Citrullination: A posttranslational modification in health and disease

Bence György, Erzsébet Tóth, Edit Tarcsa, A. Falus, E. Búzás

Research output: Contribution to journalArticle

270 Citations (Scopus)

Abstract

Posttranslational modifications are chemical changes to proteins that take place after synthesis. One such modification, peptidylarginine to peptidylcitrulline conversion, catalysed by peptidylarginine deiminases, has recently received significant interest in biomedicine. Introduction of citrulline dramatically changes the structure and function of proteins. It has been implicated in several physiological and pathological processes. Physiological processes include epithelial terminal differentiation, gene expression regulation, and apoptosis. Rheumatoid arthritis, multiple sclerosis, and Alzheimer's disease are examples of human diseases where protein citrullination involvement has been demonstrated. In this review, we discuss our current understanding on the importance of protein deimination in these processes. We describe the enzymes catalyzing the reaction, as well as their known protein substrates. We review the citrullinated peptide epitopes that are proposed as disease markers, specifically recognized in certain human autoimmune disorders. The potential autopathogenic role of citrullinated epitopes is also discussed.

Original languageEnglish
Pages (from-to)1662-1677
Number of pages16
JournalInternational Journal of Biochemistry and Cell Biology
Volume38
Issue number10
DOIs
Publication statusPublished - 2006

Fingerprint

Post Translational Protein Processing
Health
Physiological Phenomena
Proteins
Gene expression regulation
Epitopes
Citrulline
Chemical modification
Gene Expression Regulation
Pathologic Processes
Multiple Sclerosis
Rheumatoid Arthritis
Alzheimer Disease
Apoptosis
Peptides
Substrates
Enzymes

Keywords

  • Apoptosis
  • Autoimmunity
  • Biochemistry
  • Cell Biology
  • Clinical

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Citrullination : A posttranslational modification in health and disease. / György, Bence; Tóth, Erzsébet; Tarcsa, Edit; Falus, A.; Búzás, E.

In: International Journal of Biochemistry and Cell Biology, Vol. 38, No. 10, 2006, p. 1662-1677.

Research output: Contribution to journalArticle

@article{c3e98d05351b4e41927aa0d053828096,
title = "Citrullination: A posttranslational modification in health and disease",
abstract = "Posttranslational modifications are chemical changes to proteins that take place after synthesis. One such modification, peptidylarginine to peptidylcitrulline conversion, catalysed by peptidylarginine deiminases, has recently received significant interest in biomedicine. Introduction of citrulline dramatically changes the structure and function of proteins. It has been implicated in several physiological and pathological processes. Physiological processes include epithelial terminal differentiation, gene expression regulation, and apoptosis. Rheumatoid arthritis, multiple sclerosis, and Alzheimer's disease are examples of human diseases where protein citrullination involvement has been demonstrated. In this review, we discuss our current understanding on the importance of protein deimination in these processes. We describe the enzymes catalyzing the reaction, as well as their known protein substrates. We review the citrullinated peptide epitopes that are proposed as disease markers, specifically recognized in certain human autoimmune disorders. The potential autopathogenic role of citrullinated epitopes is also discussed.",
keywords = "Apoptosis, Autoimmunity, Biochemistry, Cell Biology, Clinical",
author = "Bence Gy{\"o}rgy and Erzs{\'e}bet T{\'o}th and Edit Tarcsa and A. Falus and E. B{\'u}z{\'a}s",
year = "2006",
doi = "10.1016/j.biocel.2006.03.008",
language = "English",
volume = "38",
pages = "1662--1677",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "10",

}

TY - JOUR

T1 - Citrullination

T2 - A posttranslational modification in health and disease

AU - György, Bence

AU - Tóth, Erzsébet

AU - Tarcsa, Edit

AU - Falus, A.

AU - Búzás, E.

PY - 2006

Y1 - 2006

N2 - Posttranslational modifications are chemical changes to proteins that take place after synthesis. One such modification, peptidylarginine to peptidylcitrulline conversion, catalysed by peptidylarginine deiminases, has recently received significant interest in biomedicine. Introduction of citrulline dramatically changes the structure and function of proteins. It has been implicated in several physiological and pathological processes. Physiological processes include epithelial terminal differentiation, gene expression regulation, and apoptosis. Rheumatoid arthritis, multiple sclerosis, and Alzheimer's disease are examples of human diseases where protein citrullination involvement has been demonstrated. In this review, we discuss our current understanding on the importance of protein deimination in these processes. We describe the enzymes catalyzing the reaction, as well as their known protein substrates. We review the citrullinated peptide epitopes that are proposed as disease markers, specifically recognized in certain human autoimmune disorders. The potential autopathogenic role of citrullinated epitopes is also discussed.

AB - Posttranslational modifications are chemical changes to proteins that take place after synthesis. One such modification, peptidylarginine to peptidylcitrulline conversion, catalysed by peptidylarginine deiminases, has recently received significant interest in biomedicine. Introduction of citrulline dramatically changes the structure and function of proteins. It has been implicated in several physiological and pathological processes. Physiological processes include epithelial terminal differentiation, gene expression regulation, and apoptosis. Rheumatoid arthritis, multiple sclerosis, and Alzheimer's disease are examples of human diseases where protein citrullination involvement has been demonstrated. In this review, we discuss our current understanding on the importance of protein deimination in these processes. We describe the enzymes catalyzing the reaction, as well as their known protein substrates. We review the citrullinated peptide epitopes that are proposed as disease markers, specifically recognized in certain human autoimmune disorders. The potential autopathogenic role of citrullinated epitopes is also discussed.

KW - Apoptosis

KW - Autoimmunity

KW - Biochemistry

KW - Cell Biology

KW - Clinical

UR - http://www.scopus.com/inward/record.url?scp=33745331328&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33745331328&partnerID=8YFLogxK

U2 - 10.1016/j.biocel.2006.03.008

DO - 10.1016/j.biocel.2006.03.008

M3 - Article

C2 - 16730216

AN - SCOPUS:33745331328

VL - 38

SP - 1662

EP - 1677

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 10

ER -