Studies on the decrease of liver cytochrome P-450 content by triiodothyronine

In the rat liver, the microsomal content of cytochrome P-450 decreased by 50% after triiodothyronine (T3) administration. The molecular basis for the decreased cytochrome P-450 levels was investigated. The activities of the enzymes involved in heme synthesis or degradation were not altered by thyroi...

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Autores principales:	Kleiman de Pisarev, D.L., Ferramola de Sancovich, A.M., Sancovich, H.A.
Formato:	JOUR
Materias:	(Rat liver) Cytochrome P-450 Triiodothyronine cytochrome p450 liothyronine animal experiment article hypothyroidism intraperitoneal drug administration liver level liver microsome nonhuman priority journal rat thyroidectomy 5-Aminolevulinate Synthetase Aminolevulinic Acid Animal Cytochrome P-450 Enzyme System Electrophoresis, Polyacrylamide Gel Heme Human Hydroxymethylbilane Synthase Male Microsomes, Liver Porphobilinogen Synthase Proteins Rats Rats, Inbred Strains Serum Albumin Support, Non-U.S. Gov't Animalia
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_03044165_v1074_n1_p172_KleimandePisarev
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_03044165_v1074_n1_p172_KleimandePisarev2023-10-03T15:20:40Z Studies on the decrease of liver cytochrome P-450 content by triiodothyronine Kleiman de Pisarev, D.L. Ferramola de Sancovich, A.M. Sancovich, H.A. (Rat liver) Cytochrome P-450 Triiodothyronine cytochrome p450 liothyronine animal experiment article hypothyroidism intraperitoneal drug administration liver level liver microsome nonhuman priority journal rat thyroidectomy 5-Aminolevulinate Synthetase Aminolevulinic Acid Animal Cytochrome P-450 Enzyme System Electrophoresis, Polyacrylamide Gel Heme Human Hydroxymethylbilane Synthase Male Microsomes, Liver Porphobilinogen Synthase Proteins Rats Rats, Inbred Strains Serum Albumin Support, Non-U.S. Gov't Triiodothyronine Animalia In the rat liver, the microsomal content of cytochrome P-450 decreased by 50% after triiodothyronine (T3) administration. The molecular basis for the decreased cytochrome P-450 levels was investigated. The activities of the enzymes involved in heme synthesis or degradation were not altered by thyroid hormone administration. The incorporation of 3H-δ-aminolaevulinate into the liver microsomal heme was markedly reduced in T3-treated rats. The latter appeared not to reflect a lowered binding affinity of the apoprotein moiety of cytochrome P-450 for heme. The sodium dodecyl sulfate gel electrophoresis of the microsomal preparation showed a decrease in apocytochrome P-450. It is suggested that the amount of the apocytochrome may be the primary event affected in the formation of cytochrome P-450, by triiodothyronine treatment of thyroidectommized rats. © 1991. Fil:Kleiman de Pisarev, D.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ferramola de Sancovich, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Sancovich, H.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03044165_v1074_n1_p172_KleimandePisarev
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	(Rat liver) Cytochrome P-450 Triiodothyronine cytochrome p450 liothyronine animal experiment article hypothyroidism intraperitoneal drug administration liver level liver microsome nonhuman priority journal rat thyroidectomy 5-Aminolevulinate Synthetase Aminolevulinic Acid Animal Cytochrome P-450 Enzyme System Electrophoresis, Polyacrylamide Gel Heme Human Hydroxymethylbilane Synthase Male Microsomes, Liver Porphobilinogen Synthase Proteins Rats Rats, Inbred Strains Serum Albumin Support, Non-U.S. Gov't Triiodothyronine Animalia
spellingShingle	(Rat liver) Cytochrome P-450 Triiodothyronine cytochrome p450 liothyronine animal experiment article hypothyroidism intraperitoneal drug administration liver level liver microsome nonhuman priority journal rat thyroidectomy 5-Aminolevulinate Synthetase Aminolevulinic Acid Animal Cytochrome P-450 Enzyme System Electrophoresis, Polyacrylamide Gel Heme Human Hydroxymethylbilane Synthase Male Microsomes, Liver Porphobilinogen Synthase Proteins Rats Rats, Inbred Strains Serum Albumin Support, Non-U.S. Gov't Triiodothyronine Animalia Kleiman de Pisarev, D.L. Ferramola de Sancovich, A.M. Sancovich, H.A. Studies on the decrease of liver cytochrome P-450 content by triiodothyronine
topic_facet	(Rat liver) Cytochrome P-450 Triiodothyronine cytochrome p450 liothyronine animal experiment article hypothyroidism intraperitoneal drug administration liver level liver microsome nonhuman priority journal rat thyroidectomy 5-Aminolevulinate Synthetase Aminolevulinic Acid Animal Cytochrome P-450 Enzyme System Electrophoresis, Polyacrylamide Gel Heme Human Hydroxymethylbilane Synthase Male Microsomes, Liver Porphobilinogen Synthase Proteins Rats Rats, Inbred Strains Serum Albumin Support, Non-U.S. Gov't Triiodothyronine Animalia
description	In the rat liver, the microsomal content of cytochrome P-450 decreased by 50% after triiodothyronine (T3) administration. The molecular basis for the decreased cytochrome P-450 levels was investigated. The activities of the enzymes involved in heme synthesis or degradation were not altered by thyroid hormone administration. The incorporation of 3H-δ-aminolaevulinate into the liver microsomal heme was markedly reduced in T3-treated rats. The latter appeared not to reflect a lowered binding affinity of the apoprotein moiety of cytochrome P-450 for heme. The sodium dodecyl sulfate gel electrophoresis of the microsomal preparation showed a decrease in apocytochrome P-450. It is suggested that the amount of the apocytochrome may be the primary event affected in the formation of cytochrome P-450, by triiodothyronine treatment of thyroidectommized rats. © 1991.
format	JOUR
author	Kleiman de Pisarev, D.L. Ferramola de Sancovich, A.M. Sancovich, H.A.
author_facet	Kleiman de Pisarev, D.L. Ferramola de Sancovich, A.M. Sancovich, H.A.
author_sort	Kleiman de Pisarev, D.L.
title	Studies on the decrease of liver cytochrome P-450 content by triiodothyronine
title_short	Studies on the decrease of liver cytochrome P-450 content by triiodothyronine
title_full	Studies on the decrease of liver cytochrome P-450 content by triiodothyronine
title_fullStr	Studies on the decrease of liver cytochrome P-450 content by triiodothyronine
title_full_unstemmed	Studies on the decrease of liver cytochrome P-450 content by triiodothyronine
title_sort	studies on the decrease of liver cytochrome p-450 content by triiodothyronine
url	http://hdl.handle.net/20.500.12110/paper_03044165_v1074_n1_p172_KleimandePisarev
work_keys_str_mv	AT kleimandepisarevdl studiesonthedecreaseoflivercytochromep450contentbytriiodothyronine AT ferramoladesancovicham studiesonthedecreaseoflivercytochromep450contentbytriiodothyronine AT sancovichha studiesonthedecreaseoflivercytochromep450contentbytriiodothyronine
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Studies on the decrease of liver cytochrome P-450 content by triiodothyronine

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