Peptidases: Role and Function in Health and Disease

Dear Colleagues,

Peptidases represent a large family of hydrolases, present in all living organisms, which catalyze the degradation of peptide bonds in different biological processes. Two percent of all genes encode peptidases and their homologues in all kinds of organisms, and there are almost 600 active and putative peptidases in the human genome. They can be classified into seven main groups according to their structure and catalytic type: serine, cysteine, threonine, aspartyl, glutamyl, asparaginyl, and metallopeptidases. Peptidases are involved in the degradation of proteins in lysosomes, cytosol, plasma membrane or in extracellular space; however, they may also have regulatory functions, controlling various biological processes crucial for cell homeostasis. However, besides being involved in normal protein turnover, their irregular function has been associated with a number of pathological processes in cancer, neurodegenerative, immune and cardiovascular disorders, rheumatoid arthritis, osteoarthritis, viral infections, atherosclerosis, periodontitis, pancreatitis, osteoporosis, diseases of the insufficient lysosomal degradation of proteins, and more. In this Special Issue, we would like to highlight new aspects of the proteolytic system in maintaining life functions and to present advanced approaches to neutralize the harmful proteolytic activity associated with pathological processes.    

Prof. Dr. Janko Kos
Guest Editor

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