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Beyond citrullination: other post-translational protein modifications in rheumatoid arthritis
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Beyond citrullination: other post-translational protein modifications in rheumatoid arthritis
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Journal Article
Beyond citrullination: other post-translational protein modifications in rheumatoid arthritis
2017
Overview
Key Points
As well as citrullination, several other post-translational protein modifications are targeted by autoantibodies in rheumatoid arthritis (RA)
Anti-hinge antibodies might restore the lost capacity to trigger Fc effector functions of IgG cleaved in the hinge region by proteases expressed in the synovial compartment
Anti-modified protein antibodies (AMPAs) are mainly found in anti-citrullinated protein antibody (ACPA)-positive patients
Anti-carbamylated protein (anti-CarP) antibodies and ACPAs are only partially crossreactive despite recognizing two rather similar modifications
T cell help for AMPA-producing B cells does not have to target the post-translationally modified protein owing to the crossreactive nature of AMPAs
Post-translationally modified matrix proteins could be relevant targets for AMPAs in RA because these immobile proteins are difficult to clear and hence are exposed in a durable manner
Several different autoantibody systems recognizing post-translationally modified proteins have been identified in rheumatoid arthritis, beyond the well-known rheumatoid factors and anti-citrullinated protein antibodies. This Review summarizes what is known about the presence and properties of these emerging autoantibodies, in particular those recognizing carbamylated proteins.
The presence of autoantibodies is one of the hallmarks of rheumatoid arthritis (RA). In the past few decades, rheumatoid factors (autoantibodies that recognize the Fc-tail of immunoglobulins) as well as anti-citrullinated protein antibodies (ACPAs) have been studied intensively. ACPAs recognize post-translationally modified proteins in which the amino acid arginine has been converted into a citrulline. More recently, other autoantibody systems recognizing post-translationally modified proteins have also gained attention, including autoantibodies recognizing fragmented immunoglobulin (anti-hinge antibodies), autoantibodies recognizing acetylated proteins and autoantibodies recognizing proteins that are modified by adducts formed under oxidative stress. In particular, detailed insights have been obtained on the presence and properties of autoantibodies recognizing carbamylated proteins, commonly called anti-carbamylated protein (anti-CarP) antibodies. In this Review, we summarize the current knowledge relating to these emerging autoantibodies that recognize post-translationally modified proteins identified in RA, with an emphasis on anti-CarP antibodies.
Publisher
Nature Publishing Group UK,Nature Publishing Group
