The co-chaperones of heat shock proteins and disease - Literature review Example

From the accidental discovery of the HSPs, they continue to display important roles in the cell integrity. Research shows that the dysfunction of Mitochondrial in the skeletal muscles has been said to be important in a manner of T2DM. They do this by either reducing the ability to oxidize the fatty acids that lead to the accumulation of deleterious lipid species in the surrounding tissues such as the liver and the skeletal muscles and also by altering the cellular state of Redox. This mini-review will focus on defining and analyzing the functionalities of the heat shock proteins.

The presence of environmental stress in a cell stops or slows its ability to carry out most of its functions. These features include transport processes, RNA, DNA and protein synthesis. The model of the stress response by the HSPs is usually an abrupt rise in the external temperature known as the heat shock. Ferruccio Ritossa did the discovery of the heat shock response in 1962; he discovered them when he noticed an enlargement in some of the special sections of the heat shock puffs made after a heat treatment of the flies [1].

It later came clear that the segments contained particular forms of proteins known as the heat shock proteins. These types of proteins are induced by a massive variety of impulses apart from the thermal shock in the cells of an organism. HSPs usually play an important part in preventing various diseases with a fast rising role in the field of clinical practice. The functions of the HSPs in usually essential for the homeostasis of all the living cells, and often become vital in diseases when our bodily cells have to keep up with a stressful environment.

The advancement of our knowledge of the functions and the biochemistry of HSPs enable us to acquire more tools to give a mark to the patients. The advancements also make us to have close observations and improvements in the