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J. Biol. Chem., Vol. 262, Issue 35, 16763-16766, 12, 1987
RA Colbert, JA Hucul, KA Scorsone and DA Young
The use of ultra high resolution giant two-dimensional gel electrophoresis
has expanded the number of recognizable heat-shock proteins to 68
inductions in rat thymic lymphocytes, many of which are among the less
abundant cellular proteins (Maytin, E. V., Colbert, R. A., and Young, D. A.
(1985) J. Biol. Chem. 260, 2384-2392). Previous studies also show that
cells receiving a prior heat shock recover more rapidly from the inhibition
of protein synthesis induced by a second heat shock. In this report we use
a monoclonal antibody to identify the alpha subunit of eukaryotic
initiation factor-2 (eIF-2 alpha) as a heat- shock protein. Its relative
rate of synthesis increases approximately 40% in the 2nd h and 5-fold in
the 4th h of a continuous heat shock and is stimulated more dramatically,
15-fold, in the 3rd h of recovery from a 1-h heat shock. These results
suggest that the induction of eIF-2 alpha in the heat-shock response may be
important for restoring the cell's ability to initiate protein synthesis.
In addition to identifying a function for one of the heat-shock proteins,
our findings draw attention to the likelihood that other low-abundance
heat-shock proteins may play critical roles in the heat-shock response.
Alpha subunit of eukaryotic translational initiation factor-2 is a heat- shock protein
E. Henry Keutmann Laboratories, Department of Medicine, Rochester, New York.
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