Insights into peptidylarginine deiminase expression and citrullination pathways.
citrullination
histone citrullination
inflammation
neutrophil extracellular trap (NET)
peptidylarginine deiminase
rheumatoid arthritis
Journal
Trends in cell biology
ISSN: 1879-3088
Titre abrégé: Trends Cell Biol
Pays: England
ID NLM: 9200566
Informations de publication
Date de publication:
09 2022
09 2022
Historique:
received:
13
12
2021
revised:
25
01
2022
accepted:
28
01
2022
pubmed:
25
2
2022
medline:
17
8
2022
entrez:
24
2
2022
Statut:
ppublish
Résumé
Peptidylarginine deiminases (PADs) are calcium-dependent enzymes that mediate citrullination, an irreversible post-translational modification (PTM). PAD enzymes have received increasing attention in (patho-)physiology since multi-omics analysis accelerated their expression profiling. Here, we provide a comprehensive overview of PAD expression at the RNA and protein levels, and a list of annotated substrates per PAD isozyme. We discuss novel roles of citrullination in cellular growth, epigenetic regulation, tissue remodeling, inflammation, and cancer in mouse models and humans. Additionally, we cluster similar effects of protein deimination to offer a different perspective and improve our understanding of citrullination in health and disease. Citrullination should no longer be considered as a rare PTM, but as an important regulatory mechanism in physiology and pathology.
Identifiants
pubmed: 35197210
pii: S0962-8924(22)00030-7
doi: 10.1016/j.tcb.2022.01.014
pii:
doi:
Substances chimiques
Protein-Arginine Deiminases
EC 3.5.3.15
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
746-761Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.