A aging-related diseases including cancer, heart disorder and type 2 diabetes are associated with defects in protein synthesis and folding.

Previous studies have shown that protein misfolding occurs in insulin-produced β-cells Patients with type 2 diabetesThese cells are found in pancreatic islets.

The stress is believed to be mainly within the endoplasmic reticulum, which is responsible for the production and distribution of proteins in the cell.

Eventually, stress causes cell death.

In a study published in Nature metabolismResearchers at the University of Michigan found that mitochondria also accumulates misfolded proteins, which kills β-cells.

Reversing this process can help treat type 2 diabetes.

Earlier, scientists saw that two protein-insulin and amilin are often wrong in type 2 diabetic patients.

Both are manufactured by β-cells in the pancreas.

Emilin promotes a sense of perfection after meals, while helping insulin cells into sugar helps reduce blood sugar levels.

Emilin can create amyloid sets in the cells of diabetes that are similar to the amyloid plaques found in the brain in Alzheimer’s disease.

These two proteins were the only focus in diabetic islet cells. We wanted to take a fair approach and find all misfold proteins in these cells. ,

Scott Solemanpore, MD, Professor of Larry Soderquist Diabetes Research and Director of Miching Diabetes Research Center

The team compared islet cells to the donors with type 2 diabetes to healthy donor cells and found that missfold protein manufactures higher levels than other in the islet cells in mitochondria.

The group had earlier discovered that mitochondrial damage affects β-cells, but the underlying mechanisms were not clear.

By sequence of genes and proteins in healthy and diabetes cells, researchers found that defense systems that wrongly respond to mitochondrial proteins are not operational during type 2 diabetes.

In particular, Lonp1, a protein responsible for getting rid of the Lonp1, damaged or misfolded protein was low in cells with diabetes.

“Although Lonp1 has some associations with rare mitochondrial diseases, this is the first study to show that it is a role in type 2 diabetes,” said Soolemanpor.

The team confirmed its findings by comparing mice, in which the Lonp1 system was with those who did not.

Lonp1 deficient mice had high glucose levels and low β-cells.

When Lonp1 was re -presented in mice, these defects were reversed, suggesting that targeting this system could be a new avenue for therapy.

“It is clear that people with type 2 diabetes have problems in eliminating the misfolded protein,” said Soolemanpore.

“The next step is to find drugs that can help these proteins resume or eliminate.”

The group is also interested in understanding the timeline of how type 2 diabetes develops.

The situation is often found in adults and solemanpore hypotheses that misfold proteins can accumulate over time and eventually overwhelm β-cells, causing disease.

Therefore, initial intervention may be important.