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- W2068909130 abstract "The subcellular location of adult female rat hypothalamic steroid 5α-reductase and 3α-hydroxysteroid oxidoreductase (3α-HSD) activities, which catalyze the conversion of progesterone to 3α-hydroxy-5α-pregnan-20-one via 5α-pregnane-3,20-dione, have been investigated using 3H-labeled substrates and an isotopic dilution assay system. In crude homogenates, appreciable conversion of 5α-pregnane-3,20-dione to 3α-hydroxy-5α-pregnan-20-one is observed with either NADH or NADPH as cofactor. The NADH-and NADPH-linked 3α-HSD activities can be partially separated and enriched using subcellular fractionation by differential centrifugation. The subcellular location of these 3α-HSD activities as well as progesterone 5α-reductase activity was determined with the aid of subcellular markers and electron microscopic techniques. When NADPH is the added cofactor, 3α-HSD activity is present primarily in the cytosol and cofractionates with lactate dehydrogenase activity. When NADH is the added cofactor, 3α-HSD activity is enriched in the 1000g pellet and is further localized to a cell debris-membranes fraction derived from this pellet. Using the muscarinic cholinergic receptor as a plasma membrane marker, the NADH-linked 3α-HSD activity appears to cofractionate with plasma membranes in subcellular fractions. Progesterone 5α-reductase activity is enriched in the 105,000g pellet and cofractionates with NADPH cytochrome c reductase activity, suggesting a microsomal location. On the basis of these results, there appear to be at least two hypothalamic 3α-HSD's, a cytosolic NADPH-linked activity and a plasma membrane NADH-linked 3α-HSD activity." @default.
- W2068909130 created "2016-06-24" @default.
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- W2068909130 date "1980-03-01" @default.
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- W2068909130 title "Subcellular location of hypothalamic progesterone metabolizing enzymes and evidence for distinct NADH- and NADHP-linked 3α-hydroxysteroid oxidoreductase activities" @default.
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- W2068909130 doi "https://doi.org/10.1016/0022-4731(80)90005-9" @default.
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