Peptidylarginine deiminase and citrullination

Potential therapeutic targets for inflammatory diseases

Byungki Jang, SungJae Shin

Research output: Contribution to journalReview article

3 Citations (Scopus)

Abstract

The multiple post-translational modifications of proteins display specific gain- or loss-of-function under normal and abnormal conditions. These modifications are precisely regulated by post-translational modification enzymes. The altered molecular status perturbs the pattern of gene expression and decides on a direction to signal transduction cascades as well as intrinsic properties of the proteins. Ultimately, it strictly maintains intracellular environment or results in disease manifestations. Recently, it has become that enzyme-dependent modification of arginine residue to citrulline exerts an important role in the induction of autoimmunity including rheumatoid arthritis, multiple sclerosis, and cancer. The modification of arginine residue to citrulline on proteins is called 'citrullination' or 'deimination' and is regulated by the calcium-dependent enzyme peptidylarginine deiminase (PAD). Now many effective PAD inhibitors (for example, Cl-amidine) have developed that ameliorates disease phenotypes. In this review, we discuss crucial roles of PAD enzyme and citrullination, the effectiveness of PAD inhibitors, and the implication in pathology.

Original languageEnglish
Pages (from-to)159-167
Number of pages9
JournalJournal of Bacteriology and Virology
Volume43
Issue number3
DOIs
Publication statusPublished - 2013 Jan 1

Fingerprint

Citrulline
Enzymes
Post Translational Protein Processing
Arginine
Therapeutics
Autoimmunity
Multiple Sclerosis
Signal Transduction
Rheumatoid Arthritis
Proteins
Pathology
Calcium
Phenotype
Gene Expression
protein-arginine deiminase
Neoplasms
Direction compound
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Virology

Cite this

@article{382711bc4c944d39b88053e07658f29f,
title = "Peptidylarginine deiminase and citrullination: Potential therapeutic targets for inflammatory diseases",
abstract = "The multiple post-translational modifications of proteins display specific gain- or loss-of-function under normal and abnormal conditions. These modifications are precisely regulated by post-translational modification enzymes. The altered molecular status perturbs the pattern of gene expression and decides on a direction to signal transduction cascades as well as intrinsic properties of the proteins. Ultimately, it strictly maintains intracellular environment or results in disease manifestations. Recently, it has become that enzyme-dependent modification of arginine residue to citrulline exerts an important role in the induction of autoimmunity including rheumatoid arthritis, multiple sclerosis, and cancer. The modification of arginine residue to citrulline on proteins is called 'citrullination' or 'deimination' and is regulated by the calcium-dependent enzyme peptidylarginine deiminase (PAD). Now many effective PAD inhibitors (for example, Cl-amidine) have developed that ameliorates disease phenotypes. In this review, we discuss crucial roles of PAD enzyme and citrullination, the effectiveness of PAD inhibitors, and the implication in pathology.",
author = "Byungki Jang and SungJae Shin",
year = "2013",
month = "1",
day = "1",
doi = "10.4167/jbv.2013.43.3.159",
language = "English",
volume = "43",
pages = "159--167",
journal = "Journal of Bacteriology and Virology",
issn = "1598-2467",
publisher = "Chonnam National University Medical School",
number = "3",

}

Peptidylarginine deiminase and citrullination : Potential therapeutic targets for inflammatory diseases. / Jang, Byungki; Shin, SungJae.

In: Journal of Bacteriology and Virology, Vol. 43, No. 3, 01.01.2013, p. 159-167.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Peptidylarginine deiminase and citrullination

T2 - Potential therapeutic targets for inflammatory diseases

AU - Jang, Byungki

AU - Shin, SungJae

PY - 2013/1/1

Y1 - 2013/1/1

N2 - The multiple post-translational modifications of proteins display specific gain- or loss-of-function under normal and abnormal conditions. These modifications are precisely regulated by post-translational modification enzymes. The altered molecular status perturbs the pattern of gene expression and decides on a direction to signal transduction cascades as well as intrinsic properties of the proteins. Ultimately, it strictly maintains intracellular environment or results in disease manifestations. Recently, it has become that enzyme-dependent modification of arginine residue to citrulline exerts an important role in the induction of autoimmunity including rheumatoid arthritis, multiple sclerosis, and cancer. The modification of arginine residue to citrulline on proteins is called 'citrullination' or 'deimination' and is regulated by the calcium-dependent enzyme peptidylarginine deiminase (PAD). Now many effective PAD inhibitors (for example, Cl-amidine) have developed that ameliorates disease phenotypes. In this review, we discuss crucial roles of PAD enzyme and citrullination, the effectiveness of PAD inhibitors, and the implication in pathology.

AB - The multiple post-translational modifications of proteins display specific gain- or loss-of-function under normal and abnormal conditions. These modifications are precisely regulated by post-translational modification enzymes. The altered molecular status perturbs the pattern of gene expression and decides on a direction to signal transduction cascades as well as intrinsic properties of the proteins. Ultimately, it strictly maintains intracellular environment or results in disease manifestations. Recently, it has become that enzyme-dependent modification of arginine residue to citrulline exerts an important role in the induction of autoimmunity including rheumatoid arthritis, multiple sclerosis, and cancer. The modification of arginine residue to citrulline on proteins is called 'citrullination' or 'deimination' and is regulated by the calcium-dependent enzyme peptidylarginine deiminase (PAD). Now many effective PAD inhibitors (for example, Cl-amidine) have developed that ameliorates disease phenotypes. In this review, we discuss crucial roles of PAD enzyme and citrullination, the effectiveness of PAD inhibitors, and the implication in pathology.

UR - http://www.scopus.com/inward/record.url?scp=84907854795&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84907854795&partnerID=8YFLogxK

U2 - 10.4167/jbv.2013.43.3.159

DO - 10.4167/jbv.2013.43.3.159

M3 - Review article

VL - 43

SP - 159

EP - 167

JO - Journal of Bacteriology and Virology

JF - Journal of Bacteriology and Virology

SN - 1598-2467

IS - 3

ER -