Cellular oxidant stress mediated by advanced glycation endproducts: The role of native albumin

Ram Subramaniam, Xingjun Fan, Jianqi Yang, Chung Eun Ha, Charles E. Petersen, Nadhipuram V. Bhagavan, Miriam F. Weiss, Vincent M. Monnier

Research output: Contribution to journalArticle

Abstract

Oxidative stress induced by advanced glycation endproducts (AGE) has been implicated in the pathogenesis of diabetic complications. Oxidation of dichlorofluorescein diacetate (H2DCFH-DA) to form the fluorescent analog DCF in cells exposed to AGE proteins has been widely used as an assay for intracellular generation of reactive oxygen species (ROS). Here we show that although AGE proteins apparently enhance DCF fluorescence, the observed effect is in part due to the quenching of DCF fluorescence by native bovine serum albumin (BSA) that leaks out into the medium. Using recombinant domains of human serum albumin, we show DCF fluorescence quenching is most strongly mediated by domains II and III.

Original languageEnglish (US)
Pages (from-to)65-71
Number of pages7
JournalInternational Congress Series
Volume1245
Issue numberC
DOIs
StatePublished - Nov 1 2002
Externally publishedYes

Keywords

  • Albumin
  • Dichlorofluorescein
  • Glycation
  • Oxidant stress
  • RAW 264.7 cells

ASJC Scopus subject areas

  • Medicine(all)

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  • Cite this

    Subramaniam, R., Fan, X., Yang, J., Ha, C. E., Petersen, C. E., Bhagavan, N. V., Weiss, M. F., & Monnier, V. M. (2002). Cellular oxidant stress mediated by advanced glycation endproducts: The role of native albumin. International Congress Series, 1245(C), 65-71. https://doi.org/10.1016/S0531-5131(02)00992-5