9th Annual Biomarkers Congress
Protein Quality Control in Neurodegenerative Diseases
Etoile Saint Honoré
21-25 rue Balzac
Paris, France 75008
http://www.ipsen.com/sites/default/files/Protein_Quality_0.pdf
   The health of the proteome depends upon protein quality control to
   regulate the proper synthesis, folding, translocation, and clearance
   of proteins. The cell is challenged constantly by environmental and
   physiological stress, aging, and the chronic expression of disease
   associated misfolded proteins. Substantial evidence supports the
   hypothesis that the expression of damaged proteins initiates a cascade
   of molecular events that leads to Alzheimer’s disease (AD),
   Parkinson’s disease (PD), amyotrophic lateral sclerosis ( ALS ),
   Huntington’s disease, and other diseases of protein conformation. For
   each disease, there is a distinctive clinical profile with
   characteristic age-dependent onset and selective neuronal
   vulnerability despite more widespread expression of the causative
   protein.

   Maintenance of the proteome is central to the health of the cell and
   depends on efficient protein folding homeostasis, or proteostasis, to
   monitor protein quality control and ensure folding is optimized and
   that misfolded and damaged proteins do not persist. The proteostasis
   network, composed of molecular chaperones, detoxifying enzymes,
   transport pathways, and clearance machineries also monitors
   subcellular traffi cking and organellar crosstalk, while
   simultaneously detecting and responding to expressed polymorphisms and
   random errors that occur during protein biogenesis. Exposure to
   environmental and physiological stress that enhances the flux of
   metastable proteins increases the risk for misfolding and aggregation.
   Consequently, all cells express stress-inducible genetic pathways such
   as the heat shock response and unfolded protein response that detect,
   prevent, and resolve such damage.

   There is growing evidence that proteostatic deficiencies in
   neurodegenerative disease and other diseases of protein conformation
   that interfere with protein stability and function can be suppressed
   by enhancing the activities of chaperones and restoring the proteasome
   and autophagy. Whether achieved by genetic approaches or small
   molecules, it may now be possible to achieve the goal of enhancing the
   concentration, conformation, quaternary structure and/or the location
   of a protein by readapting the innate biology of the cell to
   ameliorate the most challenging diseases of our era.

Event Sponsors

Schedule of Presentations:

Monday, May 9, 2011
08:00:00 Registration
08:30:00 Introduction Yves Christen, Richard Morimoto,
08:45:00 Aggregation toxicity and the cellular defence against it Ulrich Hartl
09:15:00 Cellular control of protein homeostasis in health and disease J Frydman
09:45:00 Neuronal control of organismal proteostasis in aging and disease Richard Morimoto,
10:15:00 Adapting proteostasis to ameliorate loss- and gain-of-function misfolding diseases Jeffery Kelly
10:45:00 Posters and coffee break
11:15:00 Mechanisms for coping with ER stress David Ron
11:45:00 Conversion of the cell non-automous role of the UPR for neurodegenerative therapeutics Andy Dillin
12:15:00 Lunch and posters
14:00:00 The regulation of autophagy Daniel J Klionsky
14:30:00 Selective autophagy in cellular quality control Ana Maria Cuervo
15:00:00 Physiological roles of cytoplasmic degradation by autophagy N Mizushima
15:30:00 Posters and coffee break
16:00:00 BAG3-mediated selective autophagy of aggregation-prone proteins Christian Behl
16:30:00 Longitudinal measures of proteastasis in live neurons: features that predict cell fate in models of neurodegenerative disease Steven Finkbeiner
17:00:00 Subversion of a developmental signaling pathway in diseased neurons Christian Neri
17:30:00 Conclusion Richard Morimoto,
18:00:00 End of the meeting
4th Annual Pharma R&D Asia Congress
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