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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 >A peptide derived from the C-terminal region of acetylcholinesterase modulates extracellular concentrations of acetylcholinesterase in the rat substantia nigra.
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A peptide derived from the C-terminal region of acetylcholinesterase modulates extracellular concentrations of acetylcholinesterase in the rat substantia nigra.

机译：源自乙酰胆碱酯酶C末端区域的肽调节大鼠黑质中乙酰胆碱酯酶的细胞外浓度。

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摘要

It is well established that acetylcholinesterase (AChE) has 'non-classical' functions independent of cholinergic transmission. A region of AChE distinct from the catalytic site may be responsible for these actions via a 14-residue peptide located between residues 586-599 at the C-terminus of human AChE. This AChE-peptide possesses a high amino acid sequence homology with a region of amyloid precursor protein and shares many biophysical and physiological characteristics. In this study, the effect of AChE-peptide (AEFHRWSSYMVHWK) on the extracellular levels of endogenous AChE was examined in rat substantia nigra in vitro. A chemiluminescent assay was used to continuously measure the soluble AChE concentration from tissue punches of the substantia nigra. Application of NMDA evoked an increase in extracellular AChE levels consistent with previous results obtained from in vivo models. AChE-peptide, when applied alone, had no effect on AChE release: however, when co-applied with NMDA, AChE-peptide reduced the effectiveness of NMDA to evoke release of AChE. These results indicate, in a region of the brain central to the aetiology of Parkinson's disease, that an AChE-peptide fragment derived from AChE displays a bioactivity that could involve regulation of Ca(2+) availability and hence the release of AChE.
机译：公认的是，乙酰胆碱酯酶（AChE）具有独立于胆碱能传递的“非经典”功能。 AChE不同于催化位点的区域可能通过位于人AChE C末端586-599残基之间的14个残基的肽负责这些作用。该AChE-肽与淀粉样前体蛋白区域具有高度的氨基酸序列同源性，并具有许多生物物理和生理特性。在这项研究中，在体外大鼠黑质中检查了AChE肽（AEFHRWSSYMVHWK）对内源性AChE胞外水平的影响。化学发光测定法用于连续测量黑质组织穿孔时的可溶性AChE浓度。 NMDA的应用引起细胞外AChE水平的增加，这与从体内模型获得的先前结果一致。单独使用时，AChE肽对AChE的释放没有影响：但是，当与NMDA共同使用时，AChE肽会降低NMDA引起AChE释放的有效性。这些结果表明，在帕金森氏病的病因中心的大脑区域中，衍生自AChE的AChE肽片段显示出生物活性，该生物活性可能涉及Ca（2+）可用性的调节，从而释放AChE。

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