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Lottis
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Posted: Fri Mar 12th, 2010 00:39 |
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wrotek wrote:
I wonder what expresses beta amyloid, since vdr is blocked, it is something else right?
This video makes a suggestion that might shed some light.
http://www.scivee.tv/node/7266
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Prof Trevor Marshall
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Posted: Fri Mar 12th, 2010 01:37 |
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Good find, Lottis 
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Santa Monica
inactive member
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Posted: Tue May 4th, 2010 20:15 |
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Found this today on amylase-A and sarcoidosis. How do I make sense of it?
http://www.medicalnewstoday.com/articles/187493.php
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Prof Trevor Marshall
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Posted: Tue May 4th, 2010 20:23 |
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It says that Sarcoidosis is a Th1 disease, that TLR2 is important, and Nuclear factor kappaB. All of which we already knew.
But it also implies that Amyloid-A, like Amyloid-beta in Alzheimers, is performing an antimicrobial function (based on the cytokines it induces). Which is interesting indeed.
So basically this is nothing really new, but confirmation of what we had already figured out
I am in Ljubljana, and very busy, but hopefully others can fill in the detail for you
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wrotek
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Posted: Tue May 4th, 2010 20:58 |
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Very interesting, since coffee also raises it.
Dr Marshall, is this protein expressed by VDR ?
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wrotek
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Posted: Tue May 4th, 2010 21:26 |
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No, it cannot be expressed by vdr since it raises when VDR is blocked
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Bane
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Posted: Tue May 4th, 2010 21:38 |
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Long-term TNF-alpha blockade in patients with amyloid A amyloidosis complicating rheumatic diseases.
http://www.ncbi.nlm.nih.gov/pubmed/20399323
Most adverse events were similar in both groups, although the number of infections was 3 times higher in amyloid A amyloidosis cases. CONCLUSION: Anti-tumor necrosis factor drugs are effective in treating amyloid A amyloidosis, although they might increase the risk of infection.
The acute phase reactant response to respiratory infection with Chlamydia pneumoniae: Implications for the pathogenesis of atherosclerosis.
http://www.ncbi.nlm.nih.gov/pubmed/20417302
A single intranasal inoculation stimulated statistically significant increases in the plasma levels of IL-2, IL-5, IL-6, IL-10, IL-12, GM-CSF, IFN-gamma, and serum amyloid A but not TNF-alpha, IL-1beta, IL-4 and serum amyloid P.
Hepatic gene expression changes in pigs experimentally infected with the lung pathogen Actinobacillus pleuropneumoniae as analysed with an innate immunity focused microarray.
http://www.ncbi.nlm.nih.gov/pubmed/19710094
The microarray analysis of liver tissue established that 51 genes were differentially expressed. A large group of these genes encoded proteins involved in the acute phase response, including serum amyloid A, C-reactive protein, fibrinogen, haptoglobin and tumor necrosis factor-alpha the expression of which were all found to be up-regulated and glutathione S-transferase, transthyretin, transferrin and albumin which were down-regulated.
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Phillyguy
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Posted: Fri May 7th, 2010 06:56 |
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http://www.physorg.com/news192255677.html
Spouses of dementia sufferers have a 6-fold increased risk of dementia onset
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Joyful
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Posted: Fri May 7th, 2010 17:46 |
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That last would be a good study to add to this KB article:
http://mpkb.org/home/pathogenesis/familial_aggregation
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Diesel
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Posted: Fri May 14th, 2010 11:12 |
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Infection Defense May Spur Alzheimer’s
http://www.nytimes.com/2010/03/09/health/09alzh.html?ref=science
Diesel
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Osteoporosis 2007 True knowledge exists in knowing that you know nothing
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titta
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Posted: Sun May 16th, 2010 10:55 |
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Hello Diesel,
this thread has started with this!
Take care,
Titta
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Frans
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Posted: Sun Sep 12th, 2010 05:17 |
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Hi all,
Just ran into this on sciencedaily:
Harmful Amyloid Interferes With Trash Pickup for Cells in Alzheimer's Disease
http://www.sciencedaily.com/releases/2010/09/100908094924.htm
So: microbiota-> inflammation -> amyloid beta -> proteasome hi-jacked ?
Best, Frans
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Lottis
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Posted: Sun Sep 12th, 2010 06:05 |
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Yes maybe
1- microbiota
2- amyloid
3- interferes with the processing of other proteins by competing for access
4- inhibits the proteasome.
Yang and postdoc Xiaobei Zhao showed that amyloid actually doesn't harm the proteasome.
Instead it interferes with the processing of other proteins by competing for access, they report in a forthcoming issue of the journal ACS Chemical Neuroscience.
And again I am tempted to give a tip about this paper on how amyloid like struktures might build up in the brain.
http://www.scivee.tv/node/7266
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titta
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Posted: Thu Sep 23rd, 2010 23:03 |
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...and Chlamydia again, at least they look for that....
Immunohistological detection of Chlamydia pneumoniae in the Alzheimer's disease brainhttp://www.biomedcentral.com/1471-2202/11/121/abstract
They have used anitbodies against this species.
I wonder when they systemically use their devices to look futher on.........probably first when they think further on......
Titta
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titta
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Posted: Thu Sep 23rd, 2010 23:05 |
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I do not know what happened.....when I wrote it it looked better. So another try.
http://www.biomedcentral.com/1471-2202/11/121/abstract
http://www.biomedcentral.com/content/pdf/1471-2202-11-121.pdf
Titta
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Bane
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Posted: Fri Dec 31st, 2010 14:41 |
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Alzheimer's Disease: Are Plaques and Tangles a Symptom, Not the Cause?
http://www.sciencedaily.com/releases/2010/12/101214181932.htm
The theory -- which holds that the beta-amyloid peptide is the key to the initiation and progression of the disease -- has had significant appeal as the peptide is the main ingredient of the disease-related plaques that are common in the brains of those affected.
Indeed, this persistent correlation has led researchers to spend many years and many millions of dollars looking for ways to prevent plaques as a way of treating, curing or preventing Alzheimer's. In recent years, however, dozens of human clinical trials based on this theory have failed.
Herrup, the chair of the Department of Cell Biology and Neuroscience at Rutgers University, suggests an alternative perspective, which he has set forth in a paper published December 14 in the Journal of Neuroscience. Pointing out that age is the most important risk factor in the disease, he suggests a new hypothesis with age as the starting point.
Age slows the brain's agility and blunts its responses to change; on their own, however, age-related changes lead only to a slow 'natural' decline in cognitive function, Herrup says. He posits that while these changes might increase one's risk of the Alzheimer's, they do not cause the disease.
Herrup believes three three key steps that are needed for an individual to progress from this natural path to the full spectrum of Alzheimer's clinical symptoms: an initiating injury that is probably vascular in nature; an inflammatory response that is both chronic and unique to Alzheimer's; and a cellular change of state, a one-way cell biological door that permanently alters the physiology of neurons and several other cell types in the Alzheimer's disease brain.
"The initiating injury might trigger a protective response in the brain cells," Herrup said. "But the real problem is that in the elderly the response doesn't know when to quit. It continues even after the injury itself subsides. In the end, the real damage is done by the persistence of the response and not by the injury, itself."
Herrup hopes his new theory will stimulate discussion and open the way to new experimental and diagnostic advances. "This new hypothesis, for example, emphasizes the value of anti-inflammatory approaches to the prevention of Alzheimer's disease," Herrup says.
He concedes that the individual components of the model aren't entirely new, but points out that by rearranging their order and shifting their priority, his view has enormous implications for modern Alzheimer's research.
"My hypothesis implies that beta-amyloid aggregation is not a central part of the biology of Alzheimer's disease," Herrup says. "It predicts that one can have plaques without having Alzheimer's and that one can have Alzheimer's without having plaques.
"Researchers should be cautious about following up these predictions, but since we've gone about as far as we can with our current hypothesis, we may have reached a point where too much caution is ill-advised. It's time to re-imagine Alzheimer's disease, so we can think creatively about treating it."
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Bane
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Posted: Sat Feb 5th, 2011 23:25 |
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A Novel Perspective for Alzheimer's Disease: Vitamin D Receptor Suppression by Amyloid-β and Preventing the Amyloid-β Induced Alterations by Vitamin D in Cortical Neurons
http://iospress.metapress.com/content/mg838747x7844354/
Amyloid-β (Aβ) is the core component of amyloid plaques of Alzheimer's disease (AD). The effects of Aβ include damage to neuronal plasma membrane, disruption of Ca2+ homeostasis, and alterations of neurotrophic factor levels. The aim of this study was to determine the effects of Aβ treatment on vitamin D receptor (VDR), L-type voltage sensitive calcium channels A1C (LVSCC A1C), NGF, and observing the effects of vitamin D treatment on Aβ induced alterations in primary cortical neurons. As to the latter, we aimed to test the suggested neuroprotective role of vitamin D as a neglected neurosteroid. The expressions of VDR and LVSCC A1C were studied with qRT-PCR and Western blotting. NGF and cytotoxicity levels were determined by ELISA. Apoptotic cell death was investigated with caspase-3 protein expression by Western blotting. Our results showed that the Aβ triggers neurodegeneration not only by inducing LVSCC A1C expression and NGF levels and but also by dramatically suppressing VDR expression. Administration of vitamin D to this model protected neurons by preventing cytotoxicity and apoptosis, and also by downregulating LVSCC A1C and upregulating VDR. Additionally, vitamin D brought NGF expression to a state of equilibrium and did not show its apoptosis inducing effects. Consequently, prevention of Aβ toxicity which was one of the major component of AD type pathology by vitamin D treatment and understanding how Aβ effects vitamin D related pathways, might open up new frontiers in clarifying molecular mechanisms of neurodegeneration and provide basis for novel perspectives in both preventing and treating AD.
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Bane
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Posted: Thu Mar 17th, 2011 03:11 |
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The Effects of Vitamin D Receptor Silencing on the Expression of LVSCC-A1C and LVSCC-A1D and the Release of NGF in Cortical Neurons.
http://www.ncbi.nlm.nih.gov/pubmed/21408608
CONCLUSIONS/SIGNIFICANCE: Our results indicate that suppression of VDR disrupts LVSCC-A1C and NGF production. In addition, when VDR is suppressed, neurons could be vulnerable to aging and neurodegeneration, and when combined with Aβ toxicity, it is possible to explain some of the events that occur during neurodegeneration.
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Phillyguy
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Posted: Thu Mar 17th, 2011 08:48 |
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http://www.msnbc.msn.com/id/41971124/ns/health-alzheimers_disease/
Alzheimers may start in the liver.
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Joyful
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Posted: Thu Mar 17th, 2011 21:14 |
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"The protein that forms plaques in the brains of people with Alzheimer's disease may have its origins in the liver, a new study in mice suggests. The researchers said that targeting the liver's production of this protein, called beta amyloid, may be a new way to treat Alzheimer's."
However, if beta amyloid is one of the body's anti-microbials (as I have read previously in this thread) then you are simply reducing the anti-microbial activity in the brain???
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