The team led by Gabor Kovacs said they are now able to show how, with the use of a specially-developed antibody, spreading of the disease occurs in the human brain...

The focus ...on the protein Alpha-synuclein that is abundant in the human brain. In patients with Parkinson's disease ... the protein appears in a pathologically-altered state.

The study showed how human nerve cells absorbed the pathologically-altered form of the protein and how it was thus transmitted from one cell to the next...

Kovacs said blocking the spreading mechanism of the Alpha-synuclein protein could now be targeted as a means of therapy for patients, and additionally the antibody could be used to aid in making diagnoses of both Parkinson's disease and Lewy body dementia.

The announcement from the team supports similar claims from Munich-based neuropathologist Armin Giese, who reported similar behaviour with Alzheimer's disease, on Tuesday last week.

http://news.xinhuanet.com/english/he..._133663718.htm

I would think another option would be to find out why/what causes the alphasynuclein to "pathologically morph" in the first place. How is it different from the alphasyn in people without PD? At what point does it begin to morph? There are a lot of questions that could be asked that might get to the actual heart of the matter, in addition to trying to stop it from spreading once it has already morphed.

There are several reasons. Mutations in alpha syn and over expression of the gene. Chemical insults to the protein, inflammation and aggregation of protein s trands are a few that cause alpha-syn to morph.

Curcumin is supposed stop this morphing atleast in vitro.

Read today of Spanish research into alpha-syn, very interesting, about mechanism for passing on protein changes is reproducible using alpha-syn human cells with lab animal subjects. Promptly lost the link but sure it came from other pd associates.

Girija, thought of you immediately, and that the paper seemed the closest to finding a cause we have seen yet. It was called something like mechanism for PD found.

Another paper in the same area:

"α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration"
Hien T. Tran, Charlotte Hiu-Yan Chung, Michiyo Iba, Bin Zhang, John Q. Trojanowski, Kelvin C. Luk, Virginia M.Y. Lee
Cell, 26 June, 2014
http://www.cell.com/cell-reports/ful...247(14)00427-6

"Misfolded and aggregated disease-specific proteins such as α-syn in Parkinson’s disease (PD) and Aβ and tau in Alzheimer’s disease (AD) are common features of many neurodegenerative diseases (NDs). Self-amplification, propagation, and transmission of these misfolded proteins are hypothesized as major contributing factors to disease onset and progression."

Working with mice, they showed that:
"α-syn immunotherapy using Syn303 reduced pathologic spread of α-syn aggregates in vivo, ameliorated motor dysfunction mediated by LB pathology, and rescued TH cell loss."

John

I was at the Neurological Institute at Columbia University this past spring and saw Virginia Lee give a presentation on the results of this research study and some others they are doing at U of Penn. Truly fascinating. What I found of real interest though, and which was only briefly mentioned in the report, was the morphing of a-syn into different strains. Lee's team found that misformed tau interacted with morphed a-syn to form a totally different morphed strain. Each of the two strains caused different PD symptoms (in rodents, of cause). It was hypothesized that this could be one of the causes of the different variants we see in PD in humans. Also of interest, only the morhed a-syn developed into different strains, the morphed tau proteins remained the same.

Certainly something to speculate about and research more.

Gary