroidogenesis by Schiff's base formation and to cellular lysis by membrane permeability changes. Prostaglandins appear to be synthesized physiologically from PUFA derived from cholesterol esters, but pathologically in much larger quantities from membrane phospholipids. Prostaglandins apparently inhibit androgen synthesis by their effects on cholesterol esterase and other steroidogenic enzymes rather than by changing blood flow." @default.
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- W2027794920 date "1975-06-01" @default.
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- W2027794920 title "Mechanisms and interactions in testicular steroidogenesis and prostaglandin synthesis" @default.
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- W2027794920 doi "https://doi.org/10.1016/0022-4731(75)90353-2" @default.
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