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Expression and distribution of UV-DDB in the nerve cells and tissues

Expression and distribution of UV-DDB in the nerve cells and tissues
UV-DDB在神经细胞和组织中的表达和分布
批准号:
11670209
负责人:
NAKANISHI Isao
金额:
$2.11万
依托单位:
依托单位国家:
日本
项目类别:
Grant-in-Aid for Scientific Research (C)
财政年份:
1999
资助国家:
日本
项目状态:
已结题
起止时间:
1999 至 2000

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中文摘要
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英文摘要
UV-damaged-DNA binding protein (UV-DDB) is an intracytoplasmic protein of heterodimer consisting of 127 kDa and 48 kDa, the former of which binds with the cytoplasmic domain of amyloid β protein precursor (APP). In this research project, we immunohistochemically investigated the expression and distribution of UV-DDB in the normal and diseased brains (3 Alzheimer's disease cases, 2 non-dementia autopsy cases) by using the specific polyclonal antibodies (Watanabe T.at al., J.Neurochem. 72, 2, 549-556, 1999). Specific antibodies against β-amyloid protein (βA), choline acetyltransferatse (ChAT), tau, ubiquitin were also applied on the paraformaldehyde-fixed paraffin section of those cases. Expression of each protein was noted on normal nerve cells, degenerating nerve cells, neurofibrillary tangles, and senile plaques in the frontal lobes, cerebral basilar nuclei and hypocampus. ChAT immunohistochemistry was negative in Alzheimer's deisease brain. βA and ubiquitin immunoreactivities were positive in the senile plaques. Particularly the degenerating nerve cells and their processes were immunoreactive with ubiquitin, suggesting the increase of proteosome enzymatic actibity. UV-DDB immunoreactivity was negative in the control brains, but Alzheimer's diseased brains were weakly positive for UV-DDB in degenerating nerve cells, particularly in areas of the diffuse type senile plaques and neurofibrillary tangles in the frontal lobes and hypocampus. Thus, UV-DDB which binds to AP sites of the protein during DNA damage may be expressed in the nuclei of particular degenerating nerve cells for reparative processes
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会议论文
Isohara T, et al : "Phosphorylation of the cytoplasmic domain of Alzheimer's β-amyloid precursor protein at Ser 655 by a novel protein kinase."Biochem.Biophys.Res.Comm.. 258・2. 300-305 (1999)
Isohara T 等人:“通过新型蛋白激酶对阿尔茨海默病 β-淀粉样前体蛋白的胞质结构域在 Ser 655 进行磷酸化。”Biochem.Biophys.Res.Comm. 258·2 (1999)。
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Muroishi,Y. et al : "Immunohistochemical and in situ hybridization studies neurons of choline acetyltransferase in large motor neurons of the human spinal cord."Histol.Histopathol.. 15・3. 689-696 (2000)
Muroishi, Y. 等人:“免疫组织化学和原位杂交研究人类脊髓大运动神经元中的胆碱乙酰转移酶神经元。” 15・3 (2000)。
DOI: --
发表时间:
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作者: []
通讯作者:
Isohara T, et al.: "Phosphorylation of the cytoplasmic domain of Alzheimer's β-amyloid precursor protein at Ser 655 by a novel protein kinase."Biochem.Biophys.Res.Comm.. 258(2). 300-305 (1999)
Isohara T 等人:“通过新型蛋白激酶对阿尔茨海默病 β-淀粉样前体蛋白的胞质结构域在 Ser 655 处进行磷酸化。”Biochem.Biophys.Res.Comm. 258(2) (1999)。
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通讯作者:
Oda,Y.: "Choline acetyltransferase : the structure, distribution and pathologic changes in the central nervous system."Pathol.Int.. 49・11. 921-937 (1999)
Oda, Y.:“胆碱乙酰转移酶:中枢神经系统的结构、分布和病理变化。Pathol.Int.. 921-937 (1999)”
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