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posted by cmn32480 on Saturday October 01 2016, @07:14AM   Printer-friendly
from the watch-out-for-the-toll-booth dept.

Researchers at Johns Hopkins report they have identified a protein that enables a toxic natural aggregate to spread from cell to cell in a mammal's brain -- and a way to block that protein's action. Their study in mice and cultured cells suggests that an immunotherapy already in clinical trials as a cancer therapy should also be tested as a way to slow the progress of Parkinson's disease, the researchers say.

A report on the study appears Sept. 30 in the journal Science.

Ted Dawson, M.D., Ph.D., director of the Institute for Cell Engineering at the Johns Hopkins University School of Medicine and one of the study's leaders, says the new findings hinge on how aggregates of α-synuclein protein enter brain cells. Abnormal clumps of α-synuclein protein are often found in autopsies of people with Parkinson's disease and are thought to cause the death of dopamine-producing brain cells.

The scientists genetically engineered mice to lack a key transmembrane receptor, LAG3, that attracts the protein aggregates responsible for Parkinson's. The mice proved immune. Antibodies that targeted LAG3 also shielded subjects from the aggregates.

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3 (DOI: 10.1126/science.aah3374) (DX)

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  • (Score: 3, Funny) by Anonymous Coward on Saturday October 01 2016, @08:22AM

    by Anonymous Coward on Saturday October 01 2016, @08:22AM (#408682)

    If only your dad had been a sad wanker like you.

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  • (Score: 2) by deimtee on Saturday October 01 2016, @03:20PM

    by deimtee (3272) on Saturday October 01 2016, @03:20PM (#408796) Journal

    That seems a bit harsh. Why do you want him to be sad?

    No problem is insoluble, but at Ksp = 2.943×10−25 Mercury Sulphide comes close.