The findings, said Ivor J. Benjamin, division chief of cardiology at the University of Utah's School of Medicine, suggest a new class of drugs could be developed to treat or prevent heart disease.

A protein called alpha B-Crystallin, considered a "molecular chaperone," helps long strips of other proteins fold inside cells, according to a U. news release.

The cells, in turn, produce a normal level of reduced glutathione, which is good for the body.

When the gene that produces alpha B-Crystallin mutates, however, the proteins misfold, becoming aggregates - or damaged proteins. As a result, cells produce too much reduced glutathione, triggering heart-damaging "reductive stress."

Benjamin said he found that by lowering the level of reduced glutathione in laboratory mice, he dramatically decreased their chances of dying, according to the news release.

The research physician accomplished this by mating mice that have the mutated alpha B-Crystallin - and thus a higher level of the enzyme that regulates glutathione - with mice that have a much lower level of the antioxidant-regulating enzyme.

The offspring, he found, had normal levels of reduced glutathione and did not develop heart failure.

"I think the important discovery is we lowered the amount of this antioxidant enzyme. We were able to eliminate the aggregates," said Benjamin, principal author of a study to be published today in the journal Cell.

Additionally, he said, "We think this has important implications for other protein-aggregate disorders, such as neurodegenerative disorders" that have similar features.

Heart disease, as well as Alzheimer's and Parkinson's, are all considered protein-aggregate diseases.

"This is a case of too much of a good thing," he said. "Our findings indicate reductive stress warrants a more thorough investigation."

lrosetta@sltrib.com