Approved by the FDA earlier this year, the Alzheimer's therapy lecanemab is an antibody that reduces the buildup in the brain of a sticky peptide called amyloid-beta (Aβ), which is thought to be a main driver of the disease. Dispensed in bimonthly infusions, lecanemab specifically targets protofibrils, the type of Aβ clumps thought to be the most neurotoxic. Studies have shown that lecanemab slows cognitive and functional decline in early-stage Alzheimer's patients.
But as with many other cutting-edge therapies, we know more about lecanemab's effectiveness than we do about how it actually works. A new study published inby researchers from The Rockefeller University identifies one possible means for its impact on patients.
Lecanemab, however, causes ARIA in only 10% of patients. Intrigued by this low number, the Rockefeller team had two questions: why is it effective, and why does it cause so much less ARIA?The researchers knew where they wanted to look: at the specific type of Aβ clumps lecanemab targets, known as protofibrils.
Protofibrils have just the right amount of real estate for two plasma proteins, coagulation factor XII and high molecular weight kininogen , to bind near each other on their surfaces. When that happens, HK is cleaved, producing a peptide called bradykinin that dilates blood vessels. Bradykinin has a variety of purposes in the body, and it can be especially useful for lowering blood pressure.
"If you block the contact system, you're going to get less Alzheimer's pathology," says co-senior author Sidney Strickland, Rockefeller's Zachary and Elizabeth M. Fisher Professor in Alzheimer's and Neurodegenerative Disease.
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