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Neuronal Lewy bodies (LB) with the aggregation of α-synuclein ( α-syn) are the hallmark of this disease. First described by James Parkinson in 1817, this chronic neurodegenerative disease is characterized by the loss of dopaminergic neurons in the substantia nigra (SN) of the midbrain resulting in decreased levels of dopamine in the striatum and disrupted motor control.

Parkinson’s disease (PD) has become increasingly prevalent as the population ages, being the second most prevalent neurodegenerative disorder worldwide. Via the vagal nerve and/or systemic exosomes, toxic α-syn may spread to dopaminergic neurons and pancreatic β-cells linking the pathogenesis of PD and T2D. MiRNA-148a- and galactose-induced mitochondrial oxidative stress activate c-Abl-mediated aggregation of α-syn which is exported by exosome release. The potential uptake of MEX miRNA-148a and miRNA-21 by enteroendocrine cells in the gut, dopaminergic neurons in substantia nigra and pancreatic β-cells may enhance miRNA-148a/DNMT1-dependent overexpression of α-syn and impair miRNA-148a/PPARGC1A- and miRNA-21/LAMP2A-dependent autophagy driving both diseases. MEX are taken up by intestinal epithelial cells and accumulate in the brain after oral administration to mice. This review provides translational evidence that milk exosomes (MEX) disturb α-syn homeostasis. Exosomes are critical transmitters of α-syn from cell to cell especially under conditions of compromised autophagy. Prion-like vagal nerve-mediated propagation of exosomal α-syn from the gut to the brain and pancreatic islets apparently link both pathologies. In T2D, α-syn promotes co-aggregation with islet amyloid polypeptide in pancreatic β-cells. PD is an α-synucleinopathy associated with mitochondrial dysfunction, oxidative stress, deficient lysosomal clearance of α-synuclein ( α-syn) and aggregation of misfolded α-syn.

Epidemiological studies associate milk consumption with an increased risk of Parkinson’s disease (PD) and type 2 diabetes mellitus (T2D).

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