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[This retracts the article DOI: 10.7759/cureus.18316.].
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[This corrects the article DOI: 10.7759/cureus.18316.].
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This review article has been necessitated by the limited number of studies on the role of heat shock proteins (HSPs) in cellular functions. The analysis is performed by reviewing evidence in various literary works concerning the topic. The main function of HSPs is to prevent the formation of non-functional proteins and facilitate protein folding. They also enhance the survival of cells in addition to being clinically significant. HSPs protect proteins from stress factors such as temperature, pH, and low levels of oxygen. Some of the common types of HSPs include HSP70, HSP90, HSP27, and HSP100. These proteins have different weights and other features which make them suit for different cellular functions. However, they have numerous similar features which make them perform almost the same functions, yet they vary in the degree of protection that they provide for the cells. The release of HSPs is controlled by four types of HSF depending on the type of stress that a cell is subjected to. HSF1 is responsible for identifying stress factors, especially heat. HSF2 performs almost similar functions as HSF1 in addition to cellular development. HSF3 is released when the stress conditions are extreme and, hence, cannot be effectively controlled by HSF1 and HSF2. HSF4 functions by inducing negative DNA transcriptions. Other tasks of HSPs include enhancing the immune system. The cells help in the management of Alzheimer's disease and other similar complications by forming protective tissues around brain cells. The cells also help in controlling cancer and heart diseases. However, their roles are more enhanced in managing cancer, extending to diagnosis and prediction. Further research on the HSPs and HSFs may extend their application to curing tumorous cells.
