Linked Life Data

15543931

Source:http://linkedlifedata.com/resource/pubmed/id/15543931

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2004-11-16
pubmed:abstractText
The level and intracellular redistribution of the two nucleo-cytoplasmic members of 70 kDa heat shock protein family (constitutive, Hsc70 or Hsp73, and inducible, Hsp72) were studied in rat liver during a 24-h period after exposure of the animals to 41 degrees C whole body hyperthermic stress. The examined proteins were detected in the liver cytosol and nuclei by Western blotting and immunohistochemical staining of paraffin sections, as well as by immnocytochemical staining of isolated nuclear smears. All three techniques applied were based on the use of monoclonal antibodies recognizing both constitutive and inducible Hsp70 isoforms or only the inducible isoform, and gave consistent results. The exposure of the animals to in vivo heat stress was shown to induce the synthesis of otherwise non-existing Hsp72, rendering Hsc70 level unchanged in comparison to unstressed controls. However, immediately after the stress the intracellular redistribution of Hsc70, i.e. its nuclear accumulation, was observed. The maximal level of Hsp70 both in the cytoplasm and in the nuclei was registered 5 h after the stress, which coincided with the maximal level of Hsp72 induction. The alterations in the level and intracellular distribution of examined proteins were still noticeable 24 h after the stress. The results of this study could shed some more light on, as yet uncertain, differences between cellular functions of these two proteins, as well as on the role of the constitutive form under normal and stress conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-35
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15543931-Animals, pubmed-meshheading:15543931-Blotting, Western, pubmed-meshheading:15543931-Cell Nucleus, pubmed-meshheading:15543931-Cytosol, pubmed-meshheading:15543931-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15543931-HSC70 Heat-Shock Proteins, pubmed-meshheading:15543931-HSP70 Heat-Shock Proteins, pubmed-meshheading:15543931-HSP72 Heat-Shock Proteins, pubmed-meshheading:15543931-Heat-Shock Proteins, pubmed-meshheading:15543931-Hot Temperature, pubmed-meshheading:15543931-Immunohistochemistry, pubmed-meshheading:15543931-Liver, pubmed-meshheading:15543931-Male, pubmed-meshheading:15543931-Protein Isoforms, pubmed-meshheading:15543931-Rats, pubmed-meshheading:15543931-Rats, Wistar, pubmed-meshheading:15543931-Temperature, pubmed-meshheading:15543931-Time Factors
pubmed:year
2004
pubmed:articleTitle
Intracellular localization of constitutive and inducible heat shock protein 70 in rat liver after in vivo heat stress.
pubmed:affiliation
Department of Biochemistry, Institute for Biological Research, Belgrade, Serbia and Montenegro (Yugoslavia).
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't