Studies on L-threose as substrate for aldose reductase: A possible role in preventing protein glycation

doi:10.1007/BF00420914

Studies on L-threose as substrate for aldose reductase: A possible role in preventing protein glycation

Published Jun 21, 1996 · Palaniyandi S Devamanoharan, S. Varma

Molecular and Cellular Biochemistry

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Abstract

L-threose is a product of ascorbate oxidation and degradation. By virtue of its free aldehyde group it can form Schiff-bases with tissue proteins, altering their normal function. In this study, we have examined the possibility of its detoxification to L-threitol by aldose reductase in the lens. The rat lens enzyme present in fresh homogenate as well as after 100 fold purification was found to utilize L-threose with a km of 7.1 × 10−4 M. The specificity of the reaction was affirmed by its inhibition with sorbinil and quercetin, the well known aldose reductase inhibitors. Further studies on the role of this enzyme in preventing toxicity due to degradation products of ascorbate are in progress.

In Vitro Study

Study Snapshot

Key takeawayAldose reductase in the rat lens can detoxify L-threose, potentially preventing protein glycation and toxicity due to ascorbate degradation products.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Studies on L-threose as substrate for aldose reductase: A possible role in preventing protein glycation

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