Abstract | OBJECTIVE: METHODS: A series of truncated peptides of human CENP-C were expressed in Escherichia coli and immunoblotting analysis was performed with 45 ACA positive sera obtained from patients with different types of autoimmune diseases. RESULTS: Although 9 epitopes were scattered over the entire molecule, the N terminus was immunodominant for IgG and IgM classes and the C terminus was dominant for IgG class. Both epitopes were separately located within the instability and centromere targeting domains in vivo, or the oligomerization-accessible and homodimerization domains in vitro, respectively. In contrast, minor epitopes were clustered at the internal DNA binding domain. A number of patterns of immunoreactivities against 3 representative antigenic sites by IgG or IgM class antibodies were found. CONCLUSION: The results indicated the existence of different anti- CENP-C responses in rheumatic diseases and a possible correlation between antigenic regions and functional sites in the CENP-C antigen.
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Authors | K Sugimoto, K Kuriyama, M Himeno, Y Muro |
Journal | The Journal of rheumatology
(J Rheumatol)
Vol. 25
Issue 3
Pg. 474-81
(Mar 1998)
ISSN: 0315-162X [Print] Canada |
PMID | 9517766
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Autoantigens
- Chromosomal Proteins, Non-Histone
- Histocompatibility Antigens Class II
- Immunoglobulin G
- Immunoglobulin M
- centromere protein C
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Topics |
- Autoantigens
(immunology)
- Centromere
(immunology)
- Chromosomal Proteins, Non-Histone
(immunology, metabolism)
- Epitope Mapping
- Histocompatibility Antigens Class II
(immunology)
- Humans
- Immunoglobulin G
(immunology)
- Immunoglobulin M
(immunology)
- Longitudinal Studies
- Protein Conformation
- Rheumatic Diseases
(immunology, metabolism)
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