May 2005
Volume 46, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2005
Proteomic Analysis of Retinal Protein Expression With the Progression of AMD
Author Affiliations & Notes
  • C.M. Ethen
    Biochemistry, Molecular Biology, and Biophysics,
    University of Minnesota, Minneapolis, MN
  • N. Basak
    Ophthalmology,
    University of Minnesota, Minneapolis, MN
  • C. Reilly
    Division of Biostatistics,
    University of Minnesota, Minneapolis, MN
  • X. Feng
    Ophthalmology,
    University of Minnesota, Minneapolis, MN
  • T.W. Olsen
    Ophthalmology,
    University of Minnesota, Minneapolis, MN
  • D.A. Ferrington
    Ophthalmology,
    University of Minnesota, Minneapolis, MN
  • Footnotes
    Commercial Relationships  C.M. Ethen, None; N. Basak, None; C. Reilly, None; X. Feng, None; T.W. Olsen, None; D.A. Ferrington, None.
  • Footnotes
    Support  NIA Grant AG025392, NIH Grant EY01234, Unrestricted grant from Research to Prevent Blindness
Investigative Ophthalmology & Visual Science May 2005, Vol.46, 5180. doi:
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      C.M. Ethen, N. Basak, C. Reilly, X. Feng, T.W. Olsen, D.A. Ferrington; Proteomic Analysis of Retinal Protein Expression With the Progression of AMD . Invest. Ophthalmol. Vis. Sci. 2005;46(13):5180.

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

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Abstract

Abstract: : Purpose: Age–related macular degeneration (AMD) is characterized by drusen formation, retinal pigment epithelium (RPE) changes, geographic atrophy, and other clinical features. However, the etiology of the disease remains unclear. Since degeneration of photoreceptors precedes loss of the RPE layer, identification of changes in the neurosensory retina may provide insight into the early mechanisms of the disease. This study identified proteins that exhibited altered expression at specified stages of AMD. Methods: Human eyes from aged (60–90 yr) donors were obtained from the MN Lions Eye Bank. The eyes were graded using the Minnesota Grading System (MGS) (Olsen and Feng, IOVS, 45; 2004). Neurosensory retinal proteins from both the macular and peripheral regions were resolved using 2D polyacrylamide gel electrophoresis. Gels were silver stained and protein expression was analyzed using densitometry. For protein spots showing significant changes in expression, MALDI–TOF mass spectrometry (MS) was utilized to obtain protein identification. Protein identities were confirmed by tandem MS. Results: After analysis of ∼600 protein spots, we detected a subset of proteins demonstrating ∼2–fold protein expression changes (both increases and decreases) in both the macular and peripheral retina. Several of these protein spots show statistically significant expression changes between early onset and late stage disease. Proteins exhibiting 2–fold expression changes include proteins involved in metabolic, chaperone and signaling pathways. Conclusions: Resolution of neurosensory retinal proteins allows comparison for expression level changes from early to late stages of AMD defined by the MGS. These comparisons led to identification of region–specific subsets of proteins indicating 2–fold changes with increasing levels of AMD. The regional variation indicates that the protein profile changes differently in the macular region as compared with the peripheral region in AMD. Identification of specific proteins with altered expression may identify pathways involved in the pathogenesis of AMD.

Keywords: proteomics • age-related macular degeneration • retina 
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