SCREENING OF SALIVARY GLAND PROTEASE WHICH SPECIFICALLY CLEAVAGES SJOGREEN'S SYNDROME RELATED AUTOANTIGEN a-PODRIN FRAGMENT
| Project/Area Number |
13670218
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Experimental pathology
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| Research Institution | The University of Tokushima |
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Principal Investigator |
ARAKAKI Rieko The University of Tokushima DENT.RES.ASSOCIATE, 歯学部, 助手 (40231120)
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| Co-Investigator(Kenkyū-buntansha) |
HAYASHI Yoshio The University of Tokushima DENT.PROF, 歯学部, 教授 (00127854)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2002: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2001: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Keywords | Sjogren's syndrome / a-fodrin / autommune diseases / salivary gland / apoptosis / caspase / α-fodrin / ELISA / caspase / 自己抗原 |
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| Research Abstract |
Sjogren's syndorome (SS) is autoimmune disorder characterized by lymphocytic infiltrates and destructed of the salivary and lacrimal glands, and systemic producion of autoantibodies. We established an animal model of primary SS in NFS/sld mutant mice thymectomyzed 3 days after birth. Recently,we identified the 120-Kd amino-terminal a-fodrin molecule as an important organ-specific autoantigen in the NFS/sld mouse model of Sjogren's syndrome (Science 1997, 276;604-607, Haneji N et al). Fodrin are known to be the central components of the membranc akeleton, play a role in the shape and stability of membranes, the molecular weight of a-fodrin are cleavaged to some fragments with apoptosis in various cells. We also showed that sera from SS patients as well as those from SS model mice specifically recognize the 120-Kd amino-terminal fragment of a-fodrin. By western blot analysis and ELISA, the almost positive sera for a-fodrin fragments in SS patient's sera react with the amino-terminal fragments but not with carboxyl-terminal fragments. To raise the Abs reco gnized amino-terminal a-fodrin, recombinant a-fodrin His_6 fusion protein encoded a-Fodrin_<37-500> AFN-A, were used to immunize rabbit, anti-AFN-A Abs recognized 155,130 Kd a-fodrin fragments different from carboxyl-terminal 150, 120 Kd fragments in apoptosis induced salivary gland cell. We tried to purify the 130 Kd N-terminal that is auto antigen of SS with affinity chromatography by anti-AFNA-A, measure the carboxyl-terminal amino acids (aa) sequence. The information aa of 130 Kd N-terminal a-fodrin fragment. Moreover, the investigation of the SS specific protease in salivary gland have important implocations for testing useful therapies.
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Report
(3 results)
Research Products
(9 results)
