Synthesis and phosphorylation of hepatic proteins in rats exposed to hyperthermic shock
1994
Butorovic, B. | Matic, G. | Kipic, J. | Dundjerski, J. | Trajkovic, D. (Institute for Biological Research "Sinisa Stankovic", Belgrade (Yugoslavia). Department of Molecular Biology and Biochemistry)
Heat shock reduced the number and content of many proteins suggesting a decrease in total synthetic rate of hepatic proteins. At the same time, a number of newly-synthesized proteins was observed, including some proteins molecular mass which correspond to HSPs 110, 90, 70 and 32, especially in the group recovering for 240 min. Heat shock rapidly triggered phosphorylation of a set of rat hepatic proteins. The major identified phosphorylation products comigrated with proteins Mr of 38 and 67 kDa. Application of SDS-PAGE, Western blot and AC-88 as a specific antibody for HSP90, revealed two isoforms of this protein (89 and 94 kDa). Exposure of animals to heat shock led to a decrease in the content of these two isoforms. At the same time, a multiple increase in the extent of phosphorylation of both 90 kDa protein and 94 kDa isoform was recorded.
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