December 2002
Volume 43, Issue 13
Free
ARVO Annual Meeting Abstract  |   December 2002
Proteomic Approaches to Age-Related Macular Degeneration
Author Affiliations & Notes
  • JW Crabb
    Cole Eye Institute The Cleveland Clinic Foundation Cleveland OH
  • M Miyagi
    Cole Eye Institute The Cleveland Clinic Foundation Cleveland OH
  • X Gu
    Case Western Reserve University Cleveland OH
  • KA West
    Cole Eye Institute The Cleveland Clinic Foundation Cleveland OH
  • A Marmorstein
    Cole Eye Institute The Cleveland Clinic Foundation Cleveland OH
  • M Kamei
    Osaka University Osaka Japan
  • KG Shadrach
    Cole Eye Institute The Cleveland Clinic Foundation Cleveland OH
  • ME Rayborn
    Cole Eye Institute The Cleveland Clinic Foundation Cleveland OH
  • RG Salomon
    Case Western Reserve University Cleveland OH
  • JG Hollyfield
    Cole Eye Institute The Cleveland Clinic Foundation Cleveland OH
  • Footnotes
    Commercial Relationships   J.W. Crabb, None; M. Miyagi, None; X. Gu, None; K.A. West, None; A. Marmorstein, None; M. Kamei, None; K.G. Shadrach, None; M.E. Rayborn, None; R.G. Salomon, None; J.G. Hollyfield, None. Grant Identification: Support: NIH, FFB, Merck,Inc., and CCF Funds
Investigative Ophthalmology & Visual Science December 2002, Vol.43, 860. doi:
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    • Get Citation

      JW Crabb, M Miyagi, X Gu, KA West, A Marmorstein, M Kamei, KG Shadrach, ME Rayborn, RG Salomon, JG Hollyfield; Proteomic Approaches to Age-Related Macular Degeneration . Invest. Ophthalmol. Vis. Sci. 2002;43(13):860.

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

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Abstract

Abstract: : Purpose: The causes of drusen formation and Bruch's membrane thickening in age-related macular degeneration (AMD) are not known. However, the progression of AMD might be slowed if these processes could be modulated. Proteomic studies of these tissues from normal and AMD donors seek clues to the biochemical pathways involved in AMD. Methods: Microdissection and laser capture methods are used to isolate drusen and Bruch's membrane. Mass spectrometry tools are used for protein identification. Oxidative protein modifications are identified using bioinformatic tools and antibodies. Immunocytochemistry provides confirmation of drusen and Bruch's membrane localization. Results: We have developed methods for isolating drusen and Bruch's membrane that provide microgram amounts of protein. Currently 29 potential drusen proteins have been identified by LC MS/MS, 8 of which were observed by others using immunocytochemistry. We have confirmed clusterin, calgranulin A and B, and psoriasin as new drusen components by immunocytochemistry. Western results suggest that docosahexenoate derived protein modifications (ie, carboxyethyl pyrrole adducts) are more abundant in AMD than normal tissues. Advanced glycation end products and abnormal protein crosslinks also appear in drusen and Bruch's membrane. Conclusions: Oxidative protein modifications may be causally involved in drusen formation and Bruch's membrane thickening. Protoemic studies to test this hypothesis are in progress.

Keywords: 391 drusen • 525 protein modifications-post translational • 526 protein purification and characterization 
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