Exosomes in Pathogenesis, Diagnosis, and Treatment of Alzheimer's Disease
- PMID: 31056537
- PMCID: PMC6515980
- DOI: 10.12659/MSM.914027
Exosomes in Pathogenesis, Diagnosis, and Treatment of Alzheimer's Disease
Abstract
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of ß-amyloid peptide 1-42 and phosphorylation of tau protein in the brain. Thus far, the transfer mechanism of these cytotoxic proteins between nerve cells remains unclear. Recent studies have shown that nanoscale extracellular vesicles (exosomes) originating from cells may play important roles in this transfer process. In addition, several genetic materials and proteins are also involved in intercellular communication by the secretion of the exosomes. That proposes novel avenues for early diagnosis and biological treatment in AD, based on exosome detection and intervention. In this review, exosome-related pathways of cytotoxic protein intercellular transfer in AD, and the effect of membrane proteins on exosomes targeting cells are first introduced. The advances in exosome-related biomarker detection in AD are summarized. Finally, the advantages and challenges of reducing cytotoxic protein accumulation via exosomal intervention for AD treatment are discussed. It is envisaged that future research in exosomes may well provide new insights into the pathogenesis, diagnosis, and treatment of AD.
Conflict of interest statement
None.
References
-
- Lattanzi S, Carbonari L, Pagliariccio G, et al. Neurocognitive functioning and cerebrovascular reactivity after carotid endarterectomy. Neurology. 2018;90:e307–15. - PubMed
-
- McKenzie JA, Spielman LJ, Pointer CB, et al. Neuroinflammation as a common mechanism associated with the modifiable risk factors for Alzheimer’s and Parkinson’s diseases. Curr Aging Sci. 2017;10:158–76. - PubMed
-
- Ling D, Salvaterra PM. A central role for autophagy in Alzheimer-type neurodegeneration. Autophagy. 2009;5:738–40. - PubMed
-
- Alonso Adel C, Mederlyova A, Novak M, et al. Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J Biol Chem. 2004;279:34873–81. - PubMed
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