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Carnosine prevents the glycation‐induced changes in electrophoretic mobility of aspartate aminotransferase

Carnosine prevents the glycation‐induced changes in electrophoretic mobility of aspartate... Carbohydrate‐derived aldehydes cause irreversible loss of protein function via glycation. We previously observed that glyceraldehyde 3‐phosphate (Glyc3P) abolishes the enzyme activity of cardiac aspartate aminotransferase (cAAT). We also examined the protective effects of carnosine against Glyc3P‐induced loss of enzyme activity. The present study looked at carnosine’s prevention of Glyc3P‐induced change in protein structure. Purified cAAT (2 mg protein/mL) was incubated with various concentrations of carnosine (1–20 mM) in the presence of Glyc3P (500 μM) for 4 days at 37ºC. Following incubation, samples were analyzed by SDS‐polyacrylamide gel electrophoresis. Carnosine showed prevention of protein modification at carnosine‐to‐Glyc3P ratios of 10:1 or greater. There was a progressive loss of the unmodified cAAT protein band as Glyc3P concentration was increased. Additionally, the gel position of the Glyc3P‐modified cAAT protein varied over time. The apparent molecular weight (MWapp) of the Glyc3P‐modified cAAT protein that formed after 1 day at 37ºC (500 μM) was greater than its MWapp after 2 days, suggesting that a chemical rearrangement of the initial adduct occurs. These observations support the hypothesis that carnosine is an antiglycation agent and that its mechanism of action involves prevention of protein modification. © 2000 John Wiley & Sons, Inc. J Biochem Toxicol 14:215–220, 2000 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Biochemical and Molecular Toxicology (Formerly Journal of Biochemical Toxicology) Wiley

Carnosine prevents the glycation‐induced changes in electrophoretic mobility of aspartate aminotransferase

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References (18)

Publisher
Wiley
Copyright
Copyright © 2000 John Wiley & Sons, Inc.
ISSN
1095-6670
eISSN
1099-0461
DOI
10.1002/(SICI)1099-0461(2000)14:4<215::AID-JBT6>3.0.CO;2-Z
Publisher site
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Abstract

Carbohydrate‐derived aldehydes cause irreversible loss of protein function via glycation. We previously observed that glyceraldehyde 3‐phosphate (Glyc3P) abolishes the enzyme activity of cardiac aspartate aminotransferase (cAAT). We also examined the protective effects of carnosine against Glyc3P‐induced loss of enzyme activity. The present study looked at carnosine’s prevention of Glyc3P‐induced change in protein structure. Purified cAAT (2 mg protein/mL) was incubated with various concentrations of carnosine (1–20 mM) in the presence of Glyc3P (500 μM) for 4 days at 37ºC. Following incubation, samples were analyzed by SDS‐polyacrylamide gel electrophoresis. Carnosine showed prevention of protein modification at carnosine‐to‐Glyc3P ratios of 10:1 or greater. There was a progressive loss of the unmodified cAAT protein band as Glyc3P concentration was increased. Additionally, the gel position of the Glyc3P‐modified cAAT protein varied over time. The apparent molecular weight (MWapp) of the Glyc3P‐modified cAAT protein that formed after 1 day at 37ºC (500 μM) was greater than its MWapp after 2 days, suggesting that a chemical rearrangement of the initial adduct occurs. These observations support the hypothesis that carnosine is an antiglycation agent and that its mechanism of action involves prevention of protein modification. © 2000 John Wiley & Sons, Inc. J Biochem Toxicol 14:215–220, 2000

Journal

Journal of Biochemical and Molecular Toxicology (Formerly Journal of Biochemical Toxicology) – Wiley

Published: Jan 1, 2000

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