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Abstract:

Addition of alkaline phosphatase to rat kidney cytosol diminishes the ability of the mineralocorticoid receptor (MR) to bind aldosterone in a time-, temperature- and concentration-dependent form. A variety of phosphatase inhibitors, including levamisole, are effective in preventing this inactivation. On the other hand, when the steroid-receptor complex is incubated in the presence of alkaline phosphatase, an increment in the rate of receptor transformation is evidenced by a change in the sedimentation coefficient from 8.8 S to 5.1 S, as well as increased DNA-binding capacity. The effects of alkaline phosphatase on activation and transformation can also be observed when the MR is incubated at 20°C in the cytosolic medium, indicating that the catalytic action of an endogenous phosphatase may be involved in the transformation process. The ability of phosphatase inhibitors such as levamisole for suppressing both alkaline phosphatase- and endogenous phosphatase-directed transformation does not correspond well between them. Evidence is presented to affirm that the endogenous phosphatase activity is not due to an alkaline phosphatase-type, but it may be due to a protein serine/threonine phosphatase, as evidenced by the inhibitory effects of okadaic acid. The experimental results also show direct evidence that the MR undergoes phosphorylation in a physiological milieu.

Registro:

Documento: Artículo
Título:Native rat kidney mineralocorticoid receptor is a phosphoprotein whose transformation to a DNA-binding form is induced by phosphatases
Autor:Galigniana, M.D.
Filiación:Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires, Argentina
1301 Medical Science Research Building III, Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109-0623, United States
Palabras clave:alkaline phosphatase; DNA; DNA binding protein; levamisole; mineralocorticoid receptor; okadaic acid; phosphoprotein; phosphoprotein phosphatase; phosphoprotein phosphatase inhibitor; animal tissue; article; controlled study; kidney; male; nonhuman; priority journal; protein DNA binding; rat; sedimentation rate; Animalia
Año:1998
Volumen:333
Número:3
Página de inicio:555
Página de fin:563
DOI: http://dx.doi.org/10.1042/bj3330555
Título revista:Biochemical Journal
Título revista abreviado:Biochem. J.
ISSN:02646021
CODEN:BIJOA
CAS:alkaline phosphatase, 9001-78-9; DNA, 9007-49-2; levamisole, 14769-73-4, 16595-80-5; okadaic acid, 78111-17-8; phosphoprotein phosphatase, 9025-75-6; protein phosphatase 2c
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v333_n3_p555_Galigniana

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Citas:

---------- APA ----------
(1998) . Native rat kidney mineralocorticoid receptor is a phosphoprotein whose transformation to a DNA-binding form is induced by phosphatases. Biochemical Journal, 333(3), 555-563.
http://dx.doi.org/10.1042/bj3330555
---------- CHICAGO ----------
Galigniana, M.D. "Native rat kidney mineralocorticoid receptor is a phosphoprotein whose transformation to a DNA-binding form is induced by phosphatases" . Biochemical Journal 333, no. 3 (1998) : 555-563.
http://dx.doi.org/10.1042/bj3330555
---------- MLA ----------
Galigniana, M.D. "Native rat kidney mineralocorticoid receptor is a phosphoprotein whose transformation to a DNA-binding form is induced by phosphatases" . Biochemical Journal, vol. 333, no. 3, 1998, pp. 555-563.
http://dx.doi.org/10.1042/bj3330555
---------- VANCOUVER ----------
Galigniana, M.D. Native rat kidney mineralocorticoid receptor is a phosphoprotein whose transformation to a DNA-binding form is induced by phosphatases. Biochem. J. 1998;333(3):555-563.
http://dx.doi.org/10.1042/bj3330555