Free radical generation by early glycation products

A mechanism for accelerated atherogenesis in diabetes

Cathleen J. Mullarkey, Diane Edelstein, Michael Brownlee

Research output: Contribution to journalArticle

607 Citations (Scopus)

Abstract

Non-enzymatic glycation of reactive amino groups in model proteins increased the rate of free radical production at physiologic pH by nearly fifty-fold over non-glycated protein. Superoxide generation was confirmed by electron paramagnetic resonance measurements with the spin-trap phenyl-t-butyl-nitrone. Both Schiff base and Amadori glycation products were found to generate free radicals in a ratio of 1:1.5. Free radicals generated by glycated protein increased peroxidation of membranes of linoleic/arachidonic acid vesicles nearly 2-fold over control, suggesting that the increased glycation of proteins in diabetes may accelerate vascular wall lipid oxidative modification.

Original languageEnglish (US)
Pages (from-to)932-939
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume173
Issue number3
DOIs
StatePublished - Dec 31 1990
Externally publishedYes

Fingerprint

Medical problems
Free Radicals
Atherosclerosis
Proteins
Schiff Bases
Electron Spin Resonance Spectroscopy
Linoleic Acid
Arachidonic Acid
Superoxides
Paramagnetic resonance
Blood Vessels
Membranes
Lipids

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Free radical generation by early glycation products : A mechanism for accelerated atherogenesis in diabetes. / Mullarkey, Cathleen J.; Edelstein, Diane; Brownlee, Michael.

In: Biochemical and Biophysical Research Communications, Vol. 173, No. 3, 31.12.1990, p. 932-939.

Research output: Contribution to journalArticle

Mullarkey, Cathleen J. ; Edelstein, Diane ; Brownlee, Michael. / Free radical generation by early glycation products : A mechanism for accelerated atherogenesis in diabetes. In: Biochemical and Biophysical Research Communications. 1990 ; Vol. 173, No. 3. pp. 932-939.
@article{834f6a77859b40b88d1bea6c52d4584c,
title = "Free radical generation by early glycation products: A mechanism for accelerated atherogenesis in diabetes",
abstract = "Non-enzymatic glycation of reactive amino groups in model proteins increased the rate of free radical production at physiologic pH by nearly fifty-fold over non-glycated protein. Superoxide generation was confirmed by electron paramagnetic resonance measurements with the spin-trap phenyl-t-butyl-nitrone. Both Schiff base and Amadori glycation products were found to generate free radicals in a ratio of 1:1.5. Free radicals generated by glycated protein increased peroxidation of membranes of linoleic/arachidonic acid vesicles nearly 2-fold over control, suggesting that the increased glycation of proteins in diabetes may accelerate vascular wall lipid oxidative modification.",
author = "Mullarkey, {Cathleen J.} and Diane Edelstein and Michael Brownlee",
year = "1990",
month = "12",
day = "31",
doi = "10.1016/S0006-291X(05)80875-7",
language = "English (US)",
volume = "173",
pages = "932--939",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Free radical generation by early glycation products

T2 - A mechanism for accelerated atherogenesis in diabetes

AU - Mullarkey, Cathleen J.

AU - Edelstein, Diane

AU - Brownlee, Michael

PY - 1990/12/31

Y1 - 1990/12/31

N2 - Non-enzymatic glycation of reactive amino groups in model proteins increased the rate of free radical production at physiologic pH by nearly fifty-fold over non-glycated protein. Superoxide generation was confirmed by electron paramagnetic resonance measurements with the spin-trap phenyl-t-butyl-nitrone. Both Schiff base and Amadori glycation products were found to generate free radicals in a ratio of 1:1.5. Free radicals generated by glycated protein increased peroxidation of membranes of linoleic/arachidonic acid vesicles nearly 2-fold over control, suggesting that the increased glycation of proteins in diabetes may accelerate vascular wall lipid oxidative modification.

AB - Non-enzymatic glycation of reactive amino groups in model proteins increased the rate of free radical production at physiologic pH by nearly fifty-fold over non-glycated protein. Superoxide generation was confirmed by electron paramagnetic resonance measurements with the spin-trap phenyl-t-butyl-nitrone. Both Schiff base and Amadori glycation products were found to generate free radicals in a ratio of 1:1.5. Free radicals generated by glycated protein increased peroxidation of membranes of linoleic/arachidonic acid vesicles nearly 2-fold over control, suggesting that the increased glycation of proteins in diabetes may accelerate vascular wall lipid oxidative modification.

UR - http://www.scopus.com/inward/record.url?scp=0025540553&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025540553&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(05)80875-7

DO - 10.1016/S0006-291X(05)80875-7

M3 - Article

VL - 173

SP - 932

EP - 939

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -