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Human α-enolase from endothelial cells as a target antigen of anti–endothelial cell antibody in Behçet's disease

Authors
 Kwang Hoon Lee  ;  Hae-Shin Chung  ;  Dongsik Bang  ;  Sungnack Lee  ;  Ja-Hyun Baik  ;  Moon-Kyung Ha  ;  Sang-Ho Oh  ;  Hyoung Sup Kim 
Citation
 Arthritis & Rheumatism, Vol.48(7) : 2025-2035, 2003 
Journal Title
 Arthritis & Rheumatism 
ISSN
 0004-3591 
Issue Date
2003
MeSH
Autoantibodies/blood* ; Autoantigens/genetics ; Autoantigens/immunology* ; Behcet Syndrome/immunology* ; Blotting, Western ; Cells, Cultured ; Cloning, Molecular ; Epitopes ; Humans ; Immunoglobulin M/blood ; Phosphopyruvate Hydratase/genetics ; Phosphopyruvate Hydratase/immunology* ; Proteomics ; Recombinant Proteins/immunology ; Skin/cytology
Keywords
12847697
Abstract
OBJECTIVE: To identify and recombine a protein of the human dermal microvascular endothelial cell (HDMEC) that specifically reacts with anti-endothelial cell antibody (AECA) in the serum of patients with Behçet's disease (BD), and to evaluate the usefulness of this protein in BD. METHODS: The proteomics technique, with 2-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry, was used to identify and recombine HDMEC antigen. Western blotting and enzyme-linked immunosorbent assay (ELISA) of recombinant protein isolated by gene cloning were performed on serum from healthy controls, patients with BD, and patients with other rheumatic diseases (rheumatoid arthritis, systemic lupus erythematosus, and Wegener's granulomatosis). RESULTS: Eighteen of 40 BD patients had serum IgM antibody to HDMEC antigen. The purified protein that reacted with AECA in BD patient sera was found to be alpha-enolase by 2-dimensional gel electrophoresis followed by immunoblotting and MALDI-TOF mass spectrometry. Recombinant alpha-enolase protein was isolated and refined by gene cloning. On Western blots, AECA-positive IgM from the sera of patients with active BD reacted strongly with recombinant human alpha-enolase. BD patient sera positive for anti-alpha-enolase did not react with human gamma-enolase. On dot-blotting, reactivity to human alpha-enolase was detected only in the IgM-positive group. Fifteen of the 18 AECA-positive sera that were positive for the HDMEC antigen showed reactivity to recombinant alpha-enolase IgM antibody by ELISA. CONCLUSION: The alpha-enolase protein is the target protein of serum AECA in BD patients. This is the first report of the presence of IgM antibodies to alpha-enolase in endothelial cells from the serum of BD patients. Although further studies relating this protein to the pathogenesis of BD will be necessary, alpha-enolase and its antibody may prove useful in the development of new diagnostic and treatment modalities in BD.
Files in This Item:
T200303110.pdf Download
DOI
10.1002/art.11074
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Dermatology (피부과학교실) > 1. Journal Papers
Yonsei Authors
Bang, Dong Sik(방동식)
Lee, Kwang Hoon(이광훈)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/113473
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