Asante Joseph Jr, Barger Steven W
Graduate Program in Bioinformatics, University of Arkansas at Little Rock, Little Rock, AR, USA.
Department of Geriatrics, University of Arkansas for Medical Sciences, Little Rock, AR, USA.
ASN Neuro. 2025;17(1):2495632. doi: 10.1080/17590914.2025.2495632. Epub 2025 Apr 23.
Alzheimer's disease (AD) is a progressive neurodegenerative disorder that affects more than 50 million people worldwide. One of the hallmark features of AD is the accumulation of amyloid β-peptide (Aβ) protein in the brain. P-glycoprotein (P-gp) is a membrane-bound protein expressed in various tissues, including the cerebrovascular endothelium. It plays a crucial role in the efflux of toxic substances, including Aβ, from the brain. Aberrations in P-gp levels or activity have been implicated in the pathogenesis of AD by promoting the accumulation of Aβ in the brain. Therefore, modulating the P-gp function represents a promising therapeutic strategy for treating AD. P-gp has multiple substrate binding sites, creating the potential for substrates to fall into complementation groups based on these sites; two substrates in the same complementation group may compete with one other, but two substrates in different groups may exhibit cooperativity. Thus, a given P-gp substrate may interfere with Aβ efflux whereas another may promote clearance. These threats and opportunities, as well as other aspects of P-gp relevance to AD, are discussed here.
阿尔茨海默病(AD)是一种进行性神经退行性疾病,全球有超过5000万人受其影响。AD的标志性特征之一是大脑中β-淀粉样肽(Aβ)蛋白的积累。P-糖蛋白(P-gp)是一种在包括脑血管内皮在内的各种组织中表达的膜结合蛋白。它在包括Aβ在内的有毒物质从大脑中流出的过程中起着关键作用。P-gp水平或活性的异常通过促进Aβ在大脑中的积累而与AD的发病机制有关。因此,调节P-gp功能是治疗AD的一种有前景的治疗策略。P-gp有多个底物结合位点,这使得底物有可能根据这些位点分成互补组;同一互补组中的两个底物可能相互竞争,但不同组中的两个底物可能表现出协同作用。因此,一种给定的P-gp底物可能会干扰Aβ的流出,而另一种底物可能会促进其清除。本文将讨论这些威胁和机遇,以及P-gp与AD相关的其他方面。