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In vivo relevance of citrullinated proteins and the challenges in their detection

Marlies De Ceuleneer UGent, Katleen Van Steendam UGent, Maarten Dhaenens UGent and Dieter Deforce UGent (2012) PROTEOMICS. 12(6). p.752-760
abstract
Citrullination is a posttranslational modification of arginine. It plays both a physiological role, for instance during apoptosis and epigenetics, and a pathological role in cancer or diseases of the central nervous system. Most research on citrullination to date focuses on its role in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis. In this context, the exact knowledge of citrullination sites in a protein can provide invaluable information about the etiological importance of these citrullinated proteins. However, few techniques exist that can accurately detect citrullination on the peptide level. This review aims to give an overview of the different methods available to date for the detection of citrullinated proteins and peptides. These include 2D-SDS-PAGE and immunodetection, as well as specific mass spectrometry approaches, both labelled and unlabelled. These MS approaches have been developed to pinpoint the exact location of citrullination on the peptide level. Improving the currently existing detection strategies while focussing on the role of citrullinated proteins will be invaluable to elucidate the importance of this posttranslational modification in vivo.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
keyword
2D-PAGE, Citrullination, Mass spectrometry, Posttranslational modification, Specific labeling, Technology, RHEUMATOID-ARTHRITIS, PEPTIDYLARGININE-DEIMINASE, MASS-SPECTROMETRY, PADI4 EXPRESSION, SYNOVIAL TISSUE, AUTOANTIBODIES, PROTEOMICS, PEPTIDE, IDENTIFICATION, PATHOGENESIS
journal title
PROTEOMICS
Proteomics
volume
12
issue
6
pages
752 - 760
Web of Science type
Review
Web of Science id
000303232800002
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
4.132 (2012)
JCR rank
14/74 (2012)
JCR quartile
1 (2012)
ISSN
1615-9853
DOI
10.1002/pmic.201100478
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2063368
handle
http://hdl.handle.net/1854/LU-2063368
date created
2012-03-09 09:49:34
date last changed
2012-09-12 10:51:52
@article{2063368,
  abstract     = {Citrullination is a posttranslational modification of arginine. It plays both a physiological role, for instance during apoptosis and epigenetics, and a pathological role in cancer or diseases of the central nervous system. Most research on citrullination to date focuses on  its role in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis. In this context, the exact knowledge of citrullination sites in a protein can provide invaluable information about the etiological importance of these citrullinated proteins. However, few techniques exist that can accurately detect citrullination on the peptide level.
This review aims to give an overview of the different methods available to date for the detection of citrullinated proteins and peptides. These include 2D-SDS-PAGE and immunodetection, as well as specific mass spectrometry approaches, both labelled and unlabelled. These MS approaches have been developed to pinpoint the exact location of citrullination on the peptide level. 
Improving the currently existing detection strategies while focussing on the role of citrullinated proteins will be invaluable to elucidate the importance of this posttranslational modification in vivo.},
  author       = {De Ceuleneer, Marlies and Van Steendam, Katleen and Dhaenens, Maarten and Deforce, Dieter},
  issn         = {1615-9853},
  journal      = {PROTEOMICS},
  keyword      = {2D-PAGE,Citrullination,Mass spectrometry,Posttranslational modification,Specific labeling,Technology,RHEUMATOID-ARTHRITIS,PEPTIDYLARGININE-DEIMINASE,MASS-SPECTROMETRY,PADI4 EXPRESSION,SYNOVIAL TISSUE,AUTOANTIBODIES,PROTEOMICS,PEPTIDE,IDENTIFICATION,PATHOGENESIS},
  language     = {eng},
  number       = {6},
  pages        = {752--760},
  title        = {In vivo relevance of citrullinated proteins and the challenges in their detection},
  url          = {http://dx.doi.org/10.1002/pmic.201100478},
  volume       = {12},
  year         = {2012},
}

Chicago
De Ceuleneer, Marlies, Katleen Van Steendam, Maarten Dhaenens, and Dieter Deforce. 2012. “In Vivo Relevance of Citrullinated Proteins and the Challenges in Their Detection.” Proteomics 12 (6): 752–760.
APA
De Ceuleneer, M., Van Steendam, K., Dhaenens, M., & Deforce, D. (2012). In vivo relevance of citrullinated proteins and the challenges in their detection. PROTEOMICS, 12(6), 752–760.
Vancouver
1.
De Ceuleneer M, Van Steendam K, Dhaenens M, Deforce D. In vivo relevance of citrullinated proteins and the challenges in their detection. PROTEOMICS. 2012;12(6):752–60.
MLA
De Ceuleneer, Marlies, Katleen Van Steendam, Maarten Dhaenens, et al. “In Vivo Relevance of Citrullinated Proteins and the Challenges in Their Detection.” PROTEOMICS 12.6 (2012): 752–760. Print.