Dehydrogenation of reduced pyridine nucleotides by Leydig cell tumors of the rat testis.
The activities of the cytochrome c reductases and of the D-T diaphorase in rat Leydig cell tumors have been described. The increase in enzymatic activity of the NADH cytochrome c reductase activity in functional tumors derived from interstitial cells of the rat testis is interpreted as being possibly related to hydroxylation of steroids by the neoplastic cells. Meanwhile, the increase in the activity of the D-T diaphorase in the other tumor is interpreted as being an anaplerotic reaction to substitute for the deficient shuttles for the transfer of reducing equivalents from the cytoplasm to the mitochondria observed in tumors.
D000818:Animals; D002458:Cell Fractionation; D003579:Cytochrome Reductases / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D007984:Leydig Cell Tumor / Q000201:enzymology / Q000378:metabolism*; D008297:Male; D008861:Microsomes / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D009249:NADP / Q000378:metabolism*; D009374:Neoplasms, Experimental / Q000201:enzymology / Q000378:metabolism; D011808:Quinone Reductases / Q000378:metabolism; D051381:Rats
D009249:NADP; D003579:Cytochrome Reductases; D011808:Quinone Reductases