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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Expression of human β-amyloid peptide in transgenic Caenorhabditis elegans
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Expression of human β-amyloid peptide in transgenic Caenorhabditis elegans

机译：人β淀粉样肽在转基因秀丽隐杆线虫中的表达

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摘要

Transgenic Caenorhabditis elegans nematodes have been engineered to express potentially amyloidic human proteins. These animals contain constructs in which the muscle-specific unc-54 promoter/enhancer of C. elegans drives the expression of the appropriate coding regions derived from human cDNA clones. Animals containing constructs expressing the 42-amino acid β-amyloid peptide (derived from human amyloid precursor protein cDNA) produce muscle-specific deposits immunoreactive with anti-β-amyloid polyclonal and monoclonal antibodies. A subset of these deposits also bind the amyloid-specific dye thioflavin S, indicating that these deposits have the tinctural characteristics of classic amyloid. Co-expression of β-peptide and transthyretin, a protein implicated in preventing the formation of insoluble β-amyloid, leads to a dramatic reduction in the number of dye-reactive deposits. These results suggest that this invertebrate model may be useful for in vivo investigation of factors that modulate amyloid formation.
机译：转基因秀丽隐杆线虫的线虫已经被工程化以表达潜在的淀粉状人类蛋白。这些动物包含其中线虫的肌肉特异性unc-54启动子/增强子驱动源自人cDNA克隆的适当编码区表达的构建体。包含表达42个氨基酸的β-淀粉样蛋白肽（源自人淀粉样蛋白前体蛋白cDNA）的构建物的动物会产生与抗β-淀粉样蛋白多克隆抗体和单克隆抗体发生免疫反应的肌肉特异性沉积物。这些沉积物的一部分也结合了淀粉样蛋白特异性染料硫黄素S，表明这些沉积物具有经典淀粉样蛋白的色泽特征。 β肽和运甲状腺素蛋白的共表达是一种与防止不溶性β淀粉样蛋白形成有关的蛋白，可显着减少染料反应性沉积物的数量。这些结果表明，该无脊椎动物模型可用于体内研究调节淀粉样蛋白形成的因素。

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