May 022012

May 2, 2012:  Karen Duff, researcher, Columbia University Medical Center (CUMC), 212 305 8790.  I left a message on Karen’s phone:  “But what causes the “malfunctioning protein?” There is a file/pile of information on the link between alzheimer’s and mercury poisoning from slow off-gasing of mercury from dental fillings over decades. I left my phone number and web address.

The article below is from Bloomberg’s.  The link is no longer valid.  There are numerous news reports on this research.  Copy and paste the title into google to find them.

As far as I know, Karen Duff did not reply to my message.

New clues unearthed on how Alzheimer’s spreads through the brain


Alzheimer’s appears to spread through the brain like poison in a river, according to a study that’s the first to track the destruction caused by an abnormal protein implicated in tile disease.

Researchers created genetically engineered mice with abnormal tau protein in the brain’s entorhinal cortex, the first place the substance shows up in people with Alzheimer’s disease, according to a paper in the journal PLoS One. From there, they mapped the mouse brains over 22 months as the tau spread across neurons within the organ to other regions governing memory, reasoning and other functions.

Tau is one of two abnormal proteins tied to Alzheimer’s. The one more closely associated is beta amyloid, which can be detected using imaging tools. While high levels of beta amyloid can predict risk, the amount of tau found after death correlates more closely with dementia, said Karen Duff, the lead researcher.

A new study suggests that Alzheimer’s disease spreads from cell to cell inside the brain through a malfunctioning protein called tau.

Beta amyloid plaque I TAU PROTEINS normally stabilize the scaffoldlike microtubules that carry messages within a healthy neuron, But in some cases, tau detaches and forms tangled clumps, disrupting the microtubules and eventually killing the cell.

SOME PREVIOUS ATTEMPTS  to halt the spread of Alzheimer’s focused on another protein called beta amyloid, which forms plaques in the early stages of the disease, The new findings should allow researchers to test methods for blocking tau.  Knowing the path tau takes in the brain may one day improve treatment, she said. “There may be an intervention point that might prevent dementia”  if scientists can figure out how to stop the tau from spreading, said Dr. Duff, who is a professor of pathology at Columbia University Medical Center in New York.

The place where abnormal tau shows up earliest isn’t associated with dementia at a1l, she said.   Tau also is involved in other kinds of dementia, including frontotemporal lobe dementia, Parkinson’s disease and Lewy body disorder, Dr, Duff said. The spread is probably similar even if the abnormal protein arises somewhere else in the brain.

It’s not clear from the research how tau and amyloid interact, a question Dr. Duff said she wants to study further. When tau is normal, it supplies nutrients to QiIVe cells in the brain. When .if is damaged, it becomes tangled and shuts off nutrients, causing the death of brain cells.

Beta amyloid is known to play a role in Alzheimer’s in part because genes that confer higher risks of the illness have to do with amyloid, Duff said. The new research suggests that it somehow interacts with the tau that ultimately kills the cells.  “There’s some interaction, and it seems amyloid has its detrimental effects through tau,” Dr, Duff said. “There’s an interaction at a fundamental level we don’t understand yet” Closer study of the mouse model, as well as imaging tools that would allow scientists to see tau accumulate in living humans’ brains, would be helpful, she said.

The mice may also prove useful for testing interventions to prevent the spread of the abnormal clumps of protein, she said. “Mostly we wanted to mimic the early stages of Alzheimer’s, because that could best give us some idea of where we could target therapeutically,” Dr. Duff said. “And if we layer on an amyloid model, we may also be able to see interactions.”

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