It has sometimes been theorized that there was a protein behind type II diabetes, but it is now confirmed by researchers. This may just lead to a treatment that could help millions.
Worldwide, some 400 million people live with diabetes and most have type II. Type II Diabetes takes place when the body is not able to produce sufficient insulin or if the insulin isn’t working as it should.
There is a fiber-like structure that is seen in type II diabetes known as amyloid fibrils. In a 2020 study published in Nature Structural and Molecular Biology, scientists reveal that they have observed it for the 1st time.
According to the research, Amyloid fibrils occur from a type of peptide protein that clumps together, known as amylin. Amylin is associated with the regulation of glucose levels in the human body.
Delighted to share our latest work on #amyloid published today in @NatureSMB with work on wild-type and S20G amylin fibrils. Fantastic #CryoEM collaboration with Sheena @RadfordLab and an amazing bit of work by @R_U_Gallardo in #LockDown https://t.co/46omSbeYxd pic.twitter.com/f9AbYfvzZW
— Neil Ranson (@naranson) September 14, 2020
According to the University of Leeds, Professor Neil Ranson, the study author from the University of Leeds, calls the find “really exciting.” He feels that way because it “is crucial in understanding the disease process… with these structures we’re getting the first glimpse at what might be going on.”
They used cryo-electron microscopy, a type of electron microscope technology to visualize the fiber structure.
After freezing the samples, they were analyzed down to the point where individual atoms could be seen.
Amyloid fibrils known as S20G are the variant that is seen in people with early-onset type II diabetes. After comparing S20G with amyloid fibrils found in those without type II diabetes, they made the discovery.
Thousands of images were analyzed in order to come up with the results. According to researchers, the molecules formed intricate structures like rungs in a ladder.
When the wild type fibrils were observed, they only had two copies of amylin per rung but with S20G, there were 3 per rung. This seemed to suggest that fibrils can form templates so additional amylin can lock to them.
Perhaps this is why S20G-variant protein lumps together quickly, leading to the rapid onset of type II diabetes.
Professor Sheena Radford is the co-author of the study from the Astbury Center. According to the University of Leeds, she said that it is important, “Not just for understanding amylin-but for understanding many amyloid diseases in which run-away fibril formation occurs.”
Amyloid fibril buildup may also be associated with other diseases, including Huntington’s disease, Parkinson’s, and Alzheimer’s.
If scientists are able to understand amyloid fibrils even better, it may lead to better diagnosis and treatments for those who suffer from those types of diseases.
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