Hernández-Zimbrón Luis Fernando, Rivas-Arancibia Selva
Rev Neurosci. 2014;25(6):773-83. doi: 10.1515/revneuro-2014-0025.
Extracellular and intracellular accumulation of amyloid beta 1-42 peptide in different states of aggregation has been involved in the development and progression of Alzheimer's disease. However, the precise mechanisms involved in amyloid beta peptide neurotoxicity have not been fully understood. There exists a wide variety of studies demonstrating the binding of amyloid beta peptide to a great variety of macromolecules and that such associations affect the cellular functions. This type of association involves proteins and receptors anchored to the plasma membrane of neurons or immune cells of the central nervous system as well as intracellular proteins that can alter intracellular transport, activate signaling pathways or affect proper mitochondrial function. In this review, we present some examples of such associations and the role played by these interactions, which are generally involved in the pathological progression of Alzheimer's disease.
淀粉样β蛋白1-42肽在不同聚集状态下的细胞外和细胞内积累与阿尔茨海默病的发生和发展有关。然而，淀粉样β肽神经毒性的确切机制尚未完全明确。有大量研究表明淀粉样β肽与多种大分子结合，且这种结合会影响细胞功能。这种结合涉及锚定在神经元或中枢神经系统免疫细胞质膜上的蛋白质和受体，以及可改变细胞内运输、激活信号通路或影响线粒体正常功能的细胞内蛋白质。在本综述中，我们列举了一些此类结合的例子以及这些相互作用所起的作用，它们通常与阿尔茨海默病的病理进展有关。
