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07-18-2010, 12:31 PM | #1 | |||
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(Please be advised, this is a "Review" article. If reading reviews precipitates annoyance, anger, scathing responses, etc, please skip. Life is too short, etc. etc. madelyn)
(I wondered what happened to the topic of heat shock proteins; there were several presentations on this topic at the last WPC conference in Wash DC. I think this topic may be especially impt for LRRK2 and Parkin genetic mutations assoc with PD. The following is link to the full text) http://www.molecularneurodegeneratio...content/5/1/24 Review Heat shock protein 90 in neurodegenerative diseases Wenjie Luo1 , Weilin Sun2 , Tony Taldone2 , Anna Rodina2 and Gabriela Chiosis2 1 Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University and Fisher Foundation for Alzheimer's Disease, New York, NY 10021, USA 2 Department of Medicine and Program in Molecular Pharmacology and Chemistry, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA Abstract Hsp90 is a molecular chaperone with important roles in regulating pathogenic transformation. In addition to its well-characterized functions in malignancy, recent evidence from several laboratories suggests a role for Hsp90 in maintaining the functional stability of neuronal proteins of aberrant capacity, whether mutated or over-activated, allowing and sustaining the accumulation of toxic aggregates. In addition, Hsp90 regulates the activity of the transcription factor heat shock factor-1 (HSF-1), the master regulator of the heat shock response, mechanism that cells use for protection when exposed to conditions of stress. These biological functions therefore propose Hsp90 inhibition as a dual therapeutic modality in neurodegenerative diseases. First, by suppressing aberrant neuronal activity, Hsp90 inhibitors may ameliorate protein aggregation and its associated toxicity. Second, by activation of HSF-1 and the subsequent induction of heat shock proteins, such as Hsp70, Hsp90 inhibitors may redirect neuronal aggregate formation, and protect against protein toxicity. This mini-review will summarize our current knowledge on Hsp90 in neurodegeneration and will focus on the potential beneficial application of Hsp90 inhibitors in neurodegenerative diseases.
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In the last analysis, we see only what we are ready to see, what we have been taught to see. We eliminate and ignore everything that is not a part of our prejudices. ~ Jean-Martin Charcot The future is already here — it's just not very evenly distributed. William Gibson |
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"Thanks for this!" says: | anon72219 (07-18-2010) |
07-20-2010, 02:50 PM | #2 | |||
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In Addition, an older review article, though directly related to PD (and full text):
http://www.biolsci.org/v03p0020.htm Are heat shock proteins therapeutic target for Parkinson's disease? Guang-Rui Luo1, Sheng Chen2, Wei-Dong Int J Biol Sci 2007; 3:20-26. Heat shock proteins (HSPs), known as molecular chaperones to assist protein folding, have recently become a research focus in Parkinson's disease (PD) because the pathogenesis of this disease is highlighted by the intracellular protein misfolding and inclusion body formation. The present review will focus on the functions of different HSPs and their protective roles in PD.
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In the last analysis, we see only what we are ready to see, what we have been taught to see. We eliminate and ignore everything that is not a part of our prejudices. ~ Jean-Martin Charcot The future is already here — it's just not very evenly distributed. William Gibson |
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"Thanks for this!" says: | anon72219 (07-20-2010) |
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