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Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Ed. by Gillery, Philippe / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Schlattmann, Peter / Tate, Jillian R.


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Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetes

4 / Kyle L. Brown1 / Sergei Chetyrkin1 / Billy Hudson1–3, ,

1Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA

2Department of Biochemistry, Vanderbilt University Medical Center, Nashville, TN, USA

3Department of Pathology, Vanderbilt University Medical Center, Nashville, TN, USA

4Division of Nephrology, Department of Medicine, Vanderbilt University Medical Center, S-3223 MCN, 1161 21st Avenue South, Nashville, TN 37232–2372, USA

Corresponding author: Dr. Paul Voziyan, Division of Nephrology, Department of Medicine, Vanderbilt University Medical Center, S-3223 MCN, 1161 21st Avenue South, Nashville, TN 37232–2372, USA, Phone: +1-615-322-3352, Fax: +1-615-343-7156, E-mail:

Citation Information: Clinical Chemistry and Laboratory Medicine. Volume 52, Issue 1, Pages 39–45, ISSN (Online) 1437-4331, ISSN (Print) 1434-6621, DOI: 10.1515/cclm-2012-0818, March 2013

Publication History

Received:
2012-11-27
Accepted:
2013-02-07
Published Online:
2013-03-13

Abstract

Non-enzymatic modification of proteins in hyperglycemia is a major proposed mechanism of diabetic complications. Specifically, advanced glycation end products (AGEs) derived from hyperglycemia-induced reactive carbonyl species (RCS) can have pathogenic consequences when they target functionally critical protein residues. Modification of a small number of these critical residues, often undetectable by the methodologies relying on measurements of total AGE levels, can cause significant functional damage. Therefore, detection of specific sites of protein damage in diabetes is central to understanding the molecular basis of diabetic complications and for identification of biomarkers which are mechanistically linked to the disease. The current paradigm of RCS-derived protein damage places a major focus on methylglyoxal (MGO), an intermediate of cellular glycolysis. We propose that glyoxal (GO) is a major contributor to extracellular matrix (ECM) damage in diabetes. Here, we review the current knowledge and provide new data about GO-derived site-specific ECM modification in experimental diabetes.

Keywords: advanced glycation end products; collagen IV; diabetes; extracellular matrix; glyoxal; mass spectrometry; methylglyoxal; pyridoxamine

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[1]
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Diabetes, 2015, Volume 64, Number 6, Page 2242
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The Scientific World Journal, 2014, Volume 2014, Page 1
[3]
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