Researchers reveal potential new drug target for dementia -
Researchers from King's College London have discovered how a "scaffold" that allows molecular key elements cells interact, comes apart in dementia and motor neuron disease, revealing a potential new target for drug discovery.
The study, published today in Nature Communications was funded by the Medical Research Council in the UK, Wellcome Trust Research UK and Alzheimer Association Motor Neurone Disease
researchers examined two components of cells :. mitochondria, "house power" the cell that generate energy for the cell;. and the endoplasmic reticulum (ER), which makes the protein and calcium stores the signaling processes within the cell ER and mitochondria form close associations and interactions allow a number of important cellular functions. However, the mechanism by which ER and mitochondria become linked has not hitherto been understood
Professor Chris Miller, King of the Institute of psychiatry and lead author of the paper, said: ". At the molecular level, many processes go wrong in dementia and motor neuron disease, and one of the riddles we face is whether there is a common pathway linking these processes. Our study suggests that the release of this "scaffolding" between mitochondria and ER in the cell may be a key process in neurodegenerative diseases such as dementia or motor neuron disease. "
by studying cells in a dish, the researchers found that ER called VAPB protein binds to mitochondrial protein called PTPIP51 to form a "scaffold" for ER and mitochondria to form close associations. in fact, by increasing the levels of VAPB and PTPIP51, mitochondria and ER re-organized to form tighter bonds.
many cell functions are controlled by the ER-mitochondria associations are disturbed in neurodegenerative diseases, so the researchers have studied how the strength of this "scaffold" has been affected in these diseases. TPD-43 is a protein that is strongly associated with amyotrophic lateral sclerosis (ALS, a form of motor neuron disease) and frontotemporal dementia -temporale (FTD, the second most common form of dementia), but exactly how the protein causes neurodegeneration is not well understood.
The researchers studied how TPD-43 to mice affected cells in a dish. They found that higher levels of TPD-43 resulted in a relaxation of the scaffolding which reduced the obligations of ER-mitochondria, affecting some important cellular functions that are linked to ALS and FTD
Professor Miller concludes :. "Our findings are important in terms of advancing our understanding of basic biology, but can also provide a potential new target for developing new treatments for these devastating disorders."
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