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08-16-2008, 08:14 PM | #1 | |||
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Michael J. Fox Foundation Awards One Million Dollars for Development of 'Trojan Horse' Delivery Technology to Treat Parkinson's Disease
Friday, August 15, 2008 http://www.foxbusiness.com/story/mic...-trojan-horse/ NEW YORK, Aug 15, 2008 /PRNewswire-USNewswire via COMTEX/ ----As part of its mission to drive transformative treatments and a cure for Parkinson's disease, The Michael J. Fox Foundation today announced that it would award Santa Monica-based biotech ArmaGen Technologies, Inc., up to $1 million if all milestones are met to take practical steps toward developing a "Trojan horse" delivery technology for the treatment of Parkinson's disease. ArmaGen's novel approach would use molecular bio-engineering techniques to "trick" the brain into allowing large-molecule (e.g. protein-based) therapeutics across the blood-brain barrier in order to access targeted regions of the brain and address the neuronal loss that characterizes Parkinson's disease. If successful, the work could yield a first-in-class drug that would increase the feasibility of treating PD with therapeutics including trophic factors -- specialized, naturally occurring proteins that protect and nourish neurons -- by allowing for delivery via non-invasive intravenous administration. "At The Michael J. Fox Foundation, we believe that our capital has an obligation to fund high-risk, high-reward projects that, if successful, could significantly improve the lives of people with Parkinson's," said Katie Hood, CEO of MJFF. "A major element of our work is the identification and prioritization of approaches like ArmaGen's -- efforts that without our backing would likely stall for lack of resources." The blood-brain barrier surrounds the brain and functions to keep out pathogens and other harmful agents. While critical to human health, it presents one of the most daunting challenges for delivery of drugs used to treat PD and other central nervous system disorders. Some of the therapeutic approaches that currently show the most promise to yield transformative treatments for PD involve the use of so-called "large molecules" that are unable to penetrate the barrier. These approaches, which include trophic factors, currently require brain surgery, an inherently risky and invasive intervention, to access the brain regions affected in Parkinson's. (In March 2008 the Foundation launched a $2-million initiative, Improving Delivery of Parkinson's Disease Therapeutics to the Brain, solely designed to address PD drug delivery; funding is anticipated in October.) READ article
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08-16-2008, 09:55 PM | #2 | |||
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Paula already posted this earlier, but it bears repeating! Great news!
http://neurotalk.psychcentral.com/thread52238.html Peg |
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08-17-2008, 07:25 AM | #3 | |||
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Magnate
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I did see the title elsewhere, so I didn't realize I duplicated the effort. Sorry Paula.
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You're alive. Do something. The directive in life, the moral imperative was so uncomplicated. It could be expressed in single words, not complete sentences. It sounded like this: Look. Listen. Choose. Act. ~~Barbara Hall I long to accomplish a great and noble tasks, but it is my chief duty to accomplish humble tasks as though they were great and noble. The world is moved along, not only by the mighty shoves of its heroes, but also by the aggregate of the tiny pushes of each honest worker. ~~Helen Keller |
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08-17-2008, 01:26 PM | #4 | |||
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Senior Member
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http://www.ncbi.nlm.nih.gov/pubmed/1...?dopt=Abstract
Biotechnol Bioeng. 2008 Jun 1;100(2):387-96.Related Articles, Links GDNF fusion protein for targeted-drug delivery across the human blood-brain barrier. Boado RJ, Zhang Y, Zhang Y, Wang Y, Pardridge WM. ArmaGen Technologies, Inc., Santa Monica, California, USA. Glial-derived neurotrophic factor (GDNF) is a neurotrophin that could be developed as a neurotherapeutic for Parkinson's disease, stroke, and motor neuron disease. However, GDNF does not cross the blood-brain barrier (BBB). Human GDNF was re-engineered by fusion of the mature GDNF protein to the carboxyl terminus of the chimeric monoclonal antibody (MAb) to the human insulin receptor (HIR). The HIRMAb-GDNF fusion protein is bi-functional, and both binds the HIR, to trigger receptor-mediated transport across the BBB, and binds the GDNF receptor (GFR)-alpha1, to activate GDNF neuroprotection pathways behind the BBB. COS cells were dual transfected with the heavy chain (HC) and light chain fusion protein expression plasmids, and the HC of the fusion protein was immunoreactive with antibodies to both human IgG and GDNF. The HIRMAb-GDNF fusion protein bound with high affinity to the extracellular domain of both the HIR, ED(50) = 0.87 +/- 0.13 nM, and the GFRalpha1, ED(50) = 1.68 +/- 0.17 nM. The HIRMAb-GDNF fusion protein activated luciferase gene expression in human neural SK-N-MC cells dual transfected with the c-ret kinase and a luciferase reporter gene under the influence of the rat tyrosine hydroxylase promoter, and the ED(50), 1.68 +/- 0.45 nM, was identical to the ED(50) in the GFRalpha1 binding assay. The fusion protein was active in vivo in a rat middle cerebral artery occlusion model, where the stroke volume was reduced 77% (P < 0.001). In conclusion, these studies describe the re-engineering of GDNF, to make this neurotrophin transportable across the human BBB. PMID: 18080333 [PubMed - indexed for MEDLINE] Additional studies from ArmaGen Technologies: http://www.bioportfolio.com/biocorpo...hnologies.html
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