Abstract |
An activated 40S ribosomal protein S6 kinase has been demonstrated previously in cytosolic extracts from proliferating as well as resting cells of a very undifferentiated rat ascites hepatoma cell line (Yoshida AH 130), grown in vivo (Cell Biol. Int. Rep., 1986, 10, 821-831). In the present report we present evidence of unmodified activity of this kinase and S6 phosphorylation in vitro in cells submitted to a physiological stress such as a sublethal temperature elevation (heat shock: 42 degrees C for 2 h). The heat treatment causes a progressive decline in the number of active ribosomes and of L-35S methionine incorporation into total protein, suggesting drastically decreased synthesis of cellular proteins under these conditions. Cells recovering from heat shock show the induced synthesis of a protein with an apparent Mr of 50 kDa. Spontaneous high expression of heat shock proteins (HSP 70, 89, 100), without heat shock, occurs in these tumor cells.
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Authors | R Comolli, M Frigerio, P Alberti |
Journal | Cell biology international reports
(Cell Biol Int Rep)
Vol. 12
Issue 10
Pg. 907-17
(Oct 1988)
ISSN: 0309-1651 [Print] England |
PMID | 2852063
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Heat-Shock Proteins
- Ribosomal Protein S6
- Ribosomal Proteins
- Phosphotransferases
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Topics |
- Animals
- Cell Line
- Cytosol
(enzymology)
- Female
- Heat-Shock Proteins
(biosynthesis)
- Liver Neoplasms, Experimental
(enzymology, metabolism)
- Phosphorylation
- Phosphotransferases
(metabolism)
- Rats
- Rats, Inbred Strains
- Ribosomal Protein S6
- Ribosomal Proteins
(metabolism)
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