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Heat shock proteins in human cancer
Author(s) -
Sarto Cecilia,
Binz PierreAlain,
Mocarelli Paolo
Publication year - 2000
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(20000401)21:6<1218::aid-elps1218>3.0.co;2-h
Subject(s) - heat shock protein , organelle , protein folding , cancer cell , microbiology and biotechnology , folding (dsp implementation) , hsp70 , function (biology) , cancer , biology , chemistry , biochemistry , biophysics , genetics , gene , engineering , electrical engineering
The heat shock proteins (hsp) are ubiquitous molecules induced in cells exposed to sublethal heat shock, present in all living cells, and highly conserved during evolution. Their function is to protect cells from environmental stress damage by binding to partially denatured proteins, dissociating protein aggregates, to regulate the correct folding, and to cooperate in transporting newly synthesized polypeptides to the target organelles. The molecular chaperones are involved in numerous diseases, including cancer, revealing changes of expression. In this review, we mainly describe the relationship of hsp expression with human cancer, and discuss what is known about their post‐translational modifications according to malignancies.