Evidence map›Paper›PMID 22906101›Full record

ArticleArthritis research & therapy2012

Cartilage oligomeric matrix protein specific antibodies are pathogenic.

Hui Geng, Kutty Selva Nandakumar, Anna Pramhed, Anders Aspberg, Ragnar Mattsson, Rikard Holmdahl

Abstract read
In one paragraph

Article in Arthritis research & therapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Trial
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  7. Article
  8. Article
  9. Review
  10. Targeting IgG in Arthritis: Disease Pathways and Therapeutic Avenues.International journal of molecular sciences · 2018
    Review
  11. Article
  12. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Hui Geng
Kutty Selva Nandakumar
Anna Pramhed
Anders Aspberg
Ragnar Mattsson
Rikard Holmdahl

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionCartilage oligomeric matrix protein (COMP) is a major non-collagenous component of cartilage. Earlier, we developed a new mouse model for rheumatoid arthritis using COMP. This study was undertaken to investigate the epitope specificity and immunopathogenicity of COMP-specific monoclonal antibodies (mAbs).

methodsB cell immunodominant regions on the COMP molecule were measured with a novel enzyme-linked immunosorbent assay using mammalian expressed full-length mouse COMP as well as a panel of recombinant mouse COMP fragments. 18 mAbs specific to COMP were generated and the pathogenicity of mAbs was investigated by passive transfer experiments.

resultsB cell immunodominant epitopes were localized within 4 antigenic domains of the COMP but with preferential response to the epidermal growth factor (EGF)-like domain. Some of our anti-COMP mAbs showed interactions with the native form of COMP, which is present in cartilage and synovium. Passive transfer of COMP-specific mAbs enhanced arthritis when co-administrated with a sub-arthritogenic dose of a mAb specific to collagen type II. Interestingly, we found that a combination of 5 COMP mAbs was capable of inducing arthritis in naive mice.

conclusionsWe have identified the specificities of mAbs to COMP and their contribution to the development of arthritis. These findings will further improve our understanding of the autoantibody mediated immunopathologies occurring widely in rheumatoid arthritis (RA), as well as in other autoimmune disorders.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalArthritis, ExperimentalCartilageCartilage Oligomeric Matrix ProteinMiceMice, 129 StrainMice, KnockoutMolecular Sequence DataAntibodies, MonoclonalCartilage Oligomeric Matrix Protein

Identifiers

PMID22906101
PMCPMC3580587

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.