Carbohydrate and blood sugar

A natural carbohydrate can help lower blood sugar levels

Washington: A new study by reearchers at the University of Virginia Health System has found that a carbohydrate isolated from the liver can help lower blood sugar levels. The study, published in the latest issue of the journal Biochemistry, states that a carbohydrate isolated from the liver lowers blood sugar levels after it is injected into diabetic rats. This compound, called D-chiro-Inositol-Galactosamine, or INS2, acts as a messenger inside cells to switch on enzymes that regulate blood sugar, taking glucose from the bloodstream into the liver and muscles where it is stored. The research could lead to new drugs to treat type 2 diabetes, the most common form of the disease. In type 2, the blood has normal or high levels of the insulin, but the liver and muscles don't respond well to the hormone. As a result, blood sugar stays high, causing health problems. "We believe this molecule works by sending a message inside the cell to respond to insulin, which helps cells dispose of excess glucose," said Joseph Larner, who has been studying the molecule for nearly two decades.

Larner and his colleagues isolated INS2 from cow livers, determined its chemical structure, synthesized it, then injected the compound into diabetic rats, with blood sugar levels at or above 500 milligrams per deciliter. The rats were then injected with insulin. Diabetes researchers at UVa were pleased that the more compound they injected, the more blood sugar decreased in the animals. "This compound is dose dependent and active. It potentiates the action of insulin," explained David Brautigan, director of the Center for Cell Signaling. Larner and Brautigan are part of a multi-disciplinary team at UVa that includes chemist Milton Brown and structural biologist John Bushweller. Using computer modeling, they docked the INS2 compound onto an enzyme in cells called PP2C. If INS2 could activate PP2C, it would trigger other events in cells activated by insulin. "INS2 was added and the purified PP2C enzyme was activated. When we changed one amino acid in PP2C that the modeling predicted was the site for INS2, then the activation by INS2 was absent. In that way the enzyme assay confirmed the model," Brautigan said.
-Oct 27, 2005