Abstract
Heat shock proteins (Hsps) are highly conserved chaperone protein family which is responsible for proper folding of newly synthesized and misfolded proteins, cellular signaling, and prevention of protein aggregation. Hsps consist of six major members: small Hsps (<30 kDa), Hsp40 (40 kDa), Hsp60 (60 kDa), Hsp70 (70 kDa), Hsp90 (90 kDa), and Hsp100 (100 kDa). Hsps are found at different parts of the cell (mitochondria, endoplasmic reticulum, cytosol) and their expression level is increased under cellular stress conditions (i.e. malignancy, infection, heavy metals, heat, hypoxia, and oxidative stress). Therefore, expression of high levels of Hsps is related with disease’s pathogenesis.
Highlights
Heat shock proteins (Hsps) are highly conserved chaperone protein family which is responsible for proper folding of newly synthesized and misfolded proteins, cellular signaling, and prevention of protein aggregation
Hsps are found at different parts of the cell and their expression level is increased under cellular stress conditions
We investigate potential roles of Hsps in tumoregenesis and pathogenesis of infection diseases
Summary
Heat shock proteins (Hsps) are highly conserved chaperone protein family which is responsible for proper folding of newly synthesized and misfolded proteins, cellular signaling, and prevention of protein aggregation. Hsps are found at different parts of the cell (mitochondria, endoplasmic reticulum, cytosol) and their expression level is increased under cellular stress conditions (i.e. malignancy, infection, heavy metals, heat, hypoxia, and oxidative stress). We investigate potential roles of Hsps in tumoregenesis and pathogenesis of infection diseases. Toxoplasmosis is an important infection disease caused by the protozoan Toxoplasma gondii.
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