May 2005
Volume 46, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2005
Role of mRNA Localization to the Mitochondrial Surface in the Physiopathology of Retina
Author Affiliations & Notes
  • M.C. Debrinsky
    Lab de Physiopathatologie Retinienne, INSERM U 592, Paris Cedex 12, France
  • V. Kaltimbacher
    Lab de Physiopathatologie Retinienne, INSERM U 592, Paris Cedex 12, France
  • C. Bonnet
    Lab de Physiopathatologie Retinienne, INSERM U 592, Paris Cedex 12, France
  • T. Leveillard
    Lab de Physiopathatologie Retinienne, INSERM U 592, Paris Cedex 12, France
  • D. Thiersé
    Laboratoire de Spectrométrie de Masse Bio–Organique, IGBMC Illkirch, Strasbourg, France
  • J.A. Sahel
    Lab de Physiopathatologie Retinienne, INSERM U 592, Paris Cedex 12, France
  • Footnotes
    Commercial Relationships  M.C. Debrinsky, None; V. Kaltimbacher, None; C. Bonnet, None; T. Leveillard, None; D. Thiersé, None; J.A. Sahel, None.
  • Footnotes
    Support  french associaitions : AFM, FRM Retina
Investigative Ophthalmology & Visual Science May 2005, Vol.46, 5147. doi:
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      M.C. Debrinsky, V. Kaltimbacher, C. Bonnet, T. Leveillard, D. Thiersé, J.A. Sahel; Role of mRNA Localization to the Mitochondrial Surface in the Physiopathology of Retina . Invest. Ophthalmol. Vis. Sci. 2005;46(13):5147.

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

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Abstract

Abstract: : Purpose: Known mitochondrial disorders, which involve retina degeneration, arise from mutations in both nuclear and mitochondrial genes encoding mitochondrial proteins such as Leber Hereditary Optic Neuropathy (LHON) and dominant optic atrophy (DOA). We predict that a growing number of genes involved in mitochondrial assembly will be discovered as causative of retina dysfunction. In yeast, mitochondrial assembly requires the delivery to the organelle surface of mRNAs, encoding mitochondrial proteins. We use this phenomenon as a tool for : (i) identifying new mitochondrial proteins. (ii) providing molecular mechanisms for retina disorders. (iii) developing a therapy to restore mitochondrial function in cells from LHON’s patients. Methods: (i) large scale proteomic survey of mitochondria purified from mouse retina and brain, as well as, from human cells are performed. (ii) the complete inventory of mRNAs localized to the mitochondrial surface will be obtained from mouse and human cells. (iii) DOA’s patients will be screneed to determine whether the disease could be the consequence of OPA1 mRNA abnormal localization. (iv) cytoplasmic versions of Atp6, Nd1 and Nd4 mitochondrial proteins will be examined for their ability of restoring mitochondrial function in cells with mutations of these genes. Results: (i) 2D gels were performed with mitochondrial proteins purified from mouse brain and retina. Several hundreds of spots are, currently, under identification. (ii) DNA microarrays hybridized with RNAs purified from mitochondrion–bound polysomes and free–cytoplasmic polysomes confirm the asymmetrical distribution of hundreds of mRNAs in mouse brain. (iii) Mitochondrial import ability of the cytoplasmic Atp6 protein is under investigation in HeLa cells. Conclusions: Human mitochondrion is probably composed of 1500 polypeptides, up today, only 750 are clearly known. Our project, which combine proteomic survey and investigation on the subcellular distribution of mRNAs, will lead to assess a more complete mammalian mitochondrial proteome. The research of mRNA sorting perturbations as causative of retinal diseases, will provide a new pathophysiological mechanism for these disorders. Finally, if we improve the cytoplasmic expression of proteins encoded by mitochondrial DNA using mRNA sorting to the mitochondrial surface, we will develop a innovative therapy to LHON that can ultimately be applied in gene therapy.

Keywords: retinal degenerations: cell biology • mitochondria • gene/expression 
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