Stability study on renal type I mineralocorticoid receptor

The purpose of this work is to review stability and activation properties of type 1 receptor, in order to explain the reasons for its extreme in vitro instability. We demonstrate that the treatment of rat kidney cytosol with H2O2 prevents aldosterone binding, DNA/steroid- receptor complex interactio...

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Autor principal: Galigniana, M.D
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Elsevier Inc. 1996
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0030581094 
024 7 |2 cas  |a 5,5' dithiobis(2 nitrobenzoic acid), 69-78-3; aldosterone, 52-39-1, 6251-69-0; DNA, 9007-49-2; edetic acid, 150-43-6, 60-00-4; egtazic acid, 67-42-5; hydrogen peroxide, 7722-84-1; iron, 14093-02-8, 53858-86-9, 7439-89-6; mercaptoethanol, 60-24-2; n ethylmaleimide, 128-53-0 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a LIFSA 
100 1 |a Galigniana, M.D. 
245 1 0 |a Stability study on renal type I mineralocorticoid receptor 
260 |b Elsevier Inc.  |c 1996 
270 1 0 |m Galigniana, M.D.; Departamento de Quimica Biologica, FCEN, Universidad de Buenos Aires, Buenos Aires 1428, Argentina 
506 |2 openaire  |e Política editorial 
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520 3 |a The purpose of this work is to review stability and activation properties of type 1 receptor, in order to explain the reasons for its extreme in vitro instability. We demonstrate that the treatment of rat kidney cytosol with H2O2 prevents aldosterone binding, DNA/steroid- receptor complex interactions, and prevents the receptor thermal inactivation. In contrast, exogenous sulfhydryl reducing reagents are necessary to insure maximum binding of mineralocorticoid receptor and DNA/steroid-receptor interaction. However, the presence of β- mercaptoethanol in thermal induced incubations reverts the H2O2 protection. We also demonstrate that contaminations with free or sequestered iron are harmful for both, receptor binding capacity (in a reversible form) and for hormone-receptor/DNA binding properties (in a partially reversible form). We propose a sulfhydryl oxidative mechanism for type I mineralocorticoid receptor inactivation in which iron contaminants might accelerate this process by oxidative catalysis. We also demonstrate that when thiol groups are blocked by specific reagents such as N-ethyl-maleimide or dithionitrobenzoic acid, type I sites loose binding capacity, but the protein is protected from oxidation as well as inactivation.  |l eng 
593 |a Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires (1428), Argentina 
690 1 0 |a MINERALOCORTICOID RECEPTOR 
690 1 0 |a OXIDATION 
690 1 0 |a STABILITY 
690 1 0 |a THIOL GROUPS 
690 1 0 |a 5,5' DITHIOBIS(2 NITROBENZOIC ACID) 
690 1 0 |a ALDOSTERONE 
690 1 0 |a DNA 
690 1 0 |a EDETIC ACID 
690 1 0 |a EGTAZIC ACID 
690 1 0 |a HYDROGEN PEROXIDE 
690 1 0 |a IRON 
690 1 0 |a MERCAPTOETHANOL 
690 1 0 |a MINERALOCORTICOID RECEPTOR 
690 1 0 |a N ETHYLMALEIMIDE 
690 1 0 |a STEROID 
690 1 0 |a THIOL GROUP 
690 1 0 |a ANIMAL CELL 
690 1 0 |a ARTICLE 
690 1 0 |a CELL FREE SYSTEM 
690 1 0 |a CYTOSOL 
690 1 0 |a DNA BINDING 
690 1 0 |a HIGH TEMPERATURE PROCEDURES 
690 1 0 |a KIDNEY 
690 1 0 |a NONHUMAN 
690 1 0 |a OXIDATION 
690 1 0 |a RAT 
690 1 0 |a RECEPTOR BINDING 
690 1 0 |a THERMOSTABILITY 
690 1 0 |a ANIMALIA 
773 0 |d Elsevier Inc., 1996  |g v. 59  |h pp. 511-521  |k n. 7  |p LIFE SCI.  |x 00243205  |w (AR-BaUEN)CENRE-749  |t Life Sciences 
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