The Role of Heat Shock Protein 70 (HSP70) in the Pathogenesis of Ocular Diseases-Current Literature Review

Heat shock proteins (HSPs) have been attracting the attention of researchers for many years. HSPs are a family of ubiquitous, well-characterised proteins that are generally regarded as protective multifunctional molecules that are expressed in response to different types of cell stress. Their activity in many organs has been reported, including the heart, brain, and retina. By acting as chaperone proteins, HSPs help to refold denatured proteins. Moreover, HSPs elicit inhibitory activity in apoptotic pathways and inflammation. Heat shock proteins were originally classified into several subfamilies, including the HSP70 family. The aim of this paper is to systematise information from the available literature about the presence of HSP70 in the human eye and its role in the pathogenesis of ocular diseases. HSP70 has been identified in the cornea, lens, and retina of a normal eye. The increased expression and synthesis of HSP70 induced by cell stress has also been demonstrated in eyes with pathologies such as glaucoma, eye cancers, cataracts, scarring of the cornea, ocular toxpoplasmosis, PEX, AMD, RPE, and diabetic retinopathy. Most of the studies cited in this paper confirm the protective role of HSP70. However, little is known about these molecules in the human eye and their role in the pathogenesis of eye diseases. Therefore, understanding the role of HSP70 in the pathophysiology of injuries to the cornea, lens, and retina is essential for the development of new therapies aimed at limiting and/or reversing the processes that cause damage to the eye.