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| News Around World | ||||||
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| Developments
in fight against Parkinson's Disease
On the other side of the world, Andrea
Lozano, Senior Scientist at the Toronto Western Research Institute,
and his colleagues discovered the protein produced by a gene called
BAG5
inhibits parkin activity and
another protein, Hsp70 that works with parkin. Parkin is part of the
cell's "garbage disposal" system that rids the cell of unwanted
proteins by degrading them. In the brain, the parkin protein works
with Hsp70, which helps correct the folding of misfolded proteins.
Loss of such ability causes such protein garbage to aggregate into
lethal clumps in neurons - a hallmark of many neurodegenerative diseases.
Experiments on rats showed that BAG5 enhances the destruction of the
dopaminergic neurons targeted by Parkinson’s. Therefore, the
inhibition of this gene would reduce such destruction. The increase
of cell survival can be achieved by intervening the interaction between
BAG5 and parkin and Hsp70. “Based no our findings, we propose
a novel mechanism for neurodegeneration in which BAG5 interacts with
both parkin and Hsp70, resulting in decreased parkin and Hsp 70 fuction,
two outcomes that are deleterious to cell survival,” concluded
the researchers. They also added, “Given the role of BAG5 in
modulating ubi quitinylation, protein aggregation, and cell death,
it may serve as a useful therapeutic target for neurodegenerative
diseases such as PD.”
According to St. Jude Children’s Research Hospital, this breakthrough is significant in the development of vaccine towards this disease. Presently, the current pneumonia vaccines are mostly designed to protect adults against the sickness and do not work in young children. “The fact that we now know the structure of this important protein means we can begin to develop a vaccine that is more effective in children than those that are currently available,” said Richard W. Kriwacki, Ph.D., associate member of St. Jude Structural Biology. Streptococcus pneumonia bacteria uses a molecule that is shaped like a large paddle to latch onto cells lining the throat and lungs. This protein was determined by researchers from St. Jude Children’s Research Hospitals and called it CbpA, holds the key to developing a new vaccine. “Using CbpA as the key part of a new vaccine against S. pneumoniae would solve a problem that now hinders our ability to protect children from this infection,” said Elaine Tuomanen, M.D. St. Jude Children’s Research Hospital stated that the knowledge of the shape of CbpA will guide researchers in their efforts to use part or all of this protein as the basis of a vaccine against S. pneumoniae. The discovery of this crucial structure included studies on how this protein work in the body as well as the determination of its actual structure using laboratory tools. The technology involved with the discovery of the protein’s structure was Nuclear Magnetic Resonance (NMR) spectroscopy and circular dishroism (CD). Another research laboratory specialist in Tuomanen’s lab confirmed that a bacteria carrying a mutated CbpA could not infect the human body. These discoveries proved that we are indeed closer to a vaccine than we were before. |
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