Induction of stress proteins by hyperosmolarity in normal and transformed cells.

The synthesis of at least three proteins, with molecular weights of approximately 87, 70, and 53 kd, was enhanced following the exposure of chick embryo fibroblasts to hyperosmolar shock of 30 min at 0.6 osM. Two of these proteins, the 87 and 70 kd, comigrated on one-dimensional gel electrophoresis with the stress proteins induced by heat shock after 30 min at 44 degrees C. In 3T3 cells, the hyperosmolar shock enhanced the expression of two proteins of 88 and 52 kd, whereas the heat shock increased the synthesis of several new polypeptides including the 88 and 52 kd mw. In SV40-transformed 3T3 cells the synthesis of two proteins of 72 and 69 kd was enhanced by heat shock, but no change of the protein pattern was recorded after the hyperosmolar shock.