García UAC, Rodríguez DFG, Fernández AO, Torres VA, Ortega R, Montiel F

Language: Spanish
References: 25
Page: 148-154
PDF size: 245.84 Kb.

ABSTRACT

Our knowledge on the chaperones, the main subfamily of stress proteins, has dramatically increased during the past 20 years. Even though since the beginning it was suspected that this class of proteins may participate in the protection and survival of the stressed cell, no one anticipated the many and surprising ways in which these molecules are involved in cellular metabolism and human patophysiology. Exploiting the basic molecular principle of polypeptide-polypeptide interaction, stress proteins (Hsp90, Hsp70, Hsp60, etc.) participate in protein folding, intracellular transport, antigenic peptide presentation, induction of maturation in dendritic cells, cellular transformation and necrotic death signals, etc. These multifunctional proteins may even be acting as molecular capacitors buffering genetic changes and modulating cell development and evolution.

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