Originally published June 11 2005
Scientists make steps in treating mad cow disease
by Mike Adams, the Health Ranger, NaturalNews Editor
Last week government scientists at the National Institute of Health found that the proteins that cause mad cow disease might be prevented from damaging the brain if they can be kept from binding to healthy brain cells. Mad cow disease and scrapie disease in sheep are similar because proteins the body normally safely harbors somehow fold into abnormal shapes called prions, which causes a chain reaction of misfolds. When enough prions accumulate, they deposit on the brain and leave behind clumps of dead cells. Researchers specially bred mice that were deficient in the fatty acid that prions bind to on brain cells, and when injected with scrapies disease, the specially bred mice showed no symptoms of the disease. Researchers say the test is promising for possibly finding a treatment for mad cow disease.
Government scientists have found an important clue to how rogue proteins that cause mad cow disease and its cousins destroy the brain: These mysterious substances must latch on to the outside of cell membranes to be toxic.
If scientists could break the fatty Velcro-like bond that anchors these so-called prions, they might devise a treatment for the deadly illnesses, suggests research published in Friday's edition of the journal Science.
"We need to focus on that as a target for drug therapy," said the lead researcher, Dr. Bruce Chesebro, a virologist at the National Institutes of Health's Rocky Mountain Laboratories.
Related diseases - including mad cow, scrapie in sheep and the human Creutzfeldt-Jakob disease - are believed to arise when a protein the body normally harbors folds into an abnormal shape, called a prion, and sets off a chain reaction of misfolds.
When enough abnormal prions accumulate, they deposit plaque on the brain and eventually leave clumps of dead brain cells.
To study how prions function, Chesebro and colleagues genetically engineered mice that lacked the fatty anchor that usually binds prions to the surface of cells.
Then the scientists injected the transgenic mice and regular mice with scrapie-causing prions.
Under a microscope, their brains show lots of the telltale plaques.
He is continuing to track some of the mice for signs of more subtle damage than scrapie usually causes, such as memory loss.
If the abnormal prions are not bound to cells' surfaces, they may be unable to disrupt signaling between cells - a leading theory behind their toxicity, said neuropathologist Adriano Aguzzi of the University Hospital of Zurich, Switzerland, in an accompanying editorial.
The work provides "a tantalizing inroad," he said.
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