Babies Are Born with Alzheimer's-Linked Proteins in Their Brains. Scientists Want to Know Why

"Alzheimer's disease is characterized by certain key changes in the brain. Among them are the development of two kinds of protein deposits: clumps made up of amyloid beta and tangles of tau. These changes can be identified in a few ways. Medical professionals and scientists can see the extent of these protein deposits in the brain using sophisticated and expensive neuroimaging."

"A newly approved test measures levels of amyloid beta and pTau217, an altered version of tau that is one of the markers of Alzheimer's disease, in a blood sample. From the time this particular marker was identified, researchers realized it could help detect preclinical Alzheimer's disease, that is, the presence of amyloid beta brain pathology prior to any symptoms. But in a twist, scientists are finding this protein marker of neurodegeneration in unexpected places."

"A new study in the journal Brain Communications reports that pTau217 is elevated among healthy newborns. In fact, these infants had higher levels than people with Alzheimer's disease. This discoveryindicates that the protein changes that characterize this devastating disorder are reversible in certain circumstanceshinting at new possibilities for treatment. Normal tau protein is involved in binding and stabilizing the network of proteins that give a neuron its structure."

Alzheimer's disease involves amyloid beta clumps and tau tangles that alter brain structure. Detection methods include costly neuroimaging and cerebrospinal fluid assays obtained via lumbar puncture. A blood test measuring amyloid beta and pTau217 enables less invasive detection and can identify preclinical amyloid pathology before symptoms. A study found pTau217 levels elevated in healthy newborns, exceeding levels seen in some people with Alzheimer's disease, implying that tau-related protein changes can occur outside of neurodegeneration and may be reversible under certain conditions. Normal tau helps bind and stabilize neuronal structural proteins.

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