Hallmark Pathology of Alzheimers Disease can be Halted by chaperone Protein

Role of Chaperone Protein

However, the present study showed that these proteins prevent various neurodegeneration-associated proteins, such as beta-amyloid and alpha-synuclein from misfolding, tangling, and forming extracellular plaques and intracellular inclusions.

Alzheimer’s disease (AD) is a neurodegenerative disease that leads to gradual memory loss and behavioral changes. It is characterized by the formation of tau tangles and beta-amyloid plaques in the brain tissues, years before the actual symptoms occur.

Similarly in Parkinson’s disease (neurodegenerative and movement disorder), the intracellular inclusions of alpha-synuclein are observed in the brains of affected patients.

“We solve a decades-long puzzle by showing this group of proteins actually constitute a major protein quality control system in cells and a never-before-seen enabler of proper folding of various proteins — including misfolding-prone proteins associated with various diseases. Keep that family of proteins functioning properly, and the tangling of rogue proteins may be diminished or stopped altogether,” says senior author Xiaolu Yang, Ph.D., a professor of Cancer Biology in the Perelman School of Medicine at the University of Pennsylvania.

The study thereby may help in formulating new targeted approaches that would help in restoring a biological system designed to keep key proteins in check and prevent diseases.

Source: Medindia