Malcolm Leissring and his team of researchers at the Mayo Clinic in Jacksonville, Fla. are partying like it’s 1955.
Using work developed by scientists more than five decades ago, Leissring, an assistant professor of molecular neuroscience, has identified a way to prevent an insulin-chewing enzyme from breaking down the hormone needed to remove sugar from the blood.
The technology, currently in animal testing, could pave the way for a new class of “protease inhibitor” drugs that help cells hold onto insulin for longer periods of time. While scientists over the years have focused on ways to stimulate the body to create more insulin, Leissring’s work allows patients to better benefit from the insulin they do produce.
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The research is “interesting and should be explored further,” said Dr. Antoinette Moran, division chief of pediatric endocrinology and diabetes at the University of Minnesota.
One major challenge is calibrating the right amount of insulin, she said. For diabetic patients, too little insulin results in dangerous levels of sugar accumulating in the blood. But too much insulin can prompt hyperinsulinemic hypoglycemia and damage the brain. Researchers must find a way to inhibit the enzyme so that just the right amount of insulin can do its job, Dr. Moran said.
Protease inhibitors, more commonly associated with the breakthrough anti-HIV drugs developed in the mid 1990s, is a relatively novel way to combat diabetes, experts say. Yet, the research dates back to 1955 when scientists purified a naturally occurring compound that could interfere with insulin-degrading enzyme (IDE). But scientists had never identified the composition of that compound — until now.
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- Malcolm Leissring, researcher, Mayo Clinic — Jacksonville, Fla.
Leissring and his team created Ii1 (IDE inhibitor 1), a compound that binds itself to IDE’s unique chemical structure. The enzyme resembles a Pac-Man whose “mouth” gobbles up insulin. Ii1 essentially acts as a latch that keeps IDE’s “mouth” shut.
“We’ve solved a 60-year-old mystery,” Leissring said. Scientists in 1955 “never finished the job. I’m fulfilling their work.”
For some reason, the liver destroys about 50 percent of the insulin produced by the pancreas. Ii1 will allow more of that insulin to reach the bloodstream, he said.
To Leissring’s pleasant surprise, the inhibitor also produced a “insulin-sparing effect.” Insulin used by “destination cells ” to convert glucose into fat appear to stick around longer. In other words, Ii1 allows insulin to work better and last longer, he said.
Leissring says he’s not sure why researchers never completed the work begun in the 1950s. He suspects finding a compound that could bind to IDE’s unique chemical structure proved too difficult. In addition, IDE could prove useful in treating Alzheimer’s disease so developing an inhibitor that stops the enzyme never gained much attention, he said.
Since Ii1 is about 1 million times more powerful than other protease inhibitors, Leissring says he still needs to develop stable compounds the body can tolerate.
However, the combination of protease inhibitors and drugs that instruct the pancreas to produce more insulin could be a powerful one-two punch in treating diabetes, Leissring said.
