Animal experiments similar to the treatment of human Alzheimer's disease have shown that the treated antibodies may actually be harmful. It has been discovered that the antibodies being tested in humans destroy the sticky plaques that form in the brain. In a mouse model of Alzheimer's disease, the antibody seems to activate more brain cells and eventually stop functioning.
"We believe this may be the failure mechanism of these antibodies in human tests," said Mark Bush of the Technical University of Munich, Germany.
Busche and his colleagues administered the same antibody drugs to Alzheimer's disease model mice and normal mice. After treatment, they found that the active brain cells of the diseased mice were five times that of the normal mice.
Alzheimer's disease collects fragments called β-amyloid. Busche et al. previously found that β-amyloid protein can cause the body to become overactive. They believe that when antibodies destroy these plaques, their effectiveness is more useless than when the plaques are intact.
After many failures in attempts to treat Alzheimer's disease, drug developers started to detect and treat the disease early. Therefore, Bush and his team studied the role of the drug in the early stages of Alzheimer's disease in these mice. At this time, there are no plaques in the brain, neurons become more active, and the disease worsens. symptom.
mice may mislead us "Even before the plaque deposits, very young mice have been found to be active. It is not yet clear what causes hyperactivity. But you don't have to throw away these drugs. Other researchers have carefully pointed out that mouse experiments are misleading. The history of sexual results. "The mouse model is incomplete. Maria Carrillo, chief scientific officer of our American charity Al Zheimer's Association, said: "We have been exposed to animal Alzheimer's for many years.
Busche agreed that the mouse model cannot simulate all aspects of human disease. "Targeted therapies for beta amyloid symptoms are still promising, but eventually more may be needed.