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Article ; Online: Citrullinated proteins: sparks that may ignite the fire in rheumatoid arthritis.

Vossenaar, Erik R / van Venrooij, Walther J

2004 Volume 6, Issue 3, Page(s) 107–111

Abstract: Antibodies directed to citrullinated proteins (e.g. anti-CCP [cyclic citrullinated peptide] antibodies) are highly specific for rheumatoid arthritis (RA). These antibodies are produced at the site of inflammation in RA, and therefore citrullinated ... ...

Abstract	Antibodies directed to citrullinated proteins (e.g. anti-CCP [cyclic citrullinated peptide] antibodies) are highly specific for rheumatoid arthritis (RA). These antibodies are produced at the site of inflammation in RA, and therefore citrullinated antigens are also expected to be present in the inflamed synovium. We discuss literature showing that the presence of citrullinated proteins in the synovium is not specific for RA. The RA-specific antibodies are therefore most likely the result of an abnormal immune response that specifically occurs in RA patients. It was recently shown that presence of anti-CCP antibodies precedes the onset of clinical symptoms of RA by years. It thus appears that it may take years for initial events that cause the generation of anti-CCP antibodies to develop into full-blown disease.
MeSH term(s)	Animals ; Arthritis, Rheumatoid/pathology ; Autoantibodies/biosynthesis ; Humans ; Inflammation/immunology ; Peptides, Cyclic/immunology
Chemical Substances	Autoantibodies ; Peptides, Cyclic ; cyclic citrullinated peptide
Language	English
Publishing date	2004
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2107602-9
ISSN	1478-6362 ; 1478-6354
ISSN (online)	1478-6362
ISSN	1478-6354
DOI	10.1186/ar1184
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Article: Autoantibodies to citrullinated (poly)peptides: a key diagnostic and prognostic marker for rheumatoid arthritis.

Zendman, Albert J W / Vossenaar, Erik R / van Venrooij, Walther J

Autoimmunity

2004 Volume 37, Issue 4, Page(s) 295–299

MeSH term(s)	Arthritis, Rheumatoid/diagnosis ; Arthritis, Rheumatoid/immunology ; Autoantibodies/immunology ; Biomarkers ; Citrulline/immunology ; Humans ; Peptides, Cyclic/immunology
Chemical Substances	Autoantibodies ; Biomarkers ; Peptides, Cyclic ; cyclic citrullinated peptide ; Citrulline (29VT07BGDA)
Language	English
Publishing date	2004-09-16
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1025450-x
ISSN	0891-6934
ISSN	0891-6934
DOI	10.1080/08916930410001708733
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Article: Anti-CCP antibodies: the new rheumatoid factor in the serology of rheumatoid arthritis.

van Venrooij, Walther J / Vossenaar, Erik R / Zendman, Albert J W

Autoimmunity reviews

2004 Volume 3 Suppl 1, Page(s) S17–9

MeSH term(s)	Antibodies, Anti-Idiotypic/blood ; Arthritis, Rheumatoid/immunology ; Biomarkers/blood ; Citrulline/immunology ; Clinical Laboratory Techniques ; Humans ; Immunologic Techniques ; Immunologic Tests ; Rheumatoid Factor/blood ; Sensitivity and Specificity ; Serologic Tests ; Serology
Chemical Substances	Antibodies, Anti-Idiotypic ; Biomarkers ; Citrulline (29VT07BGDA) ; Rheumatoid Factor (9009-79-4)
Language	English
Publishing date	2004-06
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2144145-5
ISSN	1568-9972
ISSN	1568-9972
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Article ; Online: Citrullination, a possible functional link between susceptibility genes and rheumatoid arthritis.

Vossenaar, Erik R / Zendman, Albert JW / Van Venrooij, Walther J

Arthritis research & therapy

2004 Volume 6, Issue 1, Page(s) 1–5

Abstract: Antibodies directed to citrullinated proteins (anti-cyclic citrullinated peptide) are highly specific for rheumatoid arthritis (RA). Recent data suggest that the antibodies may be involved in the disease process of RA and that several RA-associated ... ...

Abstract	Antibodies directed to citrullinated proteins (anti-cyclic citrullinated peptide) are highly specific for rheumatoid arthritis (RA). Recent data suggest that the antibodies may be involved in the disease process of RA and that several RA-associated genetic factors might be functionally linked to RA via modulation of the production of anti-cyclic citrullinated peptide antibodies or citrullinated antigens.
Language	English
Publishing date	2004
Publishing country	England
Document type	Editorial
ZDB-ID	2107602-9
ISSN	1478-6362 ; 1478-6354
ISSN (online)	1478-6362
ISSN	1478-6354
DOI	10.1186/ar1027
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Article: Autoantibodies to citrullinated proteins in rheumatoid arthritis: clinical performance and biochemical aspects of an RA-specific marker.

Nijenhuis, Suzanne / Zendman, Albert J W / Vossenaar, Erik R / Pruijn, Ger J M / vanVenrooij, Walther J

Clinica chimica acta; international journal of clinical chemistry

2004 Volume 350, Issue 1-2, Page(s) 17–34

Abstract: Rheumatoid arthritis (RA) is a common, systemic autoimmune disease of which the exact etiology is not known. In the past 10 years, substantial progress has been made in the identification of the antigens specifically recognized by the autoantibodies of ... ...

Abstract	Rheumatoid arthritis (RA) is a common, systemic autoimmune disease of which the exact etiology is not known. In the past 10 years, substantial progress has been made in the identification of the antigens specifically recognized by the autoantibodies of RA patients. A central factor in this respect is citrullination, a form of post-translational modification that is strongly associated with autoimmunity in RA. Here, we summarize and discuss our current knowledge on (i) autoantibody systems in RA, (ii) the occurrence of peptidylarginine deiminases and (iii) citrullinated proteins in natural and diseased environments, and (iv) genetic factors involved in RA that may influence the generation and presentation of citrullinated proteins and the resulting antibody production against these modified proteins. Citrullination of proteins may play a key role in the initiation and/or the progression of RA. The onset of citrulline-specific autoimmunity in RA is probably mediated by both environmental and genetic factors, and future studies will learn whether therapeutic intervention at the level of citrullination may provide new possibilities to treat RA.
MeSH term(s)	Antibody Specificity ; Arthritis, Rheumatoid/blood ; Arthritis, Rheumatoid/immunology ; Autoantibodies/blood ; Biomarkers/blood ; Citrulline/immunology ; Citrulline/metabolism ; Clinical Laboratory Techniques ; Humans ; Hydrolases/metabolism ; Immunologic Techniques ; Protein-Arginine Deiminases
Chemical Substances	Autoantibodies ; Biomarkers ; Citrulline (29VT07BGDA) ; Hydrolases (EC 3.-) ; Protein-Arginine Deiminases (EC 3.5.3.15)
Language	English
Publishing date	2004-12
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80228-1
ISSN	1873-3492 ; 0009-8981
ISSN (online)	1873-3492
ISSN	0009-8981
DOI	10.1016/j.cccn.2004.07.016
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Article ; Online: Correlation of SHOX2 gene amplification and DNA methylation in lung cancer tumors.

Schneider, Katja U / Dietrich, Dimo / Fleischhacker, Michael / Leschber, Gunda / Merk, Johannes / Schäper, Frank / Stapert, Henk R / Vossenaar, Erik R / Weickmann, Sabine / Liebenberg, Volker / Kneip, Christoph / Seegebarth, Anke / Erdogan, Fikret / Rappold, Gudrun / Schmidt, Bernd

BMC cancer

2011 Volume 11, Page(s) 102

Abstract: Background: DNA methylation in the SHOX2 locus was previously used to reliably detect lung cancer in a group of critical controls, including 'cytologically negative' samples with no visible tumor cell content, at a high specificity based on the analysis ...

Abstract	Background: DNA methylation in the SHOX2 locus was previously used to reliably detect lung cancer in a group of critical controls, including 'cytologically negative' samples with no visible tumor cell content, at a high specificity based on the analysis of bronchial lavage samples. This study aimed to investigate, if the methylation correlates with SHOX2 gene expression and/or copy number alterations. An amplification of the SHOX2 gene locus together with the observed tumor-specific hypermethylation might explain the good performance of this marker in bronchial lavage samples. Methods: SHOX2 expression, gene copy number and DNA methylation were determined in lung tumor tissues and matched morphologically normal adjacent tissues (NAT) from 55 lung cancer patients. Quantitative HeavyMethyl (HM) real-time PCR was used to detect SHOX2 DNA methylation levels. SHOX2 expression was assayed with quantitative real-time PCR, and copy numbers alterations were measured with conventional real-time PCR and array CGH. Results: A hypermethylation of the SHOX2 locus in tumor tissue as compared to the matched NAT from the same patient was detected in 96% of tumors from a group of 55 lung cancer patients. This correlated highly significantly with the frequent occurrence of copy number amplification (p < 0.0001), while the expression of the SHOX2 gene showed no difference. Conclusions: Frequent gene amplification correlated with hypermethylation of the SHOX2 gene locus. This concerted effect qualifies SHOX2 DNA methylation as a biomarker for lung cancer diagnosis, especially when sensitive detection is needed, i.e. in bronchial lavage or blood samples.
MeSH term(s)	Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Biomarkers, Tumor/physiology ; Carcinoma/diagnosis ; Carcinoma/genetics ; Carcinoma/metabolism ; Carcinoma/pathology ; Comparative Genomic Hybridization ; DNA Methylation/physiology ; DNA Mutational Analysis/methods ; Gene Amplification/physiology ; Gene Dosage/physiology ; Homeodomain Proteins/genetics ; Homeodomain Proteins/metabolism ; Homeodomain Proteins/physiology ; Humans ; Lung Neoplasms/diagnosis ; Lung Neoplasms/genetics ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Matched-Pair Analysis ; Polymorphism, Genetic ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	Biomarkers, Tumor ; Homeodomain Proteins ; SHOX2 protein, human
Language	English
Publishing date	2011-03-22
Publishing country	England
Document type	Journal Article
ISSN	1471-2407
ISSN (online)	1471-2407
DOI	10.1186/1471-2407-11-102
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Article: PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease.

Vossenaar, Erik R / Zendman, Albert J W / van Venrooij, Walther J / Pruijn, Ger J M

BioEssays : news and reviews in molecular, cellular and developmental biology

2003 Volume 25, Issue 11, Page(s) 1106–1118

Abstract: Peptidylarginine deiminase (PAD, EC 3.5.3.15) enzymes catalyze the conversion of protein-bound arginine to citrulline. This post-translational modification may have a big impact on the structure and function of the target protein. In this review, we will ...

Abstract	Peptidylarginine deiminase (PAD, EC 3.5.3.15) enzymes catalyze the conversion of protein-bound arginine to citrulline. This post-translational modification may have a big impact on the structure and function of the target protein. In this review, we will discuss the effects of citrullination and its involvement in several human diseases, including rheumatoid arthritis and multiple sclerosis. So far, four isotypes of PAD have been described in mammals. We describe the existence of PAD in non-mammalian vertebrates and the existence of a fifth mammalian PAD. In addition, tissue-specific expression, genomic organization and evolutionary conservation of the different PAD isotypes will be discussed in detail. This article contains supplementary material which may be viewed at the BioEssays website at http://www.interscience.wiley.com/jpages/0265-9247/suppmat/2003/25/v25.1106.html.
MeSH term(s)	Amino Acid Sequence ; Animals ; Arthritis, Rheumatoid/enzymology ; Humans ; Hydrolases/classification ; Hydrolases/genetics ; Hydrolases/metabolism ; Isoenzymes/classification ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Molecular Sequence Data ; Multigene Family ; Multiple Sclerosis/enzymology ; Phylogeny ; Protein Conformation ; Protein-Arginine Deiminases ; Psoriasis/enzymology ; Sequence Alignment
Chemical Substances	Isoenzymes ; Hydrolases (EC 3.-) ; Protein-Arginine Deiminases (EC 3.5.3.15)
Language	English
Publishing date	2003-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.10357
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Article: Absence of citrulline-specific autoantibodies in animal models of autoimmunity.

Vossenaar, Erik R / van Boekel, Martinus A M / van Venrooij, Walther J / López-Hoyoz, Marcos / Merino, Jesús / Merino, Ramón / Joosten, Leo A B

Arthritis and rheumatism

2004 Volume 50, Issue 7, Page(s) 2370–2372

MeSH term(s)	Animals ; Antibody Specificity ; Arthritis, Rheumatoid/immunology ; Autoantibodies/analysis ; Autoantibodies/blood ; Autoantibodies/immunology ; Autoimmunity/immunology ; Citrulline/immunology ; Disease Models, Animal ; Humans ; Mice ; Mice, Inbred MRL lpr ; Mice, Transgenic ; Peptides, Cyclic/immunology
Chemical Substances	Autoantibodies ; Peptides, Cyclic ; cf0-cyc peptide ; cyclic citrullinated peptide ; Citrulline (29VT07BGDA)
Language	English
Publishing date	2004-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	127294-9
ISSN	1529-0131 ; 0004-3591 ; 2326-5191
ISSN (online)	1529-0131
ISSN	0004-3591 ; 2326-5191
DOI	10.1002/art.20296
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Article ; Online: Citrullinated proteins have increased immunogenicity and arthritogenicity and their presence in arthritic joints correlates with disease severity.

Lundberg, Karin / Nijenhuis, Suzanne / Vossenaar, Erik R / Palmblad, Karin / van Venrooij, Walter J / Klareskog, Lars / Zendman, A J W / Harris, Helena Erlandsson

Arthritis research & therapy

2005 Volume 7, Issue 3, Page(s) R458–67

Abstract: Autoantibodies directed against citrulline-containing proteins have an impressive specificity of nearly 100% in patients with rheumatoid arthritis and have been suggested to be involved in the disease pathogenesis. The targeted epitopes are generated by ... ...

Abstract	Autoantibodies directed against citrulline-containing proteins have an impressive specificity of nearly 100% in patients with rheumatoid arthritis and have been suggested to be involved in the disease pathogenesis. The targeted epitopes are generated by a post-translational modification catalysed by the calcium-dependent enzyme peptidyl arginine deiminase (PAD), which converts positively charged arginine to polar but uncharged citrulline. The aim of this study was to explore the effects of citrullination on the immunogenicity of autoantigens as well as on potential arthritogenicity. Thus, immune responses to citrullinated rat serum albumin (Cit-RSA) and to unmodified rat serum albumin (RSA) were examined as well as arthritis development induced by immunisation with citrullinated rat collagen type II (Cit-CII) or unmodified CII. In addition, to correlate the presence of citrullinated proteins and the enzyme PAD4 with different stages of arthritis, synovial tissues obtained at different time points from rats with collagen-induced arthritis were examined immunohistochemically. Our results demonstrate that citrullination of the endogenous antigen RSA broke immunological tolerance, as was evident by the generation of antibodies directed against the modified protein and cross-reacting with the native protein. Furthermore we could demonstrate that Cit-CII induced arthritis with higher incidence and earlier onset than did the native counterpart. Finally, this study reveals that clinical signs of arthritis precede the presence of citrullinated proteins and the enzyme PAD4. As disease progressed into a more severe and chronic state, products of citrullination appeared specifically in the joints. Citrullinated proteins were detected mainly in extracellular deposits but could also be found in infiltrating cells and on the cartilage surface. PAD4 was detected in the cytoplasm of infiltrating mononuclear cells, from day 21 after immunisation and onwards. In conclusion, our data reveal the potency of citrullination to break tolerance against the self antigen RSA and to increase the arthritogenic properties of the cartilage antigen CII. We also show that citrullinated proteins and the enzyme PAD4 are not detectable in healthy joints, and that the appearance and amounts in arthritic joints of experimental animals are correlated with the severity of inflammation.
MeSH term(s)	Animals ; Arthritis, Rheumatoid/immunology ; Arthritis, Rheumatoid/pathology ; Citrulline/analysis ; Citrulline/immunology ; Female ; Joints/immunology ; Joints/pathology ; Male ; Rats ; Rats, Inbred Lew ; Severity of Illness Index
Chemical Substances	Citrulline (29VT07BGDA)
Language	English
Publishing date	2005
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2107602-9
ISSN	1478-6362 ; 1478-6354
ISSN (online)	1478-6362
ISSN	1478-6354
DOI	10.1186/ar1697
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Article: The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

Vossenaar, Erik R / Smeets, Tom J M / Kraan, Maarten C / Raats, Jos M / van Venrooij, Walther J / Tak, Paul P

Arthritis and rheumatism

2004 Volume 50, Issue 11, Page(s) 3485–3494

Abstract: Objective: Antibodies directed toward citrullinated proteins (e.g., anti-cyclic citrullinated peptide antibodies) are highly specific for rheumatoid arthritis (RA) and are produced locally at the site of inflammation. Although the presence of ... ...

Abstract	Objective: Antibodies directed toward citrullinated proteins (e.g., anti-cyclic citrullinated peptide antibodies) are highly specific for rheumatoid arthritis (RA) and are produced locally at the site of inflammation. Although the presence of citrullinated proteins in rheumatoid synovium has been described in the literature, it is uncertain whether their presence is specific for RA. The present study was undertaken to investigate this. Methods: The local production of the anti-citrullinated protein antibodies was investigated by comparing the concentration of the antibodies (corrected for the total amount of IgG present) in paired samples of serum and synovial fluid from RA patients. The presence of citrullinated proteins in the synovial tissue was investigated by immunohistochemical analysis of synovial tissue from RA patients and from patients with other arthropathies, using a variety of specific antibodies to citrullinated proteins. Results: In RA patients, anti-citrullinated protein antibodies constituted a 1.4-fold higher proportion of IgG in synovial fluid compared with serum, which is indicative of a local production of the antibodies. Immunohistochemical staining of citrullinated proteins was observed in the lining layer, the sublining layer, and in extravascular fibrin deposits in inflamed synovial tissue from RA as well as non-RA patients. Conclusion: The presence of citrullinated proteins in the inflamed synovium is not specific for RA, but rather, it may be an inflammation-associated phenomenon. The high specificity of the anti-citrullinated protein antibodies is, therefore, most likely the result of an abnormal humoral response to these proteins.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Antibodies/blood ; Antibodies/metabolism ; Arthritis, Rheumatoid/blood ; Arthritis, Rheumatoid/immunology ; Arthritis, Rheumatoid/metabolism ; Case-Control Studies ; Citrulline/immunology ; Citrulline/metabolism ; Female ; Humans ; Immunoglobulins/metabolism ; Immunohistochemistry/methods ; Joint Diseases/blood ; Joint Diseases/metabolism ; Male ; Middle Aged ; Peptides, Cyclic/blood ; Peptides, Cyclic/immunology ; Peptides, Cyclic/metabolism ; Staining and Labeling ; Synovial Membrane/immunology ; Synovial Membrane/metabolism
Chemical Substances	Antibodies ; Immunoglobulins ; Peptides, Cyclic ; cyclic citrullinated peptide ; Citrulline (29VT07BGDA)
Language	English
Publishing date	2004-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	127294-9
ISSN	1529-0131 ; 0004-3591 ; 2326-5191
ISSN (online)	1529-0131
ISSN	0004-3591 ; 2326-5191
DOI	10.1002/art.20584
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