Molecular Chaperones in the Kidney

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Abstract
▪ Abstract The normal milieu of the kidney includes hypoxia, large osmotic fluxes, and an enormous amount of fluid/solute reabsorption. Renal adaptation to these conditions requires a host of molecular chaperones that stabilize protein conformation, target nascent proteins to their final intracellular destination, and prevent protein aggregation. Under physiologic or pharmacologic stress, inducible molecular chaperones provide additional mechanisms for repairing or degrading non-native proteins and for inhibiting stress-induced apoptosis. In contrast to intracellular chaperones, chaperones present on the cell surface regulate the immune system and have cytokine-like effects. A diverse range of chaperones and chaperone functions provide the renal cell with an armamentarium of responses to improve the chances of survival.