
A chemical dye, which lights up the protein clumps hallmark of Alzheimer's disease slows also aging in worms.
The life-boosting effects of dye - Thioflavin T or basic called yellow 1 - support the idea that establishing aging underlying the deformed proteins. Drugs, which recognize such toxic detritus and warning the cell natural repair and protein recycling systems therefore could be used for the treatment of diseases of old age, a molecular geneticist at the Institute in Novato, California, Buck, who led the investigation says Gordon Lithgow,, published today in Nature1.
Proteins are almost all actions a cell to communicate with other cells to produce energy, essential. But sometimes proteins form the wrong three-dimensional forms. Misfolded proteins do not function properly and, worse still, tend to collect and other cellular systems of gum disease. "To prevent this, provide cells ' chaperone", whose task is to refold deformed proteins. In extreme cases, cells may be affected to these potentially dangerous proteins.
"There is a growing recognition that protein misfolding may be one of the very basic events of aging," says Richard Morimoto was a molecular biologist at Northwestern University in Evanston, Illinois, involved with the study. Worms genetically, for example, live with one on Touren-Up protein recycling, longer than normal worms23.
Silvestre Alavez, a member of Lithgow's lab, had the idea that Thioflavin T, the deformed clumps of protein amyloid-β (associated) colors - which is found in the brains of people with Alzheimer's disease - also this system could cause.
Lithgow was skeptical that the dye could extend the life of the roundworm of Caenorhabditis elegans roundworms, that investigated because the worms associated not produce his laboratory.
Found, small doses of Thioflavin T increases the service life of roundworms by about 78%, Alavez. Worms that have been received not the dye within 20 days all dead, but feed on more than 80% of the worms, providing an optimal dose of Thioflavin T were to the same period still alive. However Thioflavin T had to be carefully measured - too large a dose turned out to be toxic and life significantly reduces the worms.
Lithgow and Alavez have suggested that Thioflavin T life strengthened by the recognition of all types of toxic protein clumps, not only associated. The dye cause vice versa, for example, the effects of the mutations that muscle proteins misfold, and paralyzed at a certain temperature. Potentially toxic aggregates of proteins build up naturally in at the age of worms, they found, an effect which in worms of similar age fed Thioflavin t. was decreased markedly
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"We can think of it some stabilization of misfolded proteins and induced, that the cells on the waste take out," says Lithgow. His team also found that worms, which is missing important, do not deal with deformed proteins gene longer if Thioflavin t fed.
Rudolph Tanzi, neuroscientist at Massachusetts General Hospital in Boston, which was not involved in the work, describes it as an "incredibly cool experiment". Scientists have traditionally focused on the structure of proteins such as associated, because they are visible form plaques in the brain. Recently, however, scientists have recognized that much smaller protein clumps do the most damage to cells. "That goes far beyond the Alzheimer's disease," says Tanzi. "Can it a number of protein aggregates that never show slide to a pathology."
Drugs that mimic the effects of Thioflavin T can find their way into the clinic, says Lithgow. His team found extend similar connections, including ingredient in the Spice turmeric, the life span of roundworms. These chemicals or other drugs can this ramp up the cell protein recycling to treat through of the ages, such as Alzheimer's disease. "It's incredible early days," says Lithgow.
Alavez, S., Vantipalli, M. C., sugar, D. j. S., sound, I. M. & Lithgow, G. j. nature DOI: 10.1038 / nature09873 (2011).Hsu, A. L., Murphy, C. t. & Kenyon, C. Science 300, 1142-1145 (2003).?| Article |?PubMed |?ISI |?ChemPort |Morley, j. F. & Morimoto, R. I. molecular biology Biol. Cell 15, 657-664 (2004).?| Article |?PubMed |?ISI |?ChemPort |If you something offensive or inappropriate or that otherwise are not met our conditions or Community guidelines, select you the appropriate "this comment report" Link.Kommentare on this thread are marked according to the time of booking.This is a public forum. Please keep to our community guidelines. You can be controversial, but please you understand personal or offensive and keep it short. Keep in mind that our threads are for feedback and discussion - not for testing publishing, press releases and advertising.
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