Linked Life Data

8453996

Source:http://linkedlifedata.com/resource/pubmed/id/8453996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-4-20
pubmed:abstractText
The heat-shock protein of 90 kDa (hsp90), constitutively expressed in most cells, is up-regulated by thermal stress and by developmental and mitogenic stimuli. When the serum-starved chicken hepatoma cell line DU249 is stimulated by serum, insulin, or growth factors acting via tyrosine kinase receptors, a transient induced expression of the hsp90 alpha gene takes place at both the messenger RNA and the protein synthesis level. This response is protein synthesis dependent and DNA synthesis independent. The maximum level of hsp90 alpha mRNA accumulation always precedes the maximum level of thymidine incorporation, suggesting a possible link between cell cycle and hsp90 alpha regulation (Jérôme, V., J. Léger, J. Devin, E.E. Baulieu, and M. G. Catelli. Growth Factors 4:317-327, 1991). Herein, we examine the subcellular distribution of hsp90 and the cell cycle-dependent regulation of the hsp90 alpha mRNA level. We show that, in contrast to hsp70, the 35S metabolically-labeled hsp90, which accumulates in the cytosoluble fraction 6 to 8 h after serum treatment, is not preferentially translocated to the nuclear compartment, although a small fraction is always present in the nucleus. We also demonstrated that serum- or insulin-induced accumulation of hsp90 alpha mRNA results from an activation of gene transcription and that hsp90 alpha promotor activity, which is low in quiescent DU249 cells, is induced approximately fivefold after serum stimulation. Finally, in cell culture synchronized by nocodazole or aphidicholin, hsp90 alpha mRNA accumulation seems an event specific to G1/S transition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
205
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
44-51
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Cell cycle regulation of the chicken hsp90 alpha expression.
pubmed:affiliation
INSERM U33 (Communications Hormonales) and Faculté de Médecine, Université Paris-Sud. Lab. Hormones, Le Kremlin-Bicêtre, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't