EXPRESSION OF HUMAN BETA-AMYLOID PEPTIDE IN TRANSGENIC CAENORHABDITIS-ELEGANS
EXPRESSION OF HUMAN BETA-AMYLOID PEPTIDE IN TRANSGENIC CAENORHABDITIS-ELEGANS
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DOI：
10.1073/pnas.92.20.9368
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发表时间：
1995-09-26
影响因子：
11.1
通讯作者：
LINK, CD
中科院分区：
文献类型：
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作者：
LINK, CD
转基因秀丽线虫线虫已经被改造成表达潜在的淀粉样人类蛋白。在这些动物中，线虫的肌肉特异性UNC-54启动子/增强子驱动来自人类cDNA克隆的适当编码区的表达。含有表达42个氨基酸的β-淀粉样多肽(源自人类淀粉样前体蛋白基因)的构建体的动物产生肌肉特异性沉积，与抗-β-淀粉样多克隆和单抗发生免疫反应。这些沉淀物中的一部分还与淀粉样蛋白特异性染料S结合，表明这些沉淀物具有经典淀粉样蛋白的组织结构特征，β-肽和转甲状腺素的共同表达导致染料反应性沉积的数量急剧减少。这些结果表明，这种无脊椎动物模型可能有助于体内研究调节淀粉样蛋白形成的因素。
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 beta-amyloid peptide (derived from human amyloid precursor protein cDNA) produce muscle-specific deposits immunoreactive with anti-beta-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, Coexpression of beta-peptide and transthyretin, a protein implicated in preventing the formation of insoluble beta-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.