Special Issue "Dipeptidyl Peptidases: From Structure to Function"
Deadline for manuscript submissions: closed (20 July 2023) | Viewed by 814
Dipeptidyl peptidases (DPPs) belong to a family of peptidases that consists of 8 members in mamals, DPP1 (cathepsin C), DPP2 (DPP7), DPP3, DPP4, DPP6, DPP8, DPP9 and DPP10. It is a diverse family consisting of the proteins with the enzymatic activity that cleave dipeptides from the amino-termini of oligopeptides or polypeptides, and catalitically inactive proteins (DPP6 and DPP10). Enzymatically active members belong to different groups of peptidases, based on the mechanism of catalysis. DPP1 is a cystein peptidase, DPP2, 4, 8 and 9 are serine peptidases, while DPP3 is a metallopeptidase. The most thorougly investigated protein of the family is DPP4, which is mainly located on membranes, but it is also found in a circulationg form. It is involved in glucose-metabolism and is a therapeutic target in diabetes, but it is also a differentiation marker in T-lymphocytes, where it is called CD26. The only metallopeptides in the family, DPP3, which was first identified in the 1960s has regained interest in the last decade after the discovery of its role in the oxidative stress response regulation, and its identification as a potential biomaker or even therapeutic target of cardiogenic shock. Other proteins from the family have important roles in immune system, however, their patophysiological roles are still largely obscure, and are the targets of ongoing investigations.
Dr. Mihaela Matovina
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- dipeptidyl peptidase
- protein structure
- protein-protein interactions
- cell signaling
- oxidative stress
- immune control