Hey Mike, it appears that Dr. Vodyanoy of Auburn University, Alabama is looking for partners in the development of diagnostics and treatments for misfolded protein diseases, including prion-related diseases.....
Link: http://ott.auburn.edu/overview/PNC-Misfolded-Proteins.pdf
https://www.vetmed.auburn.edu/%7Evodyavi/Gliomas/GliomaMov.html
Video of PNC effect on: 1. Healthy Cells, and 2. Glioma cells Dr. Vitaly Vodyanoy, University of Auburn, Alabama
This Vodyanoy abstract above on the role of Zn nanoclusters is found at the website of the “Center for Nonlinear Studies”. The webpage is operated by the Los Alamos National Security, LLC for the National Nuclear Security Commission of the USA Department of Energy.
Sadly, this shows a direct link between the activities of the Nuclear Commission and Department of Energy with the research into misfolded proteins. The reasons for the misfolding is, in my opinion, the contamination of the environment with these 'proteon nucleating centers' which can be made up of various products from nuclear power, nuclear enrichment, nuclear explosions, weapons development [depleted uranium and tungsten bullets, projectiles and bombs, etc.] An example of this is the Phalanx weapons systems which are used by many countries, including Canada, (purchased from the USA). Its munitions were depleted uranium (DU) until the late '90s when they switched to tungsten. Quite a coincidence that prion trimer fibrils seem to have a very high affinity to uranyl ions and tungsten.
Given that these PNCs (metallic non-ionic nanoclusters) have been found "in animal and human blood, plants, and soil" it is about time we started addressing the dangerous forms which exist out there, and stop creating more of them.
Also check out Wikipedia's page on "Depleted Uranium" subtitle "Gulf War Syndrome": [here is a short excerpt]
http://en.wikipedia.org/wiki/Depleted_uranium
It takes a great deal of pressure to have something like this "admitted to" on Wikipedia's site. Seems the evidence is piling up and the connection can no longer be denied entirely. Now excuses are coming forth as to how much is really 'significantly dangerous'.
Mike, note that there is a lecture by Vitaly Vodyanoy listed at the "CNLS" site under conferences (colloqium). To take place April 9, 2007 at 3 - 4PM CNLS Conference Room (TA-3, Bldg 1690). You should investigate this and attend if you are able.
You might even want to check out the def. for prions on Wikipedia:
I couldn't help but add my own little comments to their idea, in italics
High praise of Purdey and Brown considering what the site used to say. Yes it has been recently updated and the "contrasting theory" is gaining ground.
Link: http://ott.auburn.edu/overview/PNC-Misfolded-Proteins.pdf
Overview
Auburn University is seeking a licensee or development partner for naturally occurring novel metal clusters that exhibit protein scavenging properties. Proteon nucleating centers (PNCs) consist of 1- to 2-nm nanoparticles that contain 40–300 non-ionic metal atoms. These nanoclusters have been shown to scavenge misfolded proteins to form proteons: clusters of up to 100,000 protein molecules with metal centers. Thus, PNCs have tremendous potential in the diagnosis and treatment of diseases associated with misfolded proteins, including prion-related diseases, neurological diseases, blood diseases and cancer.
Advantages
• Naturally occurring in blood, indicating inherent biocompatibility
• Scavenge misfolded proteins, suggesting numerous medical
applications
• Lethal to cultured cancer cells (view images | Quicktime movie)
• Can be isolated and purified through simple methods
• Multiple production methods exist
Description
Unfolding and subsequent aggregation of proteins is a common phenomenon linked to many human disorders. In investigating a possible mechanism by which excess hemoglobin release may be controlled in blood plasma in the disease state, it was discovered that human blood contains particles (“proteons”) that may reinforce hemoglobin scavenging.
It was later determined that these proteons consist of a small core of metal atoms (PNCs) that have scavenged misfolded proteins to form a protein shell around the metal center. PNCs have been found and isolated from humans and numerous animal species.
This activity against misfolded proteins suggests numerous potential medical applications. Proteins that have misfolded and/or aggregated have been tied to many disorders, some of which do not currently have appropriate therapies. Such disorders include prion-related diseases (e.g., Bovine spongiform encephalopathy), neurological diseases including Alzheimer’s and Parkinson’s, and blood disorders such as sickle cell anemia and some autoimmune disorders. PNCs and proteons could also be used to collect misfolded proteins in a patient, allowing for a means to diagnose and measure progression of disease states.
Additionally, PNCs were found to be unexpectedly pro-apoptotic when added to cultured animal cells, showing much greater effectiveness against cancer cells than non-cancerous cells. This, along with their natural occurrence, suggests that PNCs could have significant
effectiveness in cancer therapy. Preliminary studies also indicate PNCs could have applications in entirely different medical areas as well as non-medical areas.
Status
• A U.S. Patent has been issued (7,138,255). Several non-provisional U.S. applications (including 20050142611) and one EU patent application are pending
• Proteons and PNCs have been isolated and well characterized
• Activity against cancer cells has been demonstrated in vitro
Partnership Opportunities
• Available for exclusive, field of use, research or non-exclusive licensing
• Joint development opportunities include collaboration, funded research or joint venture
https://www.vetmed.auburn.edu/%7Evodyavi/Gliomas/GliomaMov.html
Video of PNC effect on: 1. Healthy Cells, and 2. Glioma cells Dr. Vitaly Vodyanoy, University of Auburn, Alabama
[G-proteins stands for proteins that attach to cells with a glycophospholipid anchor]http://t-7.lanl.gov/External/showtalksummary.php?selection=543
Role of Zn nanoclusters in signal transduction in olfactory neurons, Dr. Vitaly Vodyanoy
Proteons, small particles of misfolded proteins (40-250 nm) polymerized around inorganic centers, were found in animal and human blood, plants, and soil. Proteons form by reversible seeded aggregation of proteins around protein nucleating centers (PNCs). PNCs are comprised of 1–2-nm metallic nanoclusters containing 40–300 atoms. Each milliliter of human blood contained ~7 × 1013 PNCs and ~3 × 108 proteons. We recently discovered that G-protein governed olfactory signals are strongly enhanced by PNCs. We hypothesize that PNCs (small metallic nanoclusters) provide an electronic coupling between G-proteins and extracellular receptors (signals). The primary events of olfactory transduction occur at the cilia of olfactory receptor neurons and involve the binding of odorants to receptor proteins followed by activation of heterotrimeric guanine nucleotide-binding proteins (G-proteins), and effector enzymes. Two different effector enzymes, G-protein-coupled adenylyl cyclase and phospholipase C, are known to control primary responses of olfactory neurons to odor stimulation in invertebrates and vertebrates. Although the excitatory reactions involving signal pathways are well explored, the mechanism of transferring of signal from the receptor protein to G-protein is unknown. In 1996 Luka Turin [A spectroscopic mechanism for primary olfactory reception, Chemical Senses Vol 21/ 6 pp773-791] has provided a plausible mechanism of signal transduction between the odorant receptor and G-protein. He proposed that a process called "inelastic electron tunneling" is responsible for this transduction. For this electron transfer Turin suggested that a zinc ion binding sites are present both on the odorant receptor protein and the G-protein. While Turin’s theory has not been proved, it seems quite reasonable. We hypothesized that zinc metal nanoclusters and not zinc ions play role in the electron tunneling and provide a mechanism for the signal transduction between receptor proteins and G-proteins. In order to examine this hypothesis we made experiments showing that introduction of zinc nanoclusters (or PNC) to a rat olfactory epithelium or to a single olfactory neuron dramatically increases the electrical response to odorant. The effect is dose dependent and reversible. The nanoclusters made of Cu, Au, and Ag produce no significant effects when they are added instead of zinc (or PNC) particles. These results may be useful for understanding of molecular mechanisms of initial events in olfaction. The work is supported by a grant from Fetzer Foundation.
This Vodyanoy abstract above on the role of Zn nanoclusters is found at the website of the “Center for Nonlinear Studies”. The webpage is operated by the Los Alamos National Security, LLC for the National Nuclear Security Commission of the USA Department of Energy.
Sadly, this shows a direct link between the activities of the Nuclear Commission and Department of Energy with the research into misfolded proteins. The reasons for the misfolding is, in my opinion, the contamination of the environment with these 'proteon nucleating centers' which can be made up of various products from nuclear power, nuclear enrichment, nuclear explosions, weapons development [depleted uranium and tungsten bullets, projectiles and bombs, etc.] An example of this is the Phalanx weapons systems which are used by many countries, including Canada, (purchased from the USA). Its munitions were depleted uranium (DU) until the late '90s when they switched to tungsten. Quite a coincidence that prion trimer fibrils seem to have a very high affinity to uranyl ions and tungsten.
Given that these PNCs (metallic non-ionic nanoclusters) have been found "in animal and human blood, plants, and soil" it is about time we started addressing the dangerous forms which exist out there, and stop creating more of them.
Also check out Wikipedia's page on "Depleted Uranium" subtitle "Gulf War Syndrome": [here is a short excerpt]
http://en.wikipedia.org/wiki/Depleted_uranium
"...Desert Storm veterans with retained DU fragments, had developed a slight (not statistically significant) tendency to lose weight with respect to the control group, as well as two isolated cases of total inability to eat, one of which caused by abnormal tooth growth. More importantly, the high dose group, which was maintained at a chronical level of DU roughly 5 times greater than found in veterans, had developed a significant tendency to lose weight with respect to the control group; substantial amounts of uranium were accumulating in their brains and central nervous systems, and showed a significant reduction of neuronal activity in the hippocampus in response to external stimuli. The conclusions of the study show that brain damage from chronic uranium intoxication is possible at lower doses than previously thought..."
It takes a great deal of pressure to have something like this "admitted to" on Wikipedia's site. Seems the evidence is piling up and the connection can no longer be denied entirely. Now excuses are coming forth as to how much is really 'significantly dangerous'.
Mike, note that there is a lecture by Vitaly Vodyanoy listed at the "CNLS" site under conferences (colloqium). To take place April 9, 2007 at 3 - 4PM CNLS Conference Room (TA-3, Bldg 1690). You should investigate this and attend if you are able.
You might even want to check out the def. for prions on Wikipedia:
I couldn't help but add my own little comments to their idea, in italics
"Contrasting theories:
Although the identity and general properties of prions are now well-understood [really that's a surprise to me], the mechanism of prion infection and propagation remains mysterious. It is often assumed that the diseased form directly interacts with the normal form to make it rearrange its structure (enlarge the diagram above for an illustration of this mechanism). One idea, the "Protein X" hypothesis, is that an as-yet unidentified cellular protein (Protein X)[ie: radiation induced screwed-up protein fragment] enables the conversion of PrPC to PrPSc by bringing a molecule of each of the two together into a complex.[14][bringing 3 screwed-up fragments together around a metallic nanocluster called a proteon nucleating center, to form a trimer which can only then form fibrils]
Mark Purdey and Dr. David R. Brown have suggested that known metal ion interactions with prion protein might be relevant to progression of prion-mediated disease.[15] Purdey cited epidemiological studies of clusters of prion disease in locales with low soil concentrations of copper as evidence.
Brown's work claims to explain how protein tissue can be incinerated and remain "infectious", if that is the proper term for a theory that resembles heavy metal poisoning. Brown, whose primary professional affiliation is with the University of Bath in the United Kingdom, agrees that banning cannibalism in cows was a justifiable course of action."
High praise of Purdey and Brown considering what the site used to say. Yes it has been recently updated and the "contrasting theory" is gaining ground.