Abstract
Despite many years of research, radical treatment of Alzheimer's disease (AD) has still not been found. Amyloid-β (Aβ) peptide is known to play an important role in the pathogenesis of this disease. AD is characterized by three main changes occurring in the central nervous system: (1) Aβ plaque accumulation that prevents synaptic communication, (2) the accumulation of hyperphosphorylated tau proteins that inhibit the transport of molecules inside neurons, and (3) neuronal cell loss of the limbic system. Mechanisms leading to Aβ accumulation in AD are excessive Aβ production as a result of mutations in amyloid precursor protein or genes, and impairment of clearance of Aβ due to changes in Aβ aggregation properties and/or Aβ removal processes. Human ATP-binding cassette (ABC) transporters are expressed in astrocyte, microglia, neuron, brain capillary endothelial cell, choroid plexus, choroid plexus epithelial cell, and ventricular ependymal cell. ABC transporters have essential detoxification and neuroprotective roles in the brain. The expression and functional changes in ABC transporters contribute to the accumulation of Aβ peptide. In conclusion, the review was aimed to summarize and highlight accumulated evidence in the literature focusing on the changing functions of human ABC transporter members, in AD pathogenesis and progression.
Highlights
Central nervous system (CNS) barriers, consisting of the blood–brain barrier (BBB) and blood–cerebrospinal fluid barrier, are responsible for the protection of the microenvironment, which is vital in the regulation of neuronal functions.[1]
A dense accumulation of amyloid-β (Aβ), that is, a peptide resulting from amyloid precursor protein (APP) processing, and deposition of hyperphosphorylated tau protein appear in the CNS as Alzheimer’s disease (AD) pathology.[3,4]
We aimed to evaluate the roles and physiopathological features of human ATP-binding cassette (ABC) carrier members expressed in the CNS and associated with AD pathogenesis
Summary
Central nervous system (CNS) barriers, consisting of the blood–brain barrier (BBB) and blood–cerebrospinal fluid barrier, are responsible for the protection of the microenvironment, which is vital in the regulation of neuronal functions.[1]. AD is closely associated with microvascular pathologies, such as degeneration and/or dysfunction in the microvascular structure, which are key places in the exchange of nutrients in the brain between the brain and circulating blood These pathologies cause Aβ accumulation by disrupting the integrity of the BBB and preventing the clearance of neurotoxic molecules (such as Aβ) in the CNS.[1] Microtubuleassociated tau proteins and the Aβ40, Aβ42, the most common form of Aβ produced by cleavage of APP, represent the molecular-level character of AD. Enabling the movement of their substrates through intracellular organelles and cell membranes, ABC transporters, which provide the movement of its substrates from intracellular organelles and cell membranes, ensure the homeostasis of the body.[6] Recently, the emphasis on the role of ABC carriers in CNS disorders associated with high levels of Aβ, such as AD, has increased research into the causes of changes or dysfunction in the processes and pathways in which the carrier family is involved. We aimed to evaluate the roles and physiopathological features of human ABC carrier members expressed in the CNS and associated with AD pathogenesis
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