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Blocking diabetes with an impostor.

Blocking diabetes with an impostor

The chemical cross-linking believed to be responsible for some of the long-term effects of diabetes can be blocked, Rockefeller University researchers have found. After completing toxicology studies in animals, they hope to try the technique in humans within a year.

The blocking process halts some sloppy biochemistry that comes with diabetes. High concentrations of glucose in the blood react with structural proteins--primarily collagen -- throughout the body, resulting in the formation of clumps that protrude from the protein. These agglomerations are also a result of the normal aging process.

The agglormerations in turn link to one another or to blood proteins. Many researchers believe the cross-linking stiffens blood vesselsand other structures, leading to such diabetic complications as eye, kidney and cardiovascular problems. These complications occur despite insulin treatment, and are a major cause of death and disability in diabetics.

The agglomerations on the structural proteins, says Michael Brownlee, one of the researchers, grab onto other structural or blood proteins like bear traps. "The cross-links become permanent features," he says.

To break into the cycle in diabetic rats, he and Anthony Cerami and their colleagues at Rockefeller in New York City used aminoguanidine, a chemical that resembles the protein "feet" that can get caught in the trap.

Aminoguanidine prevents the collagen-collagen binding, they report in the June 27 SCIENCE. At last week's meeting of the American Diabetes Association (ADA) in Anaheim, Calif., they reported that it also prevents the binding of colagen to blood proteins and prevents the early structural changes of diabetes-associated kidney damage.

Brownlee's group is currently working on toxicity studies in animals. In the initial studies, "the rats that used it for four to five months tolerated it well," Brownlee says.

Using aminoguanidine will enable researchers to determine definitvely the role of cross-linking in diabetes, says ADA President Daniel Porte, a diabetes researcher at the University of Washington and at the Veterans Administration Medical Center in Seattle. "At this point it is still hypothetical that this mechanism is important," he says.

If further research bears it out, the work has great potential for diabetics, Porte says. But first that research must be done. "It may mean tremendous things in the future, but it may simply lead to absolutely nothing," he cautions.
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Title Annotation:aminoguanidine
Author:Silberner, Joanne
Publication:Science News
Date:Jul 5, 1986
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