CATHEPSIN D: MOLECULAR, GENETIC AND FUNCTIONAL ASPECTS IN THE TUMOR MICROENVIRONMENT

Cathepsin D (catD) is an endoprotease acidic lysosomal protein (aspartyl protease) found in virtually all mammalian cells that was initially associated with the degradation of nonspecific polypeptides. Initially, it is formed as inactive proenzymes that are subsequently activated by the proteolytic removal of the N-terminal propeptide. The detailed physiological function of catD is poorly understood. However, it is considered a multifunctional protease responsible for essential biological processes related to the regulation of the cell cycle, differentiation, migration, tissue remodeling, neuronal growth, ovulation and apoptosis. In addition, it has been reported in inflammatory and neurodegenerative processes, as a potential tumor marker and in carcinogenesis. Given its relevance, this study reviewed and characterized integrative data on the molecular and functional aspects of catD associated with the tumor microenvironment. The results provide a scientific overview of cathepsin D and its participation in the tumor microenvironment that can support new studies and prospective trials focused on carcinogenesis.