Arsenate induces stress proteins in cultured rat myoblasts.

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Abstract
The induction of stress proteins was examined in rat myoblast cultures by 2-dimensional gel electrophoresis. Arsenate, which behaved as a phosphate analog in cellular phosphate-transfer reactions, stressed cultured rat cells and induced the synthesis of a unique set of proteins. Most of the proteins synthesized after the addition of arsenate were identical to proteins synthesized in rat myoblasts in response to heat shock or arsenite stress. Both As salts induced the synthesis of 2 unique proteins not induced by heat shock. Five 25-30 kdalton stress proteins of rat cells did not contain Met residues. A majority of the proteins synthesized in stressed myogenic cells were also induced by stress in other rat cells such as hepatoma cells, pituitary tumor cells and fibroblasts. The 25-30 kdalton stress-related proteins identified in myogenic cells were induced in fibroblasts but not hepatoma or pituitary cells.

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