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首页> 外文期刊>Neuroscience Letters: An International Multidisciplinary Journal Devoted to the Rapid Publication of Basic Research in the Brain Sciences >The Abeta1-42M35C mutated amyloid peptide Abeta1-42 and the 25-35 fragment fail to mimic the subtype-specificity of actions on recombinant human nicotinic acetylcholine receptors (alpha7, alpha4beta2, alpha3beta4).
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The Abeta1-42M35C mutated amyloid peptide Abeta1-42 and the 25-35 fragment fail to mimic the subtype-specificity of actions on recombinant human nicotinic acetylcholine receptors (alpha7, alpha4beta2, alpha3beta4).

机译：Abeta1-42M35C突变的淀粉样蛋白肽Abeta1-42和25-35片段无法模仿对重组人烟碱型乙酰胆碱受体（alpha7，alpha4beta2，alpha3beta4）的作用的亚型特异性。

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摘要

Alzheimer's disease (AD) is a neurodegenerative condition involving accumulation of the beta-amyloid peptide, Abeta1-42. Previously we have shown that amyloid peptides (Abeta1-42, Abeta1-40) have different actions on the three major brain nicotinic acetylcholine receptor (nAChR) subtypes (alpha7, alpha4beta2 and alpha3beta4). The methionine in position 35 of Abeta (M35) has been shown to be important in the toxicity of Abeta and the 25-35 fragment can mimic some of the actions of the Abeta1-42 peptide. However, the extent to which this mutant and the fragment mimic subtype selectivity is unknown. Two-electrode voltage-clamp electrophysiology has been used to study the actions on alpha7, alpha4beta2 and alpha3beta4 recombinant nAChRs expressed in Xenopus laevis oocytes of full length Abeta1-42, and Abeta peptide fragments, scrambled peptides, and the Abeta1-42 peptide containing mutations of the methionine in position 35. The Abeta25-35 fragment did not display subunit specificity. Abeta1-42 with an M35C mutation showed similar subtype-specificity to wild-type Abeta1-42. However, Abeta1-42 with an M35V substitution reduced the peak amplitude of ACh-induced currents recorded from alpha4beta2 nAChRs, but did not affect those recorded from alpha7 or alpha3beta4. These results indicate that the amino acid in position 35 of Abeta1-42 is an important determinant of the subtype-specificity of this peptide on human recombinant alpha7, alpha4beta2 and alpha3beta4 nAChRs and that the 25-35 fragment fails to mimic all of the actions of the full-length peptide.
机译：阿尔茨海默氏病（AD）是一种神经退行性疾病，涉及β-淀粉样肽Abeta1-42的积累。以前我们已经证明淀粉样蛋白肽（Abeta1-42，Abeta1-40）对三种主要的脑烟碱型乙酰胆碱受体（nAChR）亚型（alpha7，alpha4beta2和alpha3beta4）具有不同的作用。已显示Abeta（M35）位置35的甲硫氨酸对Abeta的毒性很重要，而25-35片段可模仿Abeta1-42肽的某些作用。但是，该突变体和片段模拟亚型选择性的程度尚不清楚。两电极电压钳电生理已用于研究对全长Abeta1-42的非洲爪蟾卵母细胞中表达的alpha7，alpha4beta2和alpha3beta4重组nAChR的作用以及Abeta肽片段，加扰的肽和包含突变的Abeta1-42肽35位蛋氨酸的残基。Abeta25-35片段未显示亚基特异性。具有M35C突变的Abeta1-42显示出与野生型Abeta1-42类似的亚型特异性。但是，具有M35V取代的Abeta1-42降低了从alpha4beta2 nAChRs记录的ACh诱导的电流的峰值，但不影响从alpha7或alpha3beta4记录的电流。这些结果表明，Abeta1-42第35位的氨基酸是该肽对人重组α7，α4β2和α3β4nAChRs的亚型特异性的重要决定因素，并且25-35片段无法模拟Aβ1-42的所有作用。全长肽。

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