ATH 0.00% 0.3¢ alterity therapeutics limited

clarifying comment from rudy tanzi, page-24

  1. 308 Posts.
    Hi ST,

    Consider the Brain is working overtime trying to get metals into Neurons where there is currently a log jam. The Brain is working harder and harder over time and this is stressing the brain. Because of this stress the normal protein in use to aid in the transfer of metals is created in excess and many a protein is misfolded. The Brain may or may not sense it is under attack externally at this time all that it knows is that it is losing control of Neuron function. It may also be seeing a decrease in the amount of metals available for use.
    In the metals hypothesis (which has widely been reclaiming fame by many an independant scientific paper) the chaperoning that occurs allows metals out of the Amyloid so that the Plaque burden diminishes. The free metals are then able to be chaperoned into the Neurons. Since the primary burden on the brain has diminished (plaque reduction) misfolded proteins are more easily cleared. PBT2 happens to reduce the work load on the brain so well, that the brain is able to functionally improve damaged Neurons and also aid in creating new Neuron growth. The brain sees all of this happening and begins to work much more efficiently.
    If doubt still exists and as you say it is Metal Homeostasis that has you bothered, then take note because the ongoing talk now is stating Protein Homeostais as well as selective homeostasis for specific organs of the body.
    Metal Homeostasis happens to be Prana's hallmark for PBT2 because of the chaperoning effect of the drug. Prana is concentrating their drugs at the moment only on the Brain. Since most specialized cells in the body also use metals, it is not a far flung assumption that other diseases affect metals in those organs so affected.
    I can see that you have only read a trivial amount of information available on the subject and are basing your conjecture on the lack of true knowledge.
    If you look at Big Pharmas tried and failed approaches, you will find many an item to support the possibility of metals homeostasis rather than writing it off.
    When you are talking about investing in a Security, especially this one and on this board, it would be much wiser to have all your ducks in a row. Just talking about Risk/Reward at current SP, with two stage 2 trial results imminent, it would be foolish to give advice questioning any possible investment in this Security as the Reward simply outweighs the Risk even for a Daytrader where most of the board here are longs anyway!
    May you find a much better company to invest your hard earned monies as you obviously no longer believe in this company or its lead drug candidate much less its PBT434 or PBT519 which will likely come along this year.
    Please come back in a year and tell us again what you believe!
    Matrix metalloproteinases (MMPs) are zinc-dependent protein and peptide hydrolases. They have been almost exclusively studied in vertebrates and 23 paralogs are present in humans. They are widely involved in metabolism regulation through both extensive protein degradation and selective peptide-bond hydrolysis. If MMPs are not subjected to exquisite spatial and temporal control, they become destructive, which can lead to pathologies such as arthritis, inflammation, and cancer. Together with the catalytic zinc ion, this pocket has been targeted since the onset of drug development against MMPs. However, the inability of first- and second-generation inhibitors to distinguish between different MMPs led to failures in clinical trials.
    The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.
    ADAM10, a member of a disintegrin and metalloprotease family, is an a-secretase capable of anti-amyloidogenic proteolysis of the amyloid precursor protein. Here, we present evidence for genetic association of ADAM10 with Alzheimer's disease (AD) as well as two rare potentially disease-associated non-synonymous mutations, Q170H and R181G, in the ADAM10 prodomain. These mutations were found in 11 of 16 affected individuals (average onset age 69.5 years) from seven late-onset AD families

 
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