TY - JOUR
T1 - Profile of the regions on the α-chain of human acetylcholine receptor recognized by autoantibodies in myasthenia gravis
AU - Ashizawa, Tetsuo
AU - Ruan, Ke He
AU - Jinnai, Kenji
AU - Atassi, M. Zouhair
N1 - Funding Information:
*This work was supported in part by the Texas Advanced Research Program (Advanced Technology program) under grant number 117, Veterans Administration Merit Review and by the National Institutes of Health (grant number NS26280). The support of the Welch Foundation due to the award to MZA of the Robert A. Welch Chair of Chemistry is also gratefully acknowledged. We wish to thank Drs B. Mulac-Jericevic and T. Yokoi and Mr T. Manshouri for the synthesis of the peptides of human AChR a-chain. $Author to whom correspondence should be addressed: Dr M. Z. Atassi, Department of Biochemistry, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, U.S.A.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1992/12
Y1 - 1992/12
N2 - Eighteen synthetic overlapping peptides encompassing the entire extracellular part (residues α 1-210) of the α-chain of human acetylcholine receptor (AChR) and a 19th peptide (residues α 262-276) corresponding to an extracellular connection between two transmembrane regions were prepared and used for the measurement, by solid-phase radioimmunoassay, of the binding of autoantibodies in plasma from myasthenia gravis (MG) patients. Autoantibodies were found to recognize only a limited number of the synthetic peptides. The regions recognized resided predominantly within the areas α 10-30, α 111-145 and α 175-198 and, less frequently, region α 45-77. Differences in the recognition profile of the peptides from patient to patient indicated that the autoantibody responses were under genetic control. However, by using a mixture of the appropriate peptides, it was possible to determine autoantibodies in all 15 myasthenia sera and to distinguish between these, normal human sera and other neurological or autoimmune diseases. The mapping of the continuous antigenic regions recognized by autoantibodies on the α-chain of human AChR has permitted a comparison of the regions recognized by autoantibodies and autoimmune T-cells from the same donor. It also provided a peptide-based direct antibody binding method for diagnosis of MG.
AB - Eighteen synthetic overlapping peptides encompassing the entire extracellular part (residues α 1-210) of the α-chain of human acetylcholine receptor (AChR) and a 19th peptide (residues α 262-276) corresponding to an extracellular connection between two transmembrane regions were prepared and used for the measurement, by solid-phase radioimmunoassay, of the binding of autoantibodies in plasma from myasthenia gravis (MG) patients. Autoantibodies were found to recognize only a limited number of the synthetic peptides. The regions recognized resided predominantly within the areas α 10-30, α 111-145 and α 175-198 and, less frequently, region α 45-77. Differences in the recognition profile of the peptides from patient to patient indicated that the autoantibody responses were under genetic control. However, by using a mixture of the appropriate peptides, it was possible to determine autoantibodies in all 15 myasthenia sera and to distinguish between these, normal human sera and other neurological or autoimmune diseases. The mapping of the continuous antigenic regions recognized by autoantibodies on the α-chain of human AChR has permitted a comparison of the regions recognized by autoantibodies and autoimmune T-cells from the same donor. It also provided a peptide-based direct antibody binding method for diagnosis of MG.
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U2 - 10.1016/0161-5890(92)90225-M
DO - 10.1016/0161-5890(92)90225-M
M3 - Article
C2 - 1280762
AN - SCOPUS:0026463423
VL - 29
SP - 1507
EP - 1514
JO - Molecular Immunology
JF - Molecular Immunology
SN - 0161-5890
IS - 12
ER -