Involvement of Heat Shock Protein 70 (Hsp70) in Gastrointestinal Cancers

Intracellular protein homeostasis is largely controlled by Heat shock proteins (Hsp). Heat shock proteins (Hsp) impart an age-old defense mechanism for all forms of life on earth. Misfolded proteins are refolded with the aid of Hsp and proteins which are damaged beyond repair are eliminated with assistance from Hsp. Hsp are known as molecular chaperones for their cytoprotective roles. In cancer cells the Hsp are frequently overexpressed and are assumed to be associated with tumor formation. Hsp demonstrate specific affinity to particular classes of oncogenic peptides and client proteins in cancer cells, and are able to stabilize mutated oncogene proteins. They play a key regulatory role in prevention of apoptotic cell death during tumorigenesis and thereby enhance cell growth and proliferation. They may also promote chemoresistance in cancer cells. Here we present the current knowledge on the role of molecular chaperones in particular heat shock protein 70 (Hsp70) in human gastrointestinal cancers along with their therapeutic targeting. This review will focus on the role of Hsp 70 and related chaperones in several gastrointestinal cancers such as pancreatic, gastric, and liver cancers.