LONDON - A team of British scientists announced new evidence linking disease today degenerative fatal brain that killed 10 people in Britain since 1994, with bovine spongiform encephalopathy (BSE), a neurological condition known as `` the mad cow '' that has infected more than 150,000 cattle British.
The researchers have developed a test that reveals strong similarities between proteins considered responsible for human disease - a new variant of Creutzfeldt-Jakob disease (vCJD) - and those related to the BSE. `` This is the most suggestive evidence so far that the new variant CJD came from BSE, '' said Byron Caughey, a biochemist at the National Institute of Health Rocky Mountain Laboratory (NIH) in the Montana. All experts agree, however.
At a press conference this morning, John Collinge of Imperial College School of Medicine at the hospital, St. Mary London, said the simple test distinguishes the differences between the infectious proteins, or prion, isolated from the brain of humans or infected animals. Researchers decompose prion with an enzyme and separating them depending on the number of sugar groups attached thereto. relative abundances of proteins with different numbers of sugar groups produce characteristic patterns of BSE, classical CJD and the new strain of vCJD. The report will appear in tomorrow Collinge Nature
Collinge's team found that the prion model of vCJD. - That hit the victims up to 45 years - looks much closer to the ESB model of people with classic CJD, a common condition, although rare, which tends to hit the elderly. But because the new test requires brain tissue, it is usually possible to run after a patient died. The team now hopes to detect proteins in other tissue of the body that could be sampled while the patient is still alive. They analyze the lymph nodes and tonsils, where prions replicate. Collinge hope to have the results of such a test in a few months. With a potentially test can detect the disease early, `` we should seriously consider developing therapeutic products, '' said Collinge.
But some experts welcomed the results with caution. `` It's an interesting idea, but not compelling, '' said Paul Brown, a neuroscientist at the main campus of NIH in Bethesda, Maryland. Brown said he is skeptical that the differences between the forms of prions revealed in the new trial account for variations of CJD, and awaits the results of experiments on transgenic mice. Mice produce human prion which, when modified, is bound to vCJD. The mice were injected with brain tissue of victims of vCJD, but so far none have contracted CJD. Results are expected next year.
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