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Reciprocal Relationship between Cell Death versus Heat Shock Proteins and Matrixmetalloproteinases in Normal and Cancer Cells
Author(s) -
Philips Neena
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.703.6
Subject(s) - heat shock protein , hsp27 , cancer cell , programmed cell death , microbiology and biotechnology , hsp70 , biology , cell , extracellular matrix , apoptosis , matrix metalloproteinase , cancer , cancer research , heat shock , biochemistry , genetics , gene
Heat shock proteins are stress response factors that are collectively anti‐apoptotic and protein stabilization chaperones. They also have specific functions: HSP27 induces cell differentiation, HSP immunity, and HSP90 is associated with cancer progression. Matrixmetalloproteinases (MMPs) facilitate extracellular matrix remodeling and cancer metastasis. While there is a clear reciprocal relationship between cell death and apoptosis, the relationship between cell death and heat shock proteins is complex. In normal and cancer cells, increased cell viability is associated with increased expression of all heat shock proteins suggesting that heat shock proteins facilitate cell survival. However, in normal cells under oxidative stress or cancer cells treated with potential chemotherapeutics there is direct relationship between cell loss and HSPs, which may imply that the surviving cells are supported by the increased expression of HSPs. The relationship between cell loss and expression of MMPs in normal and cancer cells is also direct. Treatment options require combating of the reciprocal effect of cell toxicity versus stimulation of HSPs and MMPs in cancer cells.