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Quantification of citrullination by means of skewed isotope distribution pattern

Marlies De Ceuleneer UGent, Katleen Van Steendam UGent, Maarten Dhaenens UGent, Dirk Elewaut UGent and Dieter Deforce UGent (2012) JOURNAL OF PROTEOME RESEARCH. 11(11). p.5245-5251
abstract
Citrullination is a post-translational modification of arginine, resulting in a loss of positive charge and a 1 Da mass increase. Research on citrullinated proteins is crucial in rheumatoid arthritis, an autoimmune disease characterized by the presence of antibodies against citrullinated proteins. However, little is known about the location or quantity of deiminated arginine residues in these proteins. Since citrullination gives rise to a mass gain of only 1 Da, the isotope pattern of the citrullinated and the noncitrullinated version of a peptide will overlap. However, the difference between the theoretical, or noncitrullinated, and the measured isotope pattern can be used to quantify the amount of citrullination. We developed a method to quantify citrullinated peptides by means of their skewed isotopic distribution pattern. The method was first optimized with synthetic peptides, after both direct infusion and RP-HPLC separation on an ESi-QqTOF mass spectrometer. Additionally, we analyzed synovial fluid samples from rheumatoid arthritis patients and were able to quantify citrullinated peptides originating from citrullinated fibrinogen, a well-known antigen
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
rheumatoid arthritis, citrulline, label-free quantitation, posttranslational modification, RHEUMATOID-ARTHRITIS, SYNOVIAL-FLUID, IMMUNE-COMPLEXES, ANTIBODIES, FIBRINOGEN, IDENTIFICATION, SPECTROMETRY, PROTEINS
journal title
JOURNAL OF PROTEOME RESEARCH
J. Proteome Res.
volume
11
issue
11
pages
5245 - 5251
Web of Science type
Article
Web of Science id
000311190600011
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
5.056 (2012)
JCR rank
10/74 (2012)
JCR quartile
1 (2012)
ISSN
1535-3893
DOI
10.1021/pr3004453
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2998860
handle
http://hdl.handle.net/1854/LU-2998860
date created
2012-09-25 11:06:50
date last changed
2013-01-21 10:03:31
@article{2998860,
  abstract     = {Citrullination is a post-translational modification of arginine, resulting in a loss of positive charge and a 1 Da mass increase. Research on citrullinated proteins is crucial in rheumatoid arthritis, an autoimmune disease characterized by the presence of antibodies against citrullinated proteins. However, little is known about the location or quantity of deiminated arginine residues in these proteins. Since citrullination gives rise to a mass gain of only 1 Da, the isotope pattern of the citrullinated and the noncitrullinated version of a peptide will overlap. However, the difference between the theoretical, or noncitrullinated, and the measured isotope pattern can be used to quantify the amount of citrullination. We developed a method to quantify citrullinated peptides by means of their skewed isotopic distribution pattern. The method was first optimized with synthetic peptides, after both direct infusion and RP-HPLC separation on an ESi-QqTOF mass spectrometer. Additionally, we analyzed synovial fluid samples from rheumatoid arthritis patients and were able to quantify citrullinated peptides originating from citrullinated fibrinogen, a well-known antigen},
  author       = {De Ceuleneer, Marlies and Van Steendam, Katleen and Dhaenens, Maarten and Elewaut, Dirk and Deforce, Dieter},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {rheumatoid arthritis,citrulline,label-free quantitation,posttranslational modification,RHEUMATOID-ARTHRITIS,SYNOVIAL-FLUID,IMMUNE-COMPLEXES,ANTIBODIES,FIBRINOGEN,IDENTIFICATION,SPECTROMETRY,PROTEINS},
  language     = {eng},
  number       = {11},
  pages        = {5245--5251},
  title        = {Quantification of citrullination by means of skewed isotope distribution pattern},
  url          = {http://dx.doi.org/10.1021/pr3004453},
  volume       = {11},
  year         = {2012},
}

Chicago
De Ceuleneer, Marlies, Katleen Van Steendam, Maarten Dhaenens, Dirk Elewaut, and Dieter Deforce. 2012. “Quantification of Citrullination by Means of Skewed Isotope Distribution Pattern.” Journal of Proteome Research 11 (11): 5245–5251.
APA
De Ceuleneer, M., Van Steendam, K., Dhaenens, M., Elewaut, D., & Deforce, D. (2012). Quantification of citrullination by means of skewed isotope distribution pattern. JOURNAL OF PROTEOME RESEARCH, 11(11), 5245–5251.
Vancouver
1.
De Ceuleneer M, Van Steendam K, Dhaenens M, Elewaut D, Deforce D. Quantification of citrullination by means of skewed isotope distribution pattern. JOURNAL OF PROTEOME RESEARCH. 2012;11(11):5245–51.
MLA
De Ceuleneer, Marlies, Katleen Van Steendam, Maarten Dhaenens, et al. “Quantification of Citrullination by Means of Skewed Isotope Distribution Pattern.” JOURNAL OF PROTEOME RESEARCH 11.11 (2012): 5245–5251. Print.