Parkinson's disease (PD), a progressive neurological disorder, affects as many as 6 million people in the word, including about 1 million Americans. The disease often begins after age 50. Patients can develop muscle tremors, muscle rigidity and decreased mobility. The disease gradually strips away motor abilities, leaving people with a slow and awkward gait, rigid limbs, tremors, shuffling and a lack of balance. Its causes are not well-understood. Current treatments can only control the symptoms.
In PD people, a protein called α-synuclein is deposited in clumps known as Lewy bodies, which seem to contribute to the death of dopamine-producing brain cells. A newest study shows that an immunotherapy for cancer might also inhibit the progress of the second most common neurodegenerative disorder: Parkinson's disease (PD). The study was conducted by investigators at Johns Hopkins.
Earlier studies have indicated that α-synuclein clumps may spread from one cell to another. This transmission of pathologic α-synuclein into neurons is thought to drive PD pathogenesis. But how the protein clumps enter cells remains unknown. The new study uncovered that a transmembrane protein called LAG3 seemed to facilitate the spread of clumped α-synuclein.
Then the researchers injected α-synuclein aggregates to mice without the LAG3 gene, and found that mice without LAG3 were protected from PD. In contrast, typical mice exhibited PD-like symptoms, and lots of dopamine-producing neurons died. When the researchers used antibodies to inhibit LAG3, it protected cultured cells. Neurons treated with the LAG3 antibodies behaved similarly to the neurons that lacked LAG3. LAG3 function could be blocked by antibodies.
The data indicated that the LAG3 protein plays a role in transmitting α-synuclein aggregates from one brain cell to another, suggesting LAG3 as a possible target to slow the progression of PD. The study appears in the journal Science.
Study co-leader Dr Ted Dawson said that scientists are testing antibodies against LAG3 in clinical trials. The team is planning to continue testing LAG3 antibodies in mice and to further explore LAG3’s function.
Beth-Anne Sieber noted:“This study represents a significant advance in understanding the neurobiological changes underlying Parkinson’s disease.” CusAb offers Recombinant Mmel1 and other transmembrane proteins.
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