Surface Calreticulin Triggers Innate Immune Signaling via Cell The Rheumatoid Arthritis Shared Epitope
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منابع مشابه
Identification of the Rheumatoid Arthritis Shared Epitope Binding Site on Calreticulin
BACKGROUND The rheumatoid arthritis (RA) shared epitope (SE), a major risk factor for severe disease, is a five amino acid motif in the third allelic hypervariable region of the HLA-DRbeta chain. The molecular mechanisms by which the SE affects susceptibility to--and severity of--RA are unknown. We have recently demonstrated that the SE acts as a ligand that interacts with cell surface calretic...
متن کاملNew insights into the functional role of the rheumatoid arthritis shared epitope.
The shared epitope (SE) - an HLA-DRB1-encoded 5-amino acid sequence motif carried by the vast majority of rheumatoid arthritis (RA) patients - is a risk factor for severe disease. The mechanistic basis of RA-SE association is unknown. This group has previously demonstrated that the SE acts as a signal transduction ligand that activates nitric oxide and reactive oxygen species production. SE-act...
متن کاملCitrullinated calreticulin potentiates rheumatoid arthritis shared epitope signaling.
OBJECTIVE Citrullinated proteins are immunogenic in rheumatoid arthritis (RA), particularly in patients who carry shared epitope (SE)-coding HLA-DRB1 alleles. The mechanism underlying this association is unknown. We have previously identified the SE as a ligand that interacts with cell surface calreticulin (CRT) and activates immune dysregulation. This study was undertaken to determine the effe...
متن کاملNitric oxide signaling triggered by the rheumatoid arthritis shared epitope: a new paradigm for MHC disease association?
Many immune-mediated diseases are associated with particular MHC class I or class II alleles. In rheumatoid arthritis (RA-shared), the vast majority of patients possess HLA-DRB1 alleles encoding a shared epitope, which is a five-amino acid sequence motif in positions 70-74 of the HLA-DRbeta chain. The mechanistic basis for this association is unknown. Here we discuss recent evidence suggesting ...
متن کاملA role for calreticulin in the pathogenesis of rheumatoid arthritis.
Calreticulin (CRT) plays a role in the clearance of dying cells and has been implicated in autoimmunity. Recent evidence indicates that cell surface CRT (csCRT) acts as a signal transducing receptor for the rheumatoid arthritis (RA) shared epitope (SE). The SE binding site on CRT has been mapped to amino acid residues 217-223 in the P-domain. Upon interaction with dendritic cells (DCs), the SE ...
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تاریخ انتشار 2007