The level and phosphorylation of Hsp70 in the rat liver cytosol after adrenalectomy and hyperthermia.

Abstract:

:Hepatic heat shock protein Hsp70 synthesis and in vitro phosphorylation were studied in the liver cytosol of intact, adrenalectomized and dexamethasone-administered adrenalectomized rats after 41 degrees C whole body hyperthermic stress. Hsp70 was detected by immunoblotting with N27F3-4 monoclonal antibody recognizing both constitutive and inducible forms of the protein. A comparison between basal and heat stress-induced levels of the protein in the liver cytosol of the three groups of animals suggested that glucocorticoid hormones stimulate the basal synthesis of Hsp70 and inhibit its induction by stress. In both unstressed and hyperthermia-exposed animals, hepatic Hsp70 was detected as a phosphoprotein. The extent of its in vitro phosphorylation was found to be significantly reduced by heat stress or adrenalectomy, but dexamethasone failed to restore it to the original level.

journal_name

Cell Biol Int

authors

Cvoro A,Dundjerski J,Trajković D,Matić G

doi

10.1006/cbir.1998.0247

keywords:

subject

Has Abstract

pub_date

1999-01-01 00:00:00

pages

313-20

issue

4

eissn

1065-6995

issn

1095-8355

pii

S1065-6995(98)90247-5

journal_volume

23

pub_type

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