May 2008
Volume 49, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2008
The Interaction Between RdCVF and Tau Defines a Novel Signalisation Pathway in Photoreceptor Degeneration and Survival
Author Affiliations & Notes
  • R. Fridlich
    INSERM U592, Paris, France
  • L. Perrocheau
    INSERM U592, Paris, France
  • F. Delalande
    Laboratoire de Spectrométrie de Masse Bio-Organique, Strasbourg, France
  • W. Raffelsberger
    IGBMC, Laboratoire de Bioinformatique et Génomique Intégratives, Illkirch, France
  • O. Poch
    IGBMC, Laboratoire de Bioinformatique et Génomique Intégratives, Illkirch, France
  • A. Van Dorsselaer
    Laboratoire de Spectrométrie de Masse Bio-Organique, Strasbourg, France
  • J.-A. Sahel
    INSERM U592, Paris, France
  • T. Léveillard
    INSERM U592, Paris, France
  • Footnotes
    Commercial Relationships  R. Fridlich, None; L. Perrocheau, None; F. Delalande, None; W. Raffelsberger, None; O. Poch, None; A. Van Dorsselaer, None; J. Sahel, None; T. Léveillard, None.
  • Footnotes
    Support  INSERM, RETNET MRTN-CT-2003-504003
Investigative Ophthalmology & Visual Science May 2008, Vol.49, 2993. doi:https://doi.org/
  • Views
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      R. Fridlich, L. Perrocheau, F. Delalande, W. Raffelsberger, O. Poch, A. Van Dorsselaer, J.-A. Sahel, T. Léveillard; The Interaction Between RdCVF and Tau Defines a Novel Signalisation Pathway in Photoreceptor Degeneration and Survival. Invest. Ophthalmol. Vis. Sci. 2008;49(13):2993. doi: https://doi.org/.

      Download citation file:


      © ARVO (1962-2015); The Authors (2016-present)

      ×
  • Supplements
Abstract

Purpose: : RdCVF is a thioredoxin-like protein, derived from rods, that has the potential to rescue cone cells. The RdCVF long form (RdCVFL) has a putative thiol-oxidoreductase activity whereas the short one (RdCVF) is shown to act directly on cone photoreceptor survival. Identification of RdCVFL protein partners will enable us to understand the functional role of RdCVFL and its relation to cone rescue

Methods: : We have used a proteomic approach in order to identify RdCVFL protein partner candidates. Soluble protein lysate from chicken retina was loaded on GST-RdCVFL and GST columns. The eluted proteins were identified by MS/MS spectrometry. The interaction was validated by Cos-1 transfection followed by Co-immunoprecipitations

Results: : We identified 79 proteins that bind specifically to GST-RdCVFL. Among them, we focused on the protein Tau, because of its involvement in neurodegeneration diseases including Alzheimer. The interaction between RdCVFL and HA-tagged chicken Tau has been validated by Co-immuprecipitation. Microtubule associated protein (MAP) Tau is abnormally hyperphosphorylated in Alzheimer's disease (AD) and related tauopathies. This modified form of Tau is the major protein of paired helical filaments (PHFs)/neurofibrillary tangles (NFTs) which lead to aggregations and neuronal cell death. The interaction between Tau and RdCVFL may relate the observation that oxidative stress induces Tau hyperphosphorylation with the potential thiol-oxidoreductase activity of RdCVFL. Furthermore, this interaction may be fundamental to the process of cone degeneration in RP and allied retinal degenerations. We have analyzed the level of hyperphosphorylated Tau in RdCVF KO mice retina by western blotting. We found that Tau hyperphosphorylation is increased in RdCVF KO mice as compared with wild-type controls

Conclusions: : The interaction between RdCVFL, a thioredoxin-like protein and Tau is suggested to be intimately linked to the regulation of the redox status and hyperphosphorylation of Tau, the aggregation of paired helical filaments and as a result to photoreceptors survival

Keywords: neuroprotection • oxidation/oxidative or free radical damage • phosphorylation 
×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×