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Titolo:
The 11 beta hydroxysteroid dehydrogenase 2 exists as an inactive dimer
Autore:
Gomez-Sanchez, EP; Ganjam, V; Chen, YJ; Liu, Y; Clark, SA; Gomez-Sanchez, CE;
Indirizzi:
GV Sonny Montgomery VA Med Ctr, Endocrine Sect, Jackson, MS 39216 USA GV Sonny Montgomery VA Med Ctr Jackson MS USA 39216 Jackson, MS 39216 USA GV Sonny Montgomery VA Med Ctr, Res Serv, Jackson, MS 39216 USA GV Sonny Montgomery VA Med Ctr Jackson MS USA 39216 Jackson, MS 39216 USA Univ Mississippi, Med Ctr, Div Endocrinol, Jackson, MS 39216 USA Univ Mississippi Jackson MS USA 39216 v Endocrinol, Jackson, MS 39216 USA Univ Missouri, Dept Med, Columbia, MO 65211 USA Univ Missouri Columbia MOUSA 65211 uri, Dept Med, Columbia, MO 65211 USA Univ Missouri, Dept Vet Biomed Sci, Columbia, MO 65211 USA Univ Missouri Columbia MO USA 65211 et Biomed Sci, Columbia, MO 65211 USA
Titolo Testata:
STEROIDS
fascicolo: 11, volume: 66, anno: 2001,
pagine: 845 - 848
SICI:
0039-128X(200111)66:11<845:T1BHD2>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT 11-BETA-HYDROXYSTEROID DEHYDROGENASE; APPARENT MINERALOCORTICOID EXCESS; HIGH-AFFINITY; TARGET-CELLS; ENZYME; HYPERTENSION; SPECIFICITY; MUTATIONS; RECEPTOR; TYPE-2;
Keywords:
11 beta hydroxysteroid dehydrogenase; corticosterone; 11-dehydrocorticosterone; steroid inactivation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Gomez-Sanchez, CE GV Sonny Montgomery VA Med Ctr, Endocrine Sect, 1500 E Woodrow Wilson Dr 151, Jackson, MS 39216 USA GV Sonny Montgomery VA Med Ctr 1500 E Woodrow Wilson Dr 151 Jackson MS USA 39216
Citazione:
E.P. Gomez-Sanchez et al., "The 11 beta hydroxysteroid dehydrogenase 2 exists as an inactive dimer", STEROIDS, 66(11), 2001, pp. 845-848

Abstract

The 11 beta -hydroxysteroid dehydrogenase types 1 and 2 enzymes (11 beta -HSD1 and 11 beta -HSD2), modulate glucocorticoid occupation of the mineralocorticoid and glucocorticoid receptors by interconverting corticosterone and cortisol to the inactive metabolites 11-dehydrocorticosterone and cortisone within the target cells. The NAD(+)-dependent 11-HSD 2 in the kidney inactivates corticosterone and cortisol, allowing aldosterone, which is not metabolized. access to the receptor. Studies of the kinetics of 11-HSD 2 activity in the rat kidney have produced inconsistent results. Western blots done in the absence of the reducing agent beta -mercaptoethanol showed two bands with approximate MW of 40 and 80 kDa. When beta -mercaptoethanol was used, only the 40 kDa was detected, indicating that under non-denaturing conditions a significant proportion of the 11 beta -HSD 2 exists as a dimer. NAD(+)-dependent conversion of H-3-corticosterone by 20 mug of microsomal protein increased approximately 10 fold with the addition of 5 mM DTT concentration. NADP(+)-dependent activity with 20 mug of microsomal protein was very low and did not change significantly when using DTT. In the presence of DTT, the predominant 11-HSD activity in the rat kidney is NAD(+)-dependent with a K-m of 15.1 nM. similar to that of the cloned and expressed enzyme. These data suggest that dimerization and subsequent enzyme inactivation occur when protocols promoting oxidation of this protein are used. Published byElsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/05/18 alle ore 13:03:30