Excess of Peptides Linked to Alzheimer's Disease

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While previous research has tied Golgi fragmentation to Alzheimer's disease (AD), an excess of Abeta peptides are behind the mechanism, according to a study published on the Proceedings of the National Academy of Sciences' website. The study also provided methods to rescue damaged cells.

While previous research has tied Golgi fragmentation to Alzheimer’s disease (AD), an excess of Abeta peptides are behind the mechanism, according to a study published on the Proceedings of the National Academy of Sciences’ website. The study also provided methods to rescue damaged cells.

Yanzhuang Wang, PhD, and associates at the University of Michigan discovered that Golgi degradation is caused by “phosphorylation of Golgi structural proteins, such as GRASP65, which is induced by Aβ-triggered cyclin-dependent kinase-5 activation,” according to a statement from the University of Michigan, which leads to AD. A surplus of Abeta peptides creates a plaque and kills cells in Alzheimer’s patients.

Golgi cells are responsible for sending molecules to create new cells. When the Golgi becomes damaged, they either incorrectly send molecules or stop carrying out functions completely, Wang, the leader of the study study, said in the statement. He related the Golgi structure to a post office — when it is not functioning, packages get sent to wrong areas of the brain or not sent at all.

To “rescue” damaged Golgi cells, investigators also suggested the “inhibition of cyclin-dependent kinase-5 and expression of nonphosphorylatable GRASP65 mutants,” which decreased Aβ creation by 80%.

By highlighting the Golgi’s and Abeta peptide’s role in AD, researchers believe their findings provide insight for AD drug manufacturers. Though their research provided measures that would prevent further damage, Wang said the next step is to research methods that would reverse the overall harm done to the Golgi in mice models.

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