A new study in mice has found that a protein that damages toxic cellular waste as a result of high sugar consumption can itself be damaged by a sugary diet. The animal model study by researchers from Tufts University and other institutions shows that the results potentially apply to humans.
According to the study which appears on Aging Cell shows that too much consumption of sugar can damage a protein that alleviates age-related cellular stemming. Allen Taylor, the study’s co-author and lead researcher at Nutrition & Vision Research Team at the university said that this appears like a “double jeopardy impact.” This is because excess sugars damage the proteins and should be removed to avoid toxic effects on cells. Also, on the other hand, the protein that works to damage and repairs the cells from a high sugar diet is vulnerable to excess sugars leaving the cells threatened.
High-sugar die consumption, which is typical in the US, results in a build-up of damaging by-products in the cells. These by-products, often referred to as advanced glycation end products (AGEs), build up and can cause age-related diseases. Most importantly, the results indicated that the Pac-Man-like protein, P62, is vital in removing toxic cellular waste resulting from high sugar intake through autophagy, which means self-eating. Autophagy is a process that clears damaging by-products from cells due to high-sugar consumption.
The p62 has a self-cleaning ability and it is vital in clearing AGEs. Interestingly augmenting p62 speeds up cell cleaning but the loss of p62 can lead to cell toxicity because of sugar and AGEs accumulation. Notably, gylcative stress, which is a sugar reaction, tends to compromise the p62’s cell targeting clean-up.
Eloy Bejarano, the study’s co-author said that the results suggest that p62 can be a new intervention target to minimize the damage of sugar ion aging cells. Bejarano added that this could have applications some day for targeting heart disease, age-related macular degeneration, Parkinson’s, and Alzheimer’s diseases.