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首页> 外文期刊>Biochemistry >Myelin Basic Protein Binds to and Inhibits the Fibrillar Assembly of Aβ42 in Vitro
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Myelin Basic Protein Binds to and Inhibits the Fibrillar Assembly of Aβ42 in Vitro

机译：髓磷脂碱性蛋白结合并抑制Aβ42的原纤维组装。

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The deposition of amyloid β-protein (Aβ) fibrils into plaques within the brain parenchyma andnalong cerebral blood vessels is a hallmark of Alzheimer’s disease. Aβ peptides are produced through thensuccessive cleavage of the Aβ precursor protein by β- and γ-secretase, producing peptides between 39 andn43 amino acids in length. The most common of these are Aβ40 (the most abundant) and Aβ42. Aβ42 is morenfibrillogenic than Aβ40 and has been implicated in early Aβ plaque deposition. Our previous studiesndetermined thatmyelin basic protein (MBP) was capable of inhibiting fibril formation of a highly fibrillogenicnAβ peptide containing both E22Q (Dutch) and D23N (Iowa) mutations associated with familial forms ofncerebral amyloid angiopathy [Hoos, M. D., et al. (2007) J. Biol. Chem. 282, 9952-9961]. In this study, wenshow through a combination of biochemical and ultrastructural techniques that MBP is also capable ofninhibiting the β-sheet fibrillar assembly of the normal Aβ42 peptide. These findings suggest that MBP maynplay a role in regulating the deposition of Aβ42 and thereby also may regulate the early formation of amyloidnplaques in Alzheimer’s disease
机译：淀粉样β蛋白（Aβ）原纤维沉积到脑实质和整个脑血管内的斑块中是阿尔茨海默氏病的标志。 Aβ肽是通过β-和γ-分泌酶成功切割Aβ前体蛋白而产生的，从而产生长度在39至43个氨基酸之间的肽。其中最常见的是Aβ40（最丰富）和Aβ42。 Aβ42比Aβ40具有更多的原纤维形成作用，并且与早期Aβ斑块沉积有关。我们先前的研究确定髓磷脂碱性蛋白（MBP）能够抑制含有与家族性脑淀粉样血管病相关的E22Q（Dutch）和D23N（Iowa）突变的高度原纤维形成素Aβ肽的原纤维形成[Hoos，M.D.，et al。 （2007）J.Biol。化学282，9952-9961]。在这项研究中，温秀明通过结合生物化学和超微结构技术的研究表明，MBP还能够抑制正常Aβ42肽的β-折叠原纤维组装。这些发现表明，MBP可能在调节Aβ42的沉积中发挥作用，从而也可能调节阿尔茨海默氏病中淀粉样斑块的早期形成

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