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- Tau Protein Corruption -


General Information:

Names:
Wikipedia entry:
Dr. Ray Shahelien entry: 

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Observations:

Tau Protein Corruption

See also Tau Busters

Acetylation:

Interfering with tau protein "acetylation" may be a new approach for reducing tau-related pathology.

Great.  How?
Acetylation May Contribute to Dementia and Alzheimer's Disease; May Lead to New Treatments
ScienceDaily (Sep. 22, 2010)
A new study uncovers a protein modification that may contribute to the formation of neuron-damaging neurofibrillary tangles in the human brain. The research, published by Cell Press in the Sept. 23 issue of the journal Neuron, may lead to new strategies for treatment of neurodegenerative diseases that result from pathological aggregation of tau protein... While the link between tau acetylation and tau phosphorylation is not known, the results provide new insight into tau-mediated neuropathology. "Our findings support the model that the abnormally elevated acetylation at an early stage of the disease could block clearance of p-tau from neurons, leading to its accumulation. Our observation that p300 diminished tau acetylation and effectively eliminated p-tau supports the idea that interfering with tau acetylation may be a new approach for reducing tau-related pathology."
http://www.sciencedaily.com/releases/2010/09/100922121939.htm
Breakthrough Untangles One Key to Alzheimer’s Disease
By Rachael Rettner, MyHealth
NewsDaily Staff Writer
Sep 22, 2010 | 12:01 PM ET |

Scientists may have found a new way to reduce levels of a toxic protein that accumulates in the brains of Alzheimer's patients. The approach may one day lead to new therapies for the condition.

In patients with certain neurodegenerative diseases, including Alzheimer's, a protein called tau forms stringy blobs known as "tangles" inside brain cells. These tangles, along with brain plaques, are thought to contribute to the development of the disease.

Normally, tau proteins help maintain the cell's structure. But in Alzheimer's patients, they've become toxic because they've undergone a certain kind of chemical change, called phosphorylation. Brain cells should recognize that these changed tau proteins are damaged, and should destroy them. But this destruction doesn't happen, and scientists have not understood why.

Li Gan, a researcher at the Gladstone Institute of Neurological Disease in San Francisco, and her colleagues wondered whether these damaged tau proteins might be modified in some other way that prevents the cells from demolishing them.

They discovered a second chemical change that the toxic tau proteins have undergone, called acetylation, which makes them destruction-proof. In both mice with Alzheimer's and humans with Alzheimer's, levels of this destruction-proof tau protein were elevated at early and middle stages of the disease — before the tangles appeared.

And when they blocked the second change, levels of the damaging proteins in the cells were greatly diminished.

"We can actually make the cell more efficient," in getting rid of the damaged tau proteins, Gan told MyHealthNewsDaily.

The molecule the researchers used to block the second change might one day serve as a new class of anti-Alzheimer's disease drugs, Dr. Lennart Mucke, GIND director, said in a statement.

The researchers said the second change might work by preventing the toxic tau protein from being "tagged" for demolition by the cell.

The study will be published tomorrow (Sept. 23) in the journal Neuron.
http://myhealthnewsdaily.com/alzheimers-disease-tangles-tau-protein-100922-0418/

There are several substances (sometimes called "tau busters") that might help with tau protein corruption. Here they are in the order I found out about them:

1.  Cinnamon Proanthocyanidins
2.  Methylene Blue (Rember)
3.  Niacinamide (Nicotinamide)
4.  Grape Seed Extract
5.  Davunetide
6.  Nypta
7.  Valproic Acid (VPA, Depakote)
8.  Metformin
9.  Epothilone D

The question is, is tau protein corruption a step in the disease process, or merely just another symptom?

The shape of the tau protein aggregations in CBD and PSP is described as "clumps", whereas it is described as "tangles" in AD. Therefore, the cause of the corruption is probably quite different. One known cause of tau protein clumping is exposure to a simple sugar called D-ribose. D-ribose is one of the building blocks used by a cell to produce ATP. ATP is "adenosine triphosphate". You can think of ATP like the electricity in a Diesel-electric locomotive. The wheels of the locomotive are driven by electric motors. The Diesel oil only powers the generator engines. In a cell, glucose or ketones power the mitochondria. The mitochondria manufacture ATP, which is then used to power the functions of the cell. If the mitochondria can't quite finish the job of making ATP, it is possible that excess D-ribose hangs around unused. When proteins molecules come in contact with sugars, they often undergo a transformation of shape called "glycation". In the case of D-ribose, this has been referred to as "ribosylation". So it may be that the cause of the tau corruption is mitochondrial dysfunction. If this dysfunction is related to the production of ATP, the neurons are basically starving to death. Clearing the tau protein aggregates may impact the current status of the disease, but neurons would ultimately be doomed due to lack of energy. (Note: D-ribose may also be produced by other cells or supplied in food.)

What can be done about this? There are several ideas being investigated for addressing the mitochondrial dysfunction problem. I posted some information about this back in May:

"An interesting list of possible disease modifying agents"
http://health.groups.yahoo.com/group/pspinformation/message/14161

Substance: Coenzyme Q10
Target: Mitochondrial dysfunction
Mechanism: Complex I cofactor
Phase II trial: Significant improvement (Stamelou et al, 2008)
Phase III trial: Recruiting (NCT00382824 on clinicaltrials.gov)

Substance: Pyruvate, Creatine, Niacinamide
Target: Mitochondrial dysfunction
Mechanism: Multifunctional cocktail
Phase I trial: Active (NCT00605930 on clinicaltrials.gov)

Substance: Lithium
Target: Tau dysfunction
Mechanism: GSK-3beta inhibitors
Phase I trial: Stopped because of poor tolerability (NCT00703677 on
clinicaltrials.gov)

Substance: Valproic Acid
Target: Tau dysfunction
Mechanism: Aggregation inhibitors
Phase II trial: Active (NCT00385710 on clinicaltrials.gov)

Substance: Nypta
Target: Tau dysfunction
Mechanism: Microtubule stabilizers
Phase II trial: Recruiting (NCT01049399 on clinicaltrials.gov)

Substance: Methylthioninium Chloride (Methylene Blue)
Target: Tau dysfunction
Mechanism: Microtubule stabilizers
Phase II trial: Significant improvement in Alzheimer's disease
[This is a form of methylene blue. See also info on Rember.]

Substance: Davunetide
Target: Tau dysfunction
Mechanism: Microtubule stabilizers
Phase II trial: PSP study in preparation

Low dose of methylene blue may improve mitochondrial function. Look it up.

If the mitochondria are having a problem metabolizing glucose (into ATP), they may still be able to use ketones to finish the job. This is where the idea of a "ketogenic diet" comes into play. The body will produce ketones in the process of converting stored fat reserves into energy for survival. It will also do this when "medium chain triglycerides" are in the diet.

If you want to know more about these things, look them up. Google is a great resource.

Here is the paper on "ribosylation":
D-Ribosylated Tau forms globular aggregates with high cytotoxicity.
Chen L, Wei Y, Wang X, He R.
State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, 100101 Beijing, China.
Cell Mol Life Sci. 2009 Aug;66(15):2559-71. Epub 2009 Jun 11.

Although the glycation of Tau that is involved in paired helical filament formation in Alzheimer's disease has been widely studied, little attention has been paid to the role of D-ribose in the glycation of Tau. Here, we show that Tau is rapidly glycated in the presence of D-ribose, resulting in oligomerization and polymerization. Glycated derivatives appeared after 24 h incubation. Western blotting indicated the formation of advanced glycation end-products (AGEs) during initial stages of glycation. Thioflavin T-positive (ThT-positive) aggregations that appeared from day 4 indicated the globular-like features. Atomic force microscopy revealed that the surface morphology of ribosylated Tau40 was globular-like. Kinetic studies suggested that D-ribosylated Tau is slowly oligomerized and rapidly polymerized with ThT-positive features. Moreover, D-ribosylated Tau aggregates were highly toxic to SHSY5Y cells and resulted in both apoptosis and necrosis. This work has demonstrated that D-ribose reacted with Tau protein rapidly, producing ThT-positive aggregations which had high cytotoxicity.
PMID: 19517062
http://www.ncbi.nlm.nih.gov/pubmed/19517062?ordinalpos=1&itool=PPMCLayout.PPMCAppController.PPMCArticlePage.PPMCPubmedRA&linkpos=1
Dynamics of Chaperone Protein Critical in Rescuing Brains of Alzheimer's Mice from Neuron Damage
ScienceDaily (Dec. 3, 2010) — Dynamic regulation of the chaperone protein Hsp27 was required to get rid of abnormally accumulating tau in the brains of mice genetically modified to develop the memory-choking tau tangles associated with Alzheimer's disease, a University of South Florida-led study found...
http://www.sciencedaily.com/releases/2010/12/101203091449.htm


Alzheimer's: Tau Disrupts Neural Communication Prior to Neurodegeneration
ScienceDaily (Dec. 24, 2010) — A new study is unraveling the earliest events associated with neurodegenerative diseases characterized by abnormal accumulation of tau protein. The research, published in the December 22 issue of the journal Neuron, reveals how tau disrupts neuronal communication at synapses and may help to guide development of therapeutic strategies that precede irreversible neuronal degeneration...
http://www.sciencedaily.com/releases/2010/12/101222121500.htm

Tau-Induced Memory Loss in Alzheimer’s Mice Is Reversible; Study Raises Hopes for the Development of Effective Therapies
ScienceDaily (Feb. 17, 2011) —  ...However, it appears that the toxic effect of tau protein is largely eliminated when the corresponding tau gene is switched off. Researchers from the Max Planck Research Unit for Structural Molecular Biology at DESY in Hamburg have succeeded in demonstrating that once the gene is deactivated, mice with a human tau gene, which previously presented symptoms of dementia, regain their ability to learn and remember, and that the synapses of the mice also reappear in part... Whereas aggregated amyloid-beta protein forms insoluble clumps between the neurons, the tau protein accumulates inside them. Tau protein stabilises the tube-shaped fibers of the cytoskeleton, known as microtubules, which provide the "rails" for cellular transport. In Alzheimer disease, excess phosphate groups cause the tau protein to malfunction and form clumps (the 'neurofibrillary tangles'). As a result, nutrient transport breaks down and the neurons and their synapses die off. This process is accompanied by the initial stage of memory loss... The scientists concluded from this that mutated or pathological tau can alter healthy tau...
http://www.sciencedaily.com/releases/2011/02/110216083119.htm

Increasing Brain Enzyme May Slow Alzheimer's Disease Progression; Study Finds Damaging Accumulation of Tau Proteins Removed
ScienceDaily (Feb. 16, 2011) — ..."Our research demonstrated that increasing the brain enzyme known as PSA/NPEPPS can effectively block the accumulation of tau protein that is toxic to nerve cells and slow down the progression of neural degeneration without unwanted side effects," said Stanislav L. Karsten, PhD, the corresponding author for the study and a principal investigator at Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center (LA BioMed). "These findings suggest that increasing this naturally occurring brain peptidase, PSA/NPEPPS, may be a feasible therapeutic approach to eliminate the accumulation of unwanted toxic proteins, such as tau, that cause the neural degeneration associated with the devastating effects of Alzheimer's disease and other forms of dementia."...
http://www.sciencedaily.com/releases/2011/02/110216110538.htm

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Known sources:


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Natural sources:

None known.

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References:

Tau, not amyloid-beta, triggers neuronal death process in Alzheimer's
Date: November 1, 2014
Source: Georgetown University Medical Center
Summary: New research points to tau, not amyloid-beta plaque, as the seminal event that spurs neuron death in disorders such as Alzheimer's disease. The finding, which dramatically alters the prevailing theory of Alzheimer's development, also explains why some people with plaque build-up in their brains don't have dementia.
http://www.sciencedaily.com/releases/2014/11/141101173217.htm

Researcher Debunks Alzheimer's Prevailing Development Theory
October 31, 2014 – New research that dramatically alters the prevailing theory of how Alzheimer’s disease develops has been published online today by Georgetown researchers in the journal Molecular Neurodegeneration….  Charbel E-H Moussa, MB, PhD, of Georgetown University Medical Center… nilotinib, a drug approved to treat cancer, as a therapeutic approach in neurodegenerative diseases.
http://gumc.georgetown.edu/news/Researcher-Debunks-Alzheimers-Prevailing-Development-Theory

Tau protein, not plaque, may cause Alzheimer’s, study says
By  Nicole Kwan
Published October 31, 2014
FoxNews.com
“For a very long time, we believed, for almost 100 years, that [amyloid-beta] plaques are the main culprit in Alzheimer’s disease,” the study's senior investigator, Charbel E-H Moussa, MB, assistant professor of neuroscience at Georgetown University Medical Center, told FoxNews.com. “This study shows it’s another protein -- a very, very important one, called tau, is basically the main guilty one.”
http://www.foxnews.com/health/2014/10/31/tau-protein-not-plaque-may-cause-alzheimers-study-says/?intcmp=ob_homepage_health&intcmp=obnetwork

Post-Anesthesia Dementia, Like Alzheimer's, Looks Micro-'Tubular'
ScienceDaily (June 27, 2012)
http://www.sciencedaily.com/releases/2012/06/120627091617.htm

Computational Predictions of Volatile Anesthetic Interactions with the Microtubule Cytoskeleton: Implications for Side Effects of General Anesthesia.
Craddock TJA, St. George M, Freedman H, Barakat KH, Damaraju S, et al.
PLoS ONE, 2012 DOI:
Computational Predictions of Volatile Anesthetic Interactions with the Microtubule Cytoskeleton: Implications for Side Effects of General Anesthesia
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0037251

PubMed search on Craddock:
http://www.ncbi.nlm.nih.gov/pubmed?term=Travis%20J.%20A.%20Craddock

1. The zinc dyshomeostasis hypothesis of Alzheimer's disease.
Craddock TJ, Tuszynski JA, Chopra D, Casey N, Goldstein LE, Hameroff SR, Tanzi RE.
PLoS One. 2012;7(3):e33552. Epub 2012 Mar 23. Erratum in: PLoS One. 2012;7(4): doi/10.1371/annotation/57c710a6-83ba-444c-a352-b9f60125f2fa.
PMID: 22457776 [PubMed] Free PMC Article
http://www.ncbi.nlm.nih.gov/pubmed/22457776

2.  Cytoskeletal signaling: is memory encoded in microtubule lattices by CaMKII phosphorylation?
Craddock TJ, Tuszynski JA, Hameroff S.
PLoS Comput Biol. 2012;8(3):e1002421. Epub 2012 Mar 8.
PMID: 22412364 [PubMed] Free PMC Article
http://www.ncbi.nlm.nih.gov/pubmed/22412364

3. An investigation of the plausibility of stochastic resonance in tubulin dimers.
Saha AA, Craddock TJ, Tuszynski JA.
Biosystems. 2012 Feb;107(2):81-7. Epub 2011 Oct 7.
PMID: 22001523 [PubMed]
http://www.ncbi.nlm.nih.gov/pubmed/22001523

4.  "Memory bytes" - molecular match for CaMKII phosphorylation encoding of microtubule lattices.
Hameroff SR, Craddock TJ, Tuszynski JA.
J Integr Neurosci. 2010 Sep;9(3):253-67.
PMID: 21064217 [PubMed]
http://www.ncbi.nlm.nih.gov/pubmed/21064217

5.  Microtubule ionic conduction and its implications for higher cognitive functions.
Craddock TJ, Tuszynski JA, Priel A, Freedman H.
J Integr Neurosci. 2010 Jun;9(2):103-22. Review.
PMID: 20589950 [PubMed]
http://www.ncbi.nlm.nih.gov/pubmed/20589950

 Link Between Brain Insulin Resistance, Neuronal Stress in Worsening Alzheimer's Disease
ScienceDaily (June 26, 2012) — Rhode Island Hospital researcher Suzanne de la Monte, M.D., has found a link between brain insulin resistance (diabetes) and two other key mediators of neuronal injury that help Alzheimer's disease (AD) to propagate. The research found that once AD is established, therapeutic efforts must also work to reduce toxin production in the brain…
http://www.sciencedaily.com/releases/2012/06/120626115249.htm

Dysfunctional Pro-Ceramide, ER Stress, and Insulin/IGF Signaling Networks with Progression of Alzheimer’s Disease.
Suzanne M. de la Monte, Edward Re, Lisa Longato, Ming Tong.
Journal of Alzheimer's Disease, June 22, 2012, supplement; DOI: 10.3233/JAD-2012-111728
http://iospress.metapress.com/content/k50184847w75/

Dysfunctional Pro-Ceramide, ER Stress, and Insulin/IGF Signaling Networks with Progression of Alzheimer's Disease.
de la Monte SM, Re E, Longato L, Tong M.
J Alzheimers Dis. 2012 Jan 1;30(0):S217-29.
Source: Departments of Pathology (Neuropathology), Neurology, and Medicine, Rhode Island Hospital and The Warren Alpert Medical School of Brown University, Providence, RI, USA.
Abstract
In Alzheimer's disease (AD), brain insulin and insulin-like growth factor (IGF) resistance and deficiency begin early, and worsen with severity of disease. The factors mediating progression of brain insulin/IGF resistance in AD are not well understood. We hypothesize that AD progression is mediated via negative cross-talk that promotes toxic ceramide generation and endoplasmic reticulum (ER) stress. The rationale is that insulin resistance dysregulates lipid metabolism and promotes ceramide accumulation, and thereby increases inflammation and stress. Consequences include disruption of cytoskeletal function and AβPP-Aβ secretion. The present study correlates AD stage with activation of pro-ceramide genes, ceramide levels, and molecular indices of ER stress in postmortem human brain tissue. The results demonstrated that in AD, brain insulin/IGF resistance was associated with constitutive activation of multiple pro-ceramide genes, increased ceramide levels, and increased expression of pro-ER stress pathway genes and proteins. Expression of several pro-ceramide and pro-apoptotic ER stress pathway molecules increased with AD severity and brain insulin/IGF resistance. In contrast, ER stress molecules that help maintain homeostasis with respect to unfolded protein responses were mainly upregulated in the intermediate rather than late stage of AD. These findings support our hypothesis that in AD, a triangulated mal-signaling network initiated by brain insulin/IGF resistance is propagated by the dysregulation of ceramide and ER stress homeostasis, which themselves promote insulin resistance. Therefore, once established, this reverberating loop must be targeted using multi-pronged approaches to disrupt the AD neurodegeneration cascade.
PMID: 22297646 [PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22297646

[A prion-like disease???  There is a LOT in this, and keeping it all straight will be difficult.  How does “neurospirochetosis” fit in?  How does coffee consumption fit in?]

Alzheimer's Spread Through the Brain Mapped: Infects from Neuron to Neuron
ScienceDaily (June 26, 2012)
The illness starts in the entorhinal cortex -- a part of the cerebral cortex, and then spreads to the hippocampus. Both of these areas are important for memory. Gradually, pathological changes take place in more and more areas of the brain, while the patient becomes even sicker…
…smaller groups of beta amyloid -- called oligomeres -- seem to be the toxic form that gradually destroy the neurons and shrink the brain…
http://www.sciencedaily.com/releases/2012/06/120626172728.htm

Spreading of neurodegenerative pathology via neuron-to-neuron transmission of beta-amyloid.
Sangeeta Nath, Lotta Agholme, Firoz Kurudenkandy, Björn Granseth, Jan Marcusson and Martin Hallbeck.
Journal of Neuroscience, June 27, 2012
http://www.liu.se/forskning/forskningsnyheter/1.352091?l=en

Screen Finds an Antidepressant and Other Drugs That Might Work Against Brain-Wasting Prion Diseases
ScienceDaily (Sep. 14, 2011)
…styryl-based compounds… two that seemed both effective and non-toxic… Dr. Wisniewski's team found similar results the antidepressant trimipramine and the anti-schizophrenia drug fluphenazine…
http://www.sciencedaily.com/releases/2011/09/110914115850.htm

Styryl-Based and Tricyclic Compounds as Potential Anti-Prion Agents.
Erika Chung, Frances Prelli, Stephen Dealler, Woo Sirl Lee, Young-Tae Chang, Thomas Wisniewski.
PLoS ONE, 2011; 6 (9): e24844 DOI: 10.1371/journal.pone.0024844
http://www.eurekalert.org/pub_releases/2011-09/nlmc-sfa_1091411.php

Prions in the Brain Eliminated by Homing Molecules
ScienceDaily (Apr. 24, 2012)
http://www.sciencedaily.com/releases/2012/04/120424095704.htm

Polythiophenes inhibit prion propagation by stabilizing PrP aggregates.
I. Margalith, C. Suter, B. Ballmer, P. Schwarz, C. Tiberi, T. Sonati, J. Falsig, S. Nystrom, P. Hammarstrom, A. Aslund, K. P. R. Nilsson, A. Yam, E. Whitters, S. Hornemann, A. Aguzzi.
Journal of Biological Chemistry, 2012; DOI: 10.1074/jbc.M112.355958
http://www.alphagalileo.org/ViewItem.aspx?ItemId=119583&CultureCode=en

Alzheimer's Might Be Transmissible in Similar Way as Infectious Prion Diseases, Research Suggests
ScienceDaily (Oct. 4, 2011)
http://www.sciencedaily.com/releases/2011/10/111004113757.htm


De novo induction of amyloid-β deposition in vivo.
R Morales, C Duran-Aniotz, J Castilla, L D Estrada, C Soto.
Molecular Psychiatry, 2011; DOI: 10.1038/mp.2011.120
http://www.uthouston.edu/media/story.htm?id=3541058

Neurodegeneration 'Switched Off' in Mice
ScienceDaily (May 10, 2012)
…They found that the build up of mis-folded proteins in the brains of these mice activates a natural defense mechanism in cells, which switches off the production of new proteins. This would normally switch back 'on' again, but in these mice the continued build-up of mis-shapen protein keeps the switch turned 'off'. This is the trigger point leading to brain cell death, as those key proteins essential for nerve cell survival are not made.

By injecting a protein that blocks the 'off' switch of the pathway, the scientists were able to restore protein production, independently of the build up of mis-shapen proteins,and halt the neurodegeneration. The brain cells were protected, protein levels and synaptic transmission (the way in which brain cells signal to each other) were restored and the mice lived longer, even though only a very small part of their brain had been treated…
http://www.sciencedaily.com/releases/2012/05/120510141401.htm

Sustained translational repression by eIF2α-P mediates prion neurodegeneration.
Julie A. Moreno, Helois Radford, Diego Peretti, Joern R. Steinert, Nicholas Verity, Maria Guerra Martin, Mark Halliday, Jason Morgan, David Dinsdale, Catherine A. Ortori, David A. Barrett, Pavel Tsaytler, Anne Bertolotti, Anne E. Willis, Martin Bushell, Giovanna R. Mallucci.

Nature, 2012; DOI: 10.1038/nature11058

http://www2.le.ac.uk/offices/press/press-releases/2012/may/researchers-2018switch-off2019-neurodegeneration-in-mice?searchterm=Mallucci

New Understanding of Alzheimer's Trigger
ScienceDaily (May 2, 2012)
"This form of beta-amyloid, called pyroglutamylated (or pyroglu) beta-amyloid, is a real bad guy in Alzheimer's disease. We've confirmed that it converts more abundant beta-amyloids into a form that is up to 100 times more toxic, making this a very dangerous killer of brain cells and an attractive target for drug therapy."

Bloom said the process is similar to various prion diseases, such as mad cow disease or chronic wasting disease, where a toxic protein can "infect" normal proteins that spread through the brain and ultimately destroy it.

"You might think of this pyroglu beta-amyloid as a seed that can further contaminate something that's already bad into something much worse -- it's the trigger," Bloom said. Just as importantly, the hypertoxic mixtures that are seeded by pyroglu beta-amyloid exist as small aggregates, called oligomers, rather than as much larger fibers found in the amyloid plaques that are a signature feature of the Alzheimer's brain.

And the trigger fires a "bullet," as Bloom puts it. The bullet is a protein called tau that is stimulated by beta-amyloid to form toxic "tangles" in the brain that play a major role in the onset and development of Alzheimer's. Using mice bred to have no tau genes, the researchers found that without the interaction of toxic beta-amyloids with tau, the Alzheimer's cascade cannot begin. The pathway by which pyroglu beta-amyloid induces the tau-dependent death of neurons is now the target of further investigation to understand this important step in the early development of Alzheimer's disease
http://www.sciencedaily.com/releases/2012/05/120502132956.htm

Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β.
Justin M. Nussbaum, Stephan Schilling, Holger Cynis, Antonia Silva, Eric Swanson, Tanaporn Wangsanut, Kaycie Tayler, Brian Wiltgen, Asa Hatami, Raik Rönicke, Klaus Reymann, Birgit Hutter-Paier, Anca Alexandru, Wolfgang Jagla, Sigrid Graubner, Charles G. Glabe, Hans-Ulrich Demuth, George S. Bloom.
Nature, 2012; DOI: 10.1038/nature11060
http://www.newswise.com/articles/scientists-gain-new-understanding-of-alzheimer-s-trigger

Treatment With Vitamin C Dissolves Toxic Protein Aggregates in Alzheimer's Disease
ScienceDaily (Aug. 18, 2011)
… "When we treated brain tissue from mice suffering from Alzheimer's disease with vitamin C, we could see that the toxic protein aggregates were dissolved. Our results show a previously unknown model for how vitamin C affects the amyloid plaques," says Katrin Mani, reader in Molecular Medicine at Lund University.
"Another interesting finding is that the useful vitamin C does not need to come from fresh fruit. In our experiments, we show that the vitamin C can also be absorbed in larger quantities in the form of dehydroascorbic acid from juice that has been kept overnight in a refrigerator, for example."…
http://www.sciencedaily.com/releases/2011/08/110818101645.htm


These files and other from the web site http://www.oligomerix.com

http://www.oligomerix.com/frames/Tau%20Backgrounder.pdf

Trans-Synaptic Spread of Tau Pathology In Vivo
http://www.oligomerix.com/frames/Trans-Synaptic%20Spread%20of%20Tau%20Pathology%20In%20Vivo.pdf

Alzheimer's disease "jumps" across brain cells to spread
February 2, 2012 10:07 AM
http://www.cbsnews.com/8301-504763_162-57370328-10391704/alzheimers-disease-jumps-across-brain-cells-to-spread/


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Updated: July 2, 2012
Inception: July 2, 2012