Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification |
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Authors: | Sakamoto Hiroshi Mashima Tetsuo Yamamoto Kazuo Tsuruo Takashi |
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Affiliation: | Cancer Chemotherapy Center, Japanese Foundation for Cancer Research, Tokyo, 170-8455, Japan. |
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Abstract: | Methylglyoxal (MG) is one of the side-products in glycolysis, and it reacts with proteins under physiological conditions. Here, we identified heat-shock protein 27 (Hsp27) as a major MG-modified protein in cells. MG modification of Hsp27 selectively occurs at Arg-188 to form argpyrimidine, and mutation in the residue represses the formation of a large oligomer. This modification process is essential to its repressing activity for cytochrome c-mediated caspase activation. Inhibition of MG modification of Hsp27 causes sensitization of the cells to anti-tumor drug-induced apoptosis. Thus, MG is a novel modulator of cell survival by directly incorporating with the specific protein residue. |
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