April 2009
Volume 50, Issue 13
ARVO Annual Meeting Abstract  |   April 2009
Molecular Modifications of Human RPE Lipofuscin in vivo
Author Affiliations & Notes
  • E. R. Gaillard
    Chemistry & Biochemistry, Northern Illinois University, DeKalb, Illinois
  • L. S. Murdaugh
    Chemistry & Biochemistry, Northern Illinois University, DeKalb, Illinois
  • S. Mandal
    Chemistry & Biochemistry, Northern Illinois University, DeKalb, Illinois
  • J. P. Dillon
    Ophthalmology, Columbia University, New York, New York
  • J. D. Simon
    Chemistry, Duke University, Durham, North Carolina
  • Footnotes
    Commercial Relationships  E.R. Gaillard, None; L.S. Murdaugh, None; S. Mandal, None; J.P. Dillon, None; J.D. Simon, None.
  • Footnotes
    Support  RPB
Investigative Ophthalmology & Visual Science April 2009, Vol.50, 1837. doi:
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      E. R. Gaillard, L. S. Murdaugh, S. Mandal, J. P. Dillon, J. D. Simon; Molecular Modifications of Human RPE Lipofuscin in vivo. Invest. Ophthalmol. Vis. Sci. 2009;50(13):1837.

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

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Purpose: : To determine the molecular mechanisms of modifications to A2E found in human RPE lipofuscin.

Methods: : Human RPE lipofuscin granules were isolated as described (Feeney-Burns, 1980) from donor globes (Midwest Eye Banks). The organic soluble portion was obtained by extraction with equal amounts of CHCl3:CH3OH:H2O, and the extract was analyzed by LC-MS (Thermo Finnigan, Surveyor LC with fluorescence and PDA detectors, LCQ Advantage ion trap mass analyzer, electrospray ion source).

Results: : In addition to A2E, human RPE lipofuscin contains numerous compounds that are structurally related to A2E as determined by their fragmentation pattern (losses of M+ -190, -174 and/or -150 amu and the formation of fragments of 592 amu). The majority consists of relatively hydrophobic components corresponding to derivatized A2E with discrete molecular weights of 800-900 m/z, 970-1080 m/z and above 1200 m/z regions. In order to determine the mechanism of these modifications, A2E was chemically modified by; 1) esterification 2) reactions with specific aldehydes and 3) allowed to spontaneously auto-oxidize. The reactions with aldehydes yielded nearly identical products as found in vivo while esterification yielded very different structures as determined mass spectrometrically.

Keywords: aging • retinal pigment epithelium • oxidation/oxidative or free radical damage 

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