The emerging role of dipeptidyl peptidase 3 in pathophysiology.
Keap1-Nrf2 pathway
bioactive peptides
cancer
dipeptidyl peptidase 3 (DPP3)
metalloprotease
oxidative stress
renin angiotensin system (RAS)
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
05 2023
05 2023
Historique:
revised:
25
02
2022
received:
05
01
2022
accepted:
10
03
2022
medline:
4
5
2023
pubmed:
13
3
2022
entrez:
12
3
2022
Statut:
ppublish
Résumé
Dipeptidyl peptidase 3 (DPP3), a zinc-dependent aminopeptidase, is a highly conserved enzyme among higher animals. The enzyme cleaves dipeptides from the N-terminus of tetra- to decapeptides, thereby taking part in activation as well as degradation of signalling peptides critical in physiological and pathological processes such as blood pressure regulation, nociception, inflammation and cancer. Besides its catalytic activity, DPP3 moonlights as a regulator of the cellular oxidative stress response pathway, e.g., the Keap1-Nrf2 mediated antioxidative response. The enzyme is also recognized as a key modulator of the renin-angiotensin system. Recently, DPP3 has been attracting growing attention within the scientific community, which has significantly augmented our knowledge of its physiological relevance. Herein, we review recent advances in our understanding of the structure and catalytic activity of DPP3, with a focus on attributing its molecular architecture and catalytic mechanism to its wide-ranging biological functions. We further highlight recent intriguing reports that implicate a broader role for DPP3 as a valuable biomarker in cardiovascular and renal pathologies and furthermore discuss its potential as a promising drug target.
Substances chimiques
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
EC 3.4.14.-
Kelch-Like ECH-Associated Protein 1
0
NF-E2-Related Factor 2
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2246-2262Informations de copyright
© 2022 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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