Possible role of Hsp70 in autoantigens shuttling to dermo-epidermal junction in systemic lupus erythematosus

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R. Villalobos-Hurtado *
S.H. Sánchez-Rogriguez
E. Avalos-Díaz
R. Herrera-Esparza
(*) Corresponding Author:
R. Villalobos-Hurtado | office@pagepress.org

Abstract

Under stress cells and tissues perform a series of physiologic adjustments, including the heat shock protein production (Hsp), these proteins play a role as molecular chaperons, they are divided in five main families: Hsp27, Hsp 60, Hsp70, Hsp90 and Hsp110 (1). Hsp are constitutively induced or expressed to support the correct folding of novel proteins or to refold damaged proteins (2). Hsp70 is the most representative member of Hsp family. It is largely distributed in the majority of eukaryotic cell compartments and interact with the cytoskeleton during translocation of proteins across membranes (3).

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