View article

Alzheimer’s Dementia (AD) and Parkinson’s disease Dementia (PDD) are common causes of dementia characterised by misfolded alpha-Synuclein (SNCA) proteins, amyloid precursor proteins (APP), and microtubule associated protein tau (MAPT). Accumulation of alpha synuclein is involved in cancer. SNCA140 increases oxidative stress, and this leads to elevated amyloidogenic APP processing. There is currently no effective / disease-modifying treatment of AD and PDD. Human mesenchymal stem cells (hMSCs) are promising therapeutic candidates for the repair and regeneration of neural cells, but their viable clinical application in AD and PDD treatment requires consideration of epistatic influence of the lineage substitution of SNCA.

Here, we hypothesised that SNCAPAN exhibit lineage substitution in hMSCs-derived neurons, and it is epistatic to SNCA140 expression.

we examined phenotypic characteristic of AD and PDD biomarkers in hMSCs-derived neurons at p+6 in four biological replicates (n = 4) with non-template controls (NTCs, n = 2) for each target gene using a Q-PCR. Amplification reactions in NTCSNCA98 and NTCSNCA115 were validated by gel electrophoresis. SNCA98-SNCA126 molecular interaction observed was determined using spearman’s rank correlation regression, and this was validated by gel electrophoresis of generic PCR (50°C, 52°C, 54°C, 56°C, 58°C, and 60°C) with NTC using Universal human reference RNA (UHRR) and astrocytoma stem cells. Expression of each gene was normalised to 18S, the endogenous control. Data are presented as mean 2^(−ΔΔCt) ± SEM.

SNCAPAN …