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Titolo:
Characterization of the uridine diphosphate-glucuronosyltransferse-catalyzing thyroid hormone glucuronidation in man
Autore:
Findlay, KAB; Kaptein, E; Visser, TJ; Burchell, B;
Indirizzi:
Univ Dundee, Ninewells Hosp & Med Sch, Dept Mol & Cellular Pathol, Dundee DD1 9SY, Scotland Univ Dundee Dundee Scotland DD1 9SY lar Pathol, Dundee DD1 9SY, Scotland Erasmus Univ, Dept Internal Med 3, Sch Med, NL-3015 GE Rotterdam, Netherlands Erasmus Univ Rotterdam Netherlands NL-3015 GE GE Rotterdam, Netherlands
Titolo Testata:
JOURNAL OF CLINICAL ENDOCRINOLOGY AND METABOLISM
fascicolo: 8, volume: 85, anno: 2000,
pagine: 2879 - 2883
SICI:
0021-972X(200008)85:8<2879:COTUD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
UDP-GLUCURONOSYLTRANSFERASES; EVOLUTIONARY DIVERGENCE; GENE SUPERFAMILY; HUMAN LIVER; RAT-LIVER; BILIRUBIN; UDPGLUCURONOSYLTRANSFERASE; MICROSOMES; KIDNEY; PHENOL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Findlay, KAB Univ Dundee, Ninewells Hosp & Med Sch, Dept Mol & Cellular Pathol, Dundee DD1 9SY, Scotland Univ Dundee Dundee Scotland DD1 9SY undee DD1 9SY, Scotland
Citazione:
K.A.B. Findlay et al., "Characterization of the uridine diphosphate-glucuronosyltransferse-catalyzing thyroid hormone glucuronidation in man", J CLIN END, 85(8), 2000, pp. 2879-2883

Abstract

Increased thyroid hormone glucuronidation in rats caused by exposure to xenobiotics has stimulated a search for the individual uridine diphosphate-glucuronosyltransferases (UGTs) catalyzing this reaction in rats and man. Microsomal preparations from Crigler-Najjar liver, normal human liver, and kidney have been used to try to identify the UGT isoforms responsible for glucuronidation of the thyroid hormones. The predominant thyroid hormone released from the thyroid gland, T-4, and the inactive rT(3) are glucuronidated by cloned expressed bilirubin UGT1A1 and also phenol UGT1A9. Results from Crigler-Najjar microsomal samples indicate that UGT1A1 is the main contributor to thyroid hormone glucuronidation in the liver, with rT(3) being the preferential substrate. In kidney microsomes thyroid hormone glucuronidation is more complex, suggesting that more than just the UGT1A9 isoform may be involved. Bioactive T-3 is not significantly glucuronidated by these isoformsand other UGTs, and sulfotransferases may be involved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 23:12:51