Abstract
LH acutely increases luteal progestin biosynthesis by stimulating cholesterol side-chain cleavage, a reaction catalyzed by a complex of mitochondrial enzymes containing cytochrome P-450 (1). The steroidogenic action of LH is inhibited by cycloheximide and puromycin, indicating a requirement for protein synthesis (2). It has been suggested that availability of cholesterol governs the rate of side-chain cleavage and that proteins formed under the influence of LH play a role in translocation of cholesterol to the mitochondrial enzyme complex (1,2). In the present study, relationships between cholesterol supply and in vitro steroid synthesis by rat luteal mitochondria were explored.
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© 1979 Plenum Press, New York
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Toaff, M.E., Flickinger, G.L., Strauss, J.F., Shattil, S.J. (1979). Relationships between Cholesterol Supply and Luteal Mitochondrial Steroid Synthesis. In: Channing, C.P., Marsh, J.M., Sadler, W.A. (eds) Ovarian Follicular and Corpus Luteum Function. Advances in Experimental Medicine and Biology, vol 112. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3474-3_61
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DOI: https://doi.org/10.1007/978-1-4684-3474-3_61
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