EpitopeAnalysisofCytokeratin 18Protein binding withAutoantibodiesin SeraofPatientswith NonallergicAsthma.

PURPOSE: Recently autoantibodies to bronchial epithelial proteins were detected in sera of patients with nonallergic asthma and cytokeratin 18 (CK18) protein was identified as an autoantigen associated with nonallergic asthma. In this study, epitope of CK18 protein binding with autoantibodies in sera of patients with nonallergic asthma was analyzed. METHODS: We used sera of 3 patients with nonallergic asthma who had autoantibodies against CK18 protein. We cleaved human recombinant CK18 with caspase-3 and caspase-6 which are involved in apoptosis process. To evaluate the fragment of CK18 binding with autoantibodies of sera from patients with nonallergic asthma, immunoblot was done. RESULTS: When the CK18 protein was treated by caspase-3, C-terminal fragment (398-430 amino acid) of CK18 was removed. The autoantibodies bound to remained N-terminal fragment (1-397 amino acid) of CK18 moderately in one patient but very weakly in the other two patients compared to whole CK18 protein. When the CK18 protein was treated by caspase-6, it was cleaved into two fragments (N-terminal fragment: 1-238 amino acid, C-terminal fragment: 239-430 amino acid). The autoantibodies in one patient weakly bound to N-terminal fragment of CK18 only and autoantibodies in other two patients did not bound to both fragments. CONCLUSIONS: Autoantibodies of nonallergic asthma bound with whole molecule of CK18 protein, not with fragments of CK18 cleaved by caspase-3 or caspase-6. Antigenic determinants of CK18 protein to autoantibodies in sera of patients with non-allergic asthma seemed to be distributed in the whole molecule of CK18 protein.

Author dc:creator

• 김, 정은

Contributors dc:contributor

• 남, 동호
• 대학원 의학과
• 104299

• 비알레르기성 천식
• Cytokeratin18
• caspase
• nonallergicasthma

Language dc:language

ko

Identifier

http://dcoll.ajou.ac.kr:9080/dcollection/jsp/common/DcLoOrgPer.jsp?sItemId=000000000676
000000000676

OAI identifier oai:identifier

oai:repository.ajou.ac.kr:201003/1500