The aggregate proteins strewn about the brain are the hallmark of one of the most ordinary neurodegenerative disorders: Alzheimer's disease. But while these irregular, gunky proteins, called amyloid-β, are supposed to give to the deterioration of memory and cognitive capability in Alzheimer's patients, no one knows how they guide to these symptoms, and the harshness of the dementia doesn't straight depend on the amount of amyloid-β plaques originate in diseased brains.
New experiment from The Rockefeller University, construction on a paper published earlier this year, show how amyloid-β interact with a clotting agent in the blood, growing blood clots that are harder than usual to break down and starving neurons of their usual supply of oxygen. The research suggest that the effects of amyloid-β on the blood vessels feed the brain could be an significant aspect of the havoc they wreak on the brain.
"There has been a proposal that vascular dementia and Alzheimer's disease might be connected, and our present work provides a possible connection between the two," says Sidney Strickland, head of the Laboratory of Neurobiology and Genetics at Rockefeller. Led by Hyung Jin Ahn, a postdoctoral connect in Strickland's lab, researchers used biochemical tests to home in on accurately how a particularly nasty form of amyloid-β, called Aβ42, interact with the blood clotting agent fibrinogen, reason fibrinogen to raise into unusual clot structure that are hard to degrade.
New experiment from The Rockefeller University, construction on a paper published earlier this year, show how amyloid-β interact with a clotting agent in the blood, growing blood clots that are harder than usual to break down and starving neurons of their usual supply of oxygen. The research suggest that the effects of amyloid-β on the blood vessels feed the brain could be an significant aspect of the havoc they wreak on the brain.
"There has been a proposal that vascular dementia and Alzheimer's disease might be connected, and our present work provides a possible connection between the two," says Sidney Strickland, head of the Laboratory of Neurobiology and Genetics at Rockefeller. Led by Hyung Jin Ahn, a postdoctoral connect in Strickland's lab, researchers used biochemical tests to home in on accurately how a particularly nasty form of amyloid-β, called Aβ42, interact with the blood clotting agent fibrinogen, reason fibrinogen to raise into unusual clot structure that are hard to degrade.
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