Anti-CCP antibody test predicts the disease course during 3 years in early rheumatoid arthritis (the Swedish TIRA project)

Kastbom, Alf; Strandberg, Gunnar; Lindroos, Annette; Skogh, Thomas

doi:10.1136/ard.2003.016808

Cited by 323 publications

(268 citation statements)

References 33 publications

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“…Because of these features suggesting that ACPAs represent a factor influencing the severity of RA, combined with the observation that ACPAs display a high specificity (13) and are predictive of the development of RA (14,15), it has been hypothesized that ACPAs are relevant to the pathophysiology of RA. This hypothesis remains unproven, because these features could also be a result of a bystander effect.…”

Section: Autoantibodiesmentioning

confidence: 99%

Emerging patterns of risk factor make‐up enable subclassification of rheumatoid arthritis

Mil¹,

Huizinga²,

Vries³

et al. 2007

Arthritis & Rheumatism

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Section: Autoantibodiesmentioning

confidence: 99%

Emerging patterns of risk factor make‐up enable subclassification of rheumatoid arthritis

Mil¹,

Huizinga²,

Vries³

et al. 2007

Arthritis & Rheumatism

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“…Kuhn et al, for example, recently demonstrated that administration of anti-citrullinated fibrinogen antibodies enhanced disease severity in an experimental mouse model of arthritis (4). In the majority of patients with RA, the presence of ACPAs antedates disease onset (5,6), and ACPA-positive patients present with a more severe and erosive form of arthritis (7)(8)(9)(10)(11)(12)(13)(14)(15)(16). A commercial enzyme-linked immunosorbent assay (ELISA) based on cyclic citrullinated peptides (CCPs) detects ACPAs and is now routinely used in the diagnosis of RA.…”

mentioning

confidence: 99%

Antibodies to citrullinated α‐enolase peptide 1 are specific for rheumatoid arthritis and cross‐react with bacterial enolase

Lundberg

Kinloch

Fisher

et al. 2008

Arthritis & Rheumatism

338

312

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Objective. To map the antibody response to human citrullinated ␣-enolase, a candidate autoantigen in rheumatoid arthritis (RA), and to examine crossreactivity with bacterial enolase.Methods. Serum samples obtained from patients with RA, disease control subjects, and healthy control subjects were tested by enzyme-linked immunosorbent assay (ELISA) for reactivity with citrullinated ␣-enolase peptides. Antibodies specific for the immunodominant epitope were raised in rabbits or were purified from RA sera. Cross-reactivity with other citrullinated epitopes was investigated by inhibition ELISAs, and cross-reactivity with bacterial enolase was investigated by immunoblotting.Results. An immunodominant peptide, citrullinated ␣-enolase peptide 1, was identified. Antibodies to this epitope were observed in 37-62% of sera obtained from patients with RA, 3% of sera obtained from disease control subjects, and 2% of sera obtained from healthy control subjects. Binding was inhibited with homologous peptide but not with the arginine-containing control peptide or with 4 citrullinated peptides from elsewhere on the molecule, indicating that antibody binding was dependent on both citrulline and flanking amino acids. The immunodominant peptide showed 82% homology with enolase from Porphyromonas gingivalis, and the levels of antibodies to citrullinated ␣-enolase peptide 1 correlated with the levels of antibodies to the bacterial peptide (r 2 ‫؍‬ 0.803, P < 0.0001). Affinitypurified antibodies to the human peptide cross-reacted with citrullinated recombinant P gingivalis enolase.Conclusion. We have identified an immunodominant epitope in citrullinated ␣-enolase, to which antibodies are specific for RA. Our data on sequence similarity and cross-reactivity with bacterial enolase may indicate a role for bacterial infection, particularly with P gingivalis, in priming autoimmunity in a subset of patients with RA.

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“…Autoantibodies directed against citrulline, an amino acid that results from post-translational modification of arginine in inflamed synovial membranes, have been shown to have a high specificity of 93-98% in early RA [3]. These antibodies to cyclic-citrullinated peptide (aCCP) are also of prognostic value in predicting disease severity, erosive damage and response to therapy [4,5].…”

mentioning

confidence: 99%

The diagnostic utility of the anti-CCP antibody test is no better than rheumatoid factor in South Africans with early rheumatoid arthritis

et al. 2010

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To establish the diagnostic utility of the anticyclic-citrullinated peptide antibody (aCCP) test in Black South Africans with early rheumatoid arthritis (RA). A cross-sectional study comparing the rheumatoid factor (RF) and aCCP status in RA patients and a control group consisting of healthy subjects, and patients with systemic lupus erythematosus (SLE) and scleroderma. The sensitivity, specificity, positive (PPV) and negative predictive values of the aCCP test alone were 82.5%, 84.9%, 87.6% and 79% versus 81.7%, 90.7%, 92.5% and 78% for RF alone. The best specificity (95.3) and PPV (95.8%) was observed when both aCCP and RF tests were positive. Patients with erosive disease had a significantly higher mean RF titre compared with those with non-erosive disease (p=0.007). There was a trend towards an association of smoking (OR=4.1, 95% CI=0.9-18.6) and functional disability (p=0.07) with RF-positive status. No similar clinical associations were observed with aCCP. Almost a third of SLE patients were aCCP positive. Despite the best specificity and PPV observed when both the aCCP and RF tests were positive, our findings suggest that testing for aCCP is only cost-effective in the RF-negative patient in whom there is a strong clinical suspicion of RA.

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Anti-CCP antibody test predicts the disease course during 3 years in early rheumatoid arthritis (the Swedish TIRA project)

Cited by 323 publications

References 33 publications

Emerging patterns of risk factor make‐up enable subclassification of rheumatoid arthritis

Emerging patterns of risk factor make‐up enable subclassification of rheumatoid arthritis

Antibodies to citrullinated α‐enolase peptide 1 are specific for rheumatoid arthritis and cross‐react with bacterial enolase

The diagnostic utility of the anti-CCP antibody test is no better than rheumatoid factor in South Africans with early rheumatoid arthritis

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