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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 / Payne, Deborah A. / Schlattmann, Peter / Tate, Jillian R.

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1437-4331
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Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetes

Paul Voziyan
  • Division of Nephrology, Department of Medicine, Vanderbilt University Medical Center, S-3223 MCN, 1161 21st Avenue South, Nashville, TN 37232–2372, USA
  • :
/ Kyle L. Brown
  • Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA
/ Sergei Chetyrkin
  • Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA
/ Billy Hudson
  • Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA
  • Department of Biochemistry, Vanderbilt University Medical Center, Nashville, TN, USA
  • Department of Pathology, Vanderbilt University Medical Center, Nashville, TN, USA
Published Online: 2013-03-13 | DOI: https://doi.org/10.1515/cclm-2012-0818

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

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:


Received: 2012-11-27

Accepted: 2013-02-07

Published Online: 2013-03-13

Published in Print: 2014-01-01


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

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[1]
Kyle L. Brown, Carl Darris, Kristie Lindsey Rose, Otto A. Sanchez, Hartman Madu, Josh Avance, Nickolas Brooks, Ming-Zhi Zhang, Agnes Fogo, Raymond Harris, Billy G. Hudson, and Paul Voziyan
Diabetes, 2015, Volume 64, Number 6, Page 2242
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Halyna M. Semchyshyn
The Scientific World Journal, 2014, Volume 2014, Page 1
[3]
Helen Vlassara and Gary E. Striker
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