Saposin B Binds the Lipofuscin Bisretinoid A2E and Prevents its Enzymatic and Photooxidation

Jay Tinklepaugh, Britannia M. Smith, Yan Nie, Kelsey Moody, Kris Grohn, Fadi Bou-Abdallah, Robert P. Doyle

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Vitamin A based bisretinoid accumulation is a major focus in the study of macular degeneration. Whether specific endogenous lysosomal proteins can bind A2E, a pronounced bisretinoid in lipofuscin granules in retinal pigment epithelial cells, and interfere with enzymatic or photoinduced oxidation of such, has not been explored. Herein, using fluorescence and electronic absorption spectroscopy and mass spectrometry, we demonstrate that Saposin B, a critical protein in the degradation of sulfatides and “flushing” of lipids, can bind A2E, preventing its H2O2-dependent enzymatic oxidation by horseradish peroxidase and photooxidation by blue light (λ=450–460 nm).

Original languageEnglish (US)
Pages (from-to)256-259
Number of pages4
JournalChemPhotoChem
Volume1
Issue number6
DOIs
StatePublished - Jun 1 2017

Keywords

  • bisretinoids
  • enzymatic oxidation
  • macular degeneration
  • photooxidation
  • saposin B

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Analytical Chemistry

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    Tinklepaugh, J., Smith, B. M., Nie, Y., Moody, K., Grohn, K., Bou-Abdallah, F., & Doyle, R. P. (2017). Saposin B Binds the Lipofuscin Bisretinoid A2E and Prevents its Enzymatic and Photooxidation. ChemPhotoChem, 1(6), 256-259. https://doi.org/10.1002/cptc.201700039