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Diabetes, Vol 40, Issue 2 190-196, Copyright © 1991 by American Diabetes Association
Effect of diabetes and aging on carboxymethyllysine levels in human urine
KJ Knecht, JA Dunn, KF McFarland, DR McCance, TJ Lyons, SR Thorpe and JW Baynes
Department of Chemistry, University of South Carolina, Columbia 29208.
Carboxymethyllysine (CML) has been identified as a modified amino acid that
accumulates with age in human lens proteins and collagen. CML may be formed
by oxidation of fructoselysine (FL), the Amadori adduct formed on
nonenzymatic glycosylation of lysine residues in protein, or by reaction of
ascorbate with protein under autoxidizing conditions. We proposed that
measurements of tissue and urinary CML may be useful as indices of
oxidative stress or damage to proteins in vivo. To determine the extent to
which oxidation of nonenzymatically glycosylated proteins contributes to
urinary CML, we measured the urinary concentrations of FL and CML in
diabetic (n = 26) and control (n = 28) patients. The urinary concentration
of FL correlated strongly with HbA1 measurements and was significantly
higher in diabetic compared with control samples (9.2 +/- 6.5 and 4.0 +/-
2.8 micrograms/mg creatinine, respectively; P less than 0.0001). There was
also a strong correlation between the concentrations of CML and FL in both
diabetic and control urine (r = 0.67, P less than 0.0001) but only a weakly
significant increase in the CML concentration in diabetic compared with
control urine (1.2 +/- 0.5 and 1.0 +/- 0.3 micrograms/mg creatinine,
respectively; P = 0.05). The molar ratio of CML to FL was significantly
lower in diabetic compared with control patients (0.25 +/- 0.12 and 0.43
+/- 0.16, respectively; P less than 0.0001).(ABSTRACT TRUNCATED AT 250
WORDS)

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Copyright © 1991 by the American Diabetes Association.
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