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Glyceraldehyde metabolism in human erythrocytes in comparison with that of glucose and dihydroxyacetone
Author(s) -
Taguchi Tadao,
Murase Shigeki,
Miwa Ichitomo
Publication year - 2002
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.952
Subject(s) - glyceraldehyde , dihydroxyacetone , glyceric acid , dihydroxyacetone phosphate , aldose reductase , biochemistry , lactate dehydrogenase , metabolism , glycerol , dehydrogenase , glycolysis , glyceraldehyde 3 phosphate dehydrogenase , chemistry , carbohydrate metabolism , sorbinil , aldehyde reductase , fructose , polyol pathway , biology , enzyme , aldose reductase inhibitor
Metabolism of D ‐glyceraldehyde in human erythrocytes in comparison with that of glucose and dihydroxyacetone was studied. Both trioses were metabolized to produce L ‐lactate at rates comparable to that of L ‐lactate formation from glucose. Almost complete inactivation of glyceraldehyde‐3‐phosphate dehydrogenase by treatment of cells with iodoacetate resulted in a 95% decrease in L ‐lactate formation from the ketotriose as well as from glucose, whereas L ‐lactate formation from the aldotriose was only partially reduced (60%). D ‐Lactate was produced faster from either the aldotriose or the ketotriose than from glucose, but the ability of the two trioses to produce D ‐lactate was far lower than that to produce L ‐lactate. Almost complete inhibition of aldehyde dehydrogenase by disulfiram and of both aldose reductase and aldehyde reductase II by sorbinil, had no effect on L ‐lactate formation from D ‐glyceraldehyde. The present study suggests that D ‐glyceraldehyde is metabolized via two or more pathways including the glycolytic pathway after its phosphorylation by triokinase, and that neither oxidation to D ‐glyceric acid nor reduction to glycerol is a prerequisite for D ‐glyceraldehyde metabolism. Copyright © 2002 John Wiley & Sons, Ltd.