The role of heat shock proteins and glucose regulated proteins in cancer
- Author:
Jia Shin Jessica Tan
;
Kien Chai Ong
;
Anthony Rhodes
- Publication Type:Review
- Keywords:
Glucose regulated protein;
cancer
- From:The Malaysian Journal of Pathology
2016;38(2):75-82
- CountryMalaysia
- Language:English
-
Abstract:
Heat shock proteins (HSPs) are a family of evolutionary conserved proteins that work as molecular
chaperones for cellular proteins essential for cell viability and growth as well as having numerous
cyto-protective roles. They are sub-categorised based on their molecular weights; amongst which
some of the most extensively studied are the HSP90 and HSP70 families. Important members of
these two families; Heat shock proteins 70 and heat shock proteins 90 (Hsp70/90), are the glucose
regulated proteins (GRP). These stress-inducible chaperones possess distinct roles from that of the
other HSPs, residing mostly in the endoplasmic reticulum and mitochondria, but they can also be
translocated to other cellular locations. Their ability in adapting to stress conditions in the tumour
microenvironment suggests novel functions in cancer. GRPs have been implicated in many crucial
steps of carcinogenesis to include stabilization of oncogenic proteins, induction of tumour angiogenesis,
inhibition of apoptosis and replicative senescence, and promotion of invasion and metastasis.
- Full text:P020161004009648634242.pdf
