An evaluation of anti-VacA antibody and its target molecules in the cerebrospinal fluid of patients with demyelinating form of Guillain-Barre syndrome.
| Project/Area Number |
15500242
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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 |
Nerve anatomy/Neuropathology
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| Research Institution | Sapporo Medical University |
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Principal Investigator |
CHIBA Susumu Sapporo Medical University, Department of Neurology, School of Medicine, Associate Professor, 医学部, 助教授 (30167514)
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| Co-Investigator(Kenkyū-buntansha) |
SUGIYAMA Toshiroh Toyama University, The 3rd Department of Internal Medicine, School of Medicine, Professor, 医学部, 教授 (00196768)
IMAI Tomihiro Sapporo Medical University, Department of Neurology, School of Medicine, Assistant Professor, 医学部, 講師 (40231162)
NONAKA Michio Sapporo Medical University, Department of Neurology, School of Medicine, Instructor, 医学部, 助手 (50363685)
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| Project Period (FY) |
2003 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2005: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2004: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2003: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Helicobacter pylori / anti-VacA antibody / cerebrospinal fluid / Guillain-Barre syndrome / molecular homology / 分子相同性 / 髄液抗HSP抗体 / 自然免疫応答 / 免疫組織化学 / 末梢神経・神経根 / Na^+-K^+ ATPaseαsubunit / ミエリンPO蛋白 |
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| Research Abstract |
Immunological study
In order to detect antibodies against recombinant vacuolating cytotoxin (r-VacA) of Helicobacter pylori (H.pylori) in the cerebrospinal fluid (CSF) from patients with Guillain-Barre syndrome (GBS). The CSF samples from 13 patients with GBS (electrophysiologically classified as 8 acute inflammatory demyelinating polyradiculoneuropathy (AIDP), 4 acute motor axonal neuropathy (AMAN), and 1 unexcitable) and 8 disease control patients were studied. The r-VacA protein was separated by SDS-PAGE and Western blot analysis was carried out. Six of the 13 GBS patients had a specific IgG antibody against VacA of H.pylori, which was confirmed by absorption experiments using r-VacA. Every patient with positive CSF anti-r-VacA antibody had AIDP. The sequence homology between VacA and human (Na^++K^+)-ATPase α subunit has been outlined. Our findings lead to the possible hypothesis that anti-VacA antibodies involve ion channels in abaxonal Schwann cell plasmalemma resulting in demyeli
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nation in some patients with GBS.
Histochemical evaluation
To identify the target molecules of anti-VacA-antibody (A-VacA-Ab) in the human ventral nerve roots, the immunohistochemical examination was carried out. A-VacA-Ab obtained from rabbits was prepared by immunization of the native VacA purified by the culture media of H.pylori. Cervical ventral nerve roots were obtained from patients with no known neurologic disorders within two hours after death. Both DAB and FITC procedures were employed. Disseminated spotty stainings were observed in cross sections. In longitudinal sections, string-like immunostainings were also seen both by DAB and FITC procedures. These were localized within the nerve fibers. Consequently, the target epitopes of A-VacA-Ab were thought to be present in the myelin components of the nerve roots. These results indicate that the target molecules of A-VacA-Ab in the cerebrospinal fluid obtained from patients with GBS are probably associated with some components of the peripheral nerve myelin. A-VacA-Ab may play an important role in the immune responses of patients with the demyelinating form of GBS. Less
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Report
(4 results)
Research Products
(18 results)
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[Journal Article] Localization and function in ER stress tolelance of Erdj3, a new member of HSP4O family protein.2004
Author(s)
Nakanishi K, Kamiguchi K, Torigoe T, Nabeta C, Hirohashi Y, Asanuma H, Tobioka H, Koge N, Harad IO, Ichimiya S, Noagno H, Yano S, Chiba S, Matsumoto H, Sato N.
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Journal Title
Cell stress and Chaperone 9
Pages: 253-264
Description
「研究成果報告書概要(和文)」より
Related Report
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[Journal Article] Localization and function in ER stress tolelance of Erdj3, a new member of HSP40 family protein.2004
Author(s)
Nakanishi K, Kamiguchi K, Torigoe T, Nabeta C, Hirohashi Y, Asanuma H, Tobioka H, Koge N, Harad IO, Ichimiya S, Noagno H, Yano S, Chiba S, Matsumoto H, Sato N.
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Journal Title
Cell stress and Chaperone 9
Pages: 253-264
Related Report
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