Heat shock proteins (HSPs) are a type of protein that are produced by cells in response to stress.
The stress can be caused by things like high temperatures, chemicals, or physical stress.
HSPs play an important role in helping cells to maintain their normal function and survive under stress.
One of the main functions of HSPs is to help protein folding.
When a cell is under stress, the proteins in the cell can become damaged or misfolded. HSPs can help to refold these proteins, which helps to prevent cellular damage.
Additionally, HSPs have also been shown to play a role in preventing protein aggregation and promoting protein degradation, as well as in regulating cellular signaling pathways.
Mutations in HSP genes have been associated with various diseases, including cancer, Alzheimer’s disease, and Huntington’s disease.
Molecules essential for cell life and overexpressed in a variety of human cancers.
Implicated in tumor cell growth and differentiation.
A molecular chaperone, required for refolding proteins during stress and for conformational maturation of key signaling proteins.
HER-2 receptor most sensitive association.
Inhibition causes ubiquitination of heat shock associated proteins and their trafficking to the proteasome, where they are degraded.
Hsp60 and Hps10 are mitochondrial molecular agents that when overexpressed protect cells from ischemia, hypoxemia, oxidative injury and maintain mitochondrial integrity and function, suppress mitochondrial membrane permeability, inhibit apoptosis and necrotic cell death.
Hsp60 and Hps10 overexpressed during endocervical, colorectal and prostate carcinogenesis..