August 21, 2010
The Fisher Center for Alzheimer’s Research Foundation funds scientists who continue to be at the forefront of research into the understanding of beta amyloid, a protein that is at the root of Alzheimer’s disease. Beta amyloid forms dense protein deposits called plaques. Sometimes compared to tiny scouring pads, these beta amyloid plaques accumulate in the spaces between brain cells, choking them off and causing them to die Fisher Center scientists were among the first to define the specific steps by which beta amyloid is produced, and their discovery that pharmacological substances can interrupt this process set off a worldwide race to develop drugs to inhibit beta amyloid buildup.
The Foundation’s beta amyloid research is now focused on a protein called amyloid precursor protein (APP). When broken down in a certain way, APP results in the formation of beta amyloid plaque. Fisher scientists are unraveling the process by which APP processing is regulated. Their immediate goal is to develop ways to slow the accumulation of plaque and other forms of beta amyloid in the brain and reduce their toxic effects on nerve cells, moving much closer to a cure for Alzheimer’s disease. In fact, Fisher Center Foundation scientists are making significant progress in developing therapies aimed at reducing the production of toxic beta-amyloid, an achievement that will ultimately prevent, slow or even cure the disease. Fisher scientists recently identified several proteins that regulate the amount of beta-amyloid produced in the brain. What’s new is that these “regulator” proteins exert control over one or both of the enzymes that are known to produce beta-amyloid directly. Discovery of this “molecular fine-tuning” mean that Fisher scientists can now search for, or design, new drugs for treating Alzheimer’s.
Fisher scientists have also recently discovered how beta-amyloid damages communication between brain cells and how fibers connecting brain cells can be grown or made to shrink. With this understanding, it may be possible to devise therapies that protect the brain even when beta-amyloid production goes awry.