Abstract
Parkinson’s disease (PD) is the second most prevalent neurodegenerative disease. However, it is unclear whether microbiota and metabolites have demonstrated changes at early PD due to the difficulties in diagnosis and identification of early PD in clinical practice. In a previous study, we generated A53T transgenic monkeys with early Parkinson’s symptoms, including anxiety and cognitive impairment. Here we analyzed the gut microbiota by metagenomic sequencing and metabolites by targeted gas chromatography. The gut microbiota analysis showed that the A53T monkeys have higher degree of diversity in gut microbiota with significantly elevated Sybergistetes, Akkermansia, and Eggerthella lenta compared with control monkeys. Prevotella significantly decreased in A53T transgenic monkeys. Glyceric acid, L-Aspartic acid, and p-Hydroxyphenylacetic acid were significantly elevated, whereas Myristic acid and 3-Methylindole were significantly decreased in A53T monkeys. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (KO0131) and the oxidative phosphorylation reaction (KO2147) were significantly increased in metabolic pathways of A53T monkeys. Our study suggested that the transgenic A53T and α-syn aggregation may affect the intestine microbiota and metabolites of rhesus monkeys, and the identified five compositional different metabolites that are mainly associated with mitochondrial dysfunction may be related to the pathogenesis of PD.
Highlights
Parkinson’s disease (PD) is the second most prevalent neurodegenerative disease[1,2]
The composition and diversity of the gut microbiota are different in A53T monkeys of early PD and control monkeys
The alpha diversity significantly elevated in A53T transgenic monkeys compared to control monkeys (Shannon Index: p < 0.05)
Summary
Parkinson’s disease (PD) is the second most prevalent neurodegenerative disease[1,2]. Cognitive impairment, anxiety and disturbed sleep, asymmetric vague shoulder pain, or depression[3,4,5,6]. The most recent hypothesis is that PD may originate in the gut and spread to the brain through α-syn transmission, systemic inflammation, and increased permeability of the blood-brain barrier[7,8]. New data suggests that α-syn can interact with mitochondria by binding to the mitochondrial outer membrane[19,20]. This indicates a certain relationship between the α-syn and the mitochondria. The accumulation of α-syn in the outer membrane may interfere with the introduction mechanism of the protein but may interfere with the homeostatic pathway of other mitochondria[19,21]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
