Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.12.7.2 (hydrogenase)
 3,522 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A crude human hypophyseal extract (HE), as well as human growth hormone (GH), ovine prolactin (PRL) and commercial preparations of ACTH, TSH, pregnant mare's serum gonadotrophins (PMS) and chorionic gonadotrophin (CG) were tested for their ability to induce the activities of cytoplasmic 17 beta-hydroxysteroid dehydrogenase and microsomal delta 4-5alpha-hydrogenase and to repress the activities of microsomal 3alpha- and 3beta-hydroxysteroid dehydrogenases in the liver of hypophysectomized rats. The activity of 17beta-hydroxysteroid dehydrogenase was not affected by any of the administered hormones. For the other enzymes, only PRL was effective in causing changes in the activities; the repressive effect on 3alpha-hydroxysteroid dehydrogenase activity was highly significant (P less than 0.001). These results indicate that PRL is involved in the regulation of at least some of the enzyme activities of hepatic steroid hormone metabolism.
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PMID:Regulation of the activities of the enzymes involved in the metabolism of steroid hormones in rat liver: the effect of administration of anterior hypophyseal hormones and gonadotrophin preparations to hypophysectomized rats. 18 36

The metabolism of testosterone by experimental granulation tissue, fibroblasts and the oral mucosa of rats of both sexes was studied. The experimental granulation tissue was produced by implanting viscose-cellulose sponges beneath the dorsal skin of female and male rats for 21 days. The granuloma capsules, fibroblasts in the sponges and the oral mucosae were homogenated. Mitochondrial, microsomal and soluble fractions were incubated with [4-14C]testosterone and NADPH for 30 min at pH 7.4 and 37 degrees C. The metabolites were identified with column and TLC and radioautography and quantified with liquid scintillation counting. The experimental granulation tissue and fibroblasts of both sexes showed less activity in metabolizing testosterone than the gingival tissue. The tissues were shown to contain 3 alpha-, 3 beta- and 17 beta-hydroxysteroid dehydrogenase and 5 alpha- and 5 beta-steroid hydrogenase activities. The activities of the enzymes in the oral mucosae were higher than in the experimental granulation tissue and fibroblasts.
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PMID:Role of granulation tissue and fibroblasts in gingival testosterone metabolism in the rat in vitro. 379 46

11 beta-Hydroxysteroid dehydrogenase (11-HSD) catalyzes the conversion of cortisol to cortisone and corticosterone to 11-dehydrocorticosterone. This activity may be required to confer normal ligand specificity upon the mineralocorticoid receptor. Although an isozyme of 11-HSD was previously isolated from rat liver, a different isozyme is apparently expressed in mineralocorticoid target tissues. We isolated a sheep kidney cDNA clone encoding this isozyme by expression screening using Xenopus oocytes. The cDNA is 1.8 kb in length and encodes a protein of 427 amino acid residues with a predicted M(r) of 46,700. When expressed in oocytes, this enzyme functions as an NAD(+)-dependent 11 beta-hydrogenase with very high affinity for steroids, but it has no detectable reductase activity. It is 37% identical in amino acid sequence to an NAD(+)-dependent isozyme of 17 beta-hydroxysteroid dehydrogenase, but only 20% identical to the NADP(+)-dependent liver isozyme of 11-HSD. It is expressed at high levels in the kidney and adrenal and at lower levels in the colon. The corresponding gene is present in a single copy in the sheep genome. In humans, this gene is a candidate locus for the syndrome of apparent mineralocorticoid excess, a form of hypertension postulated to result from 11-HSD deficiency in mineralocorticoid target tissues.
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PMID:Cloning of cDNA encoding an NAD(+)-dependent isoform of 11 beta-hydroxysteroid dehydrogenase in sheep kidney. 758 2