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

doi:10.1016/S0531-5131(02)00992-5

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	65-71
Number of pages	7
Journal	International Congress Series
Volume	1245
Issue number	C
DOIs	https://doi.org/10.1016/S0531-5131(02)00992-5
State	Published - Nov 1 2002
Externally published	Yes

Keywords

Albumin
Dichlorofluorescein
Glycation
Oxidant stress
RAW 264.7 cells

ASJC Scopus subject areas

Medicine(all)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/S0531-5131(02)00992-5

Cite this

@article{990502fbc0ea4f5980aa1f2d40c396db,

title = "Cellular oxidant stress mediated by advanced glycation endproducts: The role of native albumin",

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.",

keywords = "Albumin, Dichlorofluorescein, Glycation, Oxidant stress, RAW 264.7 cells",

author = "Ram Subramaniam and Xingjun Fan and Jianqi Yang and Ha, {Chung Eun} and Petersen, {Charles E.} and Bhagavan, {Nadhipuram V.} and Weiss, {Miriam F.} and Monnier, {Vincent M.}",

year = "2002",

month = nov,

day = "1",

doi = "10.1016/S0531-5131(02)00992-5",

language = "English (US)",

volume = "1245",

pages = "65--71",

journal = "International Congress Series",

issn = "0531-5131",

publisher = "Elsevier BV",

number = "C",

}

TY - JOUR

T1 - Cellular oxidant stress mediated by advanced glycation endproducts

T2 - The role of native albumin

AU - Subramaniam, Ram

AU - Fan, Xingjun

AU - Yang, Jianqi

AU - Ha, Chung Eun

AU - Petersen, Charles E.

AU - Bhagavan, Nadhipuram V.

AU - Weiss, Miriam F.

AU - Monnier, Vincent M.

PY - 2002/11/1

Y1 - 2002/11/1

N2 - 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.

AB - 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.

KW - Albumin

KW - Dichlorofluorescein

KW - Glycation

KW - Oxidant stress

KW - RAW 264.7 cells

UR - http://www.scopus.com/inward/record.url?scp=85023003039&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85023003039&partnerID=8YFLogxK

U2 - 10.1016/S0531-5131(02)00992-5

DO - 10.1016/S0531-5131(02)00992-5

M3 - Article

AN - SCOPUS:85023003039

SN - 0531-5131

VL - 1245

SP - 65

EP - 71

JO - International Congress Series

JF - International Congress Series

IS - C

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this