Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase.
There is increasing evidence that lipid aldehydes generated endogenously during the process of degradation of lipid peroxides, are causally involved in the pathophysiology effects associated with oxidative stress. We report here that 4-hydroxynonenal (HNE), which is one of the most abundant and toxic lipid aldehyde can be efficiently detoxified by the aldo-keto reductase, aldose reductase, purified from bovine lens. The enzyme displays a Km of congruent to 9 microM for HNE and 34 microM for the glutathione adduct of HNE (HNE-GS) assigning HNE and HNE-GS to be the best natural substrates of aldose reductase known so far and exposing a new efficient detoxification route of HNE.
Srivastava
S
S
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77555-0647, USA.
Chandra
A
A
Bhatnagar
A
A
Srivastava
S K
SK
Ansari
N H
NH
D000449:Aldehyde Reductase / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D005609:Free Radicals; D005978:Glutathione / Q000378:metabolism*; D007700:Kinetics; D007908:Lens, Crystalline / Q000201:enzymology; D008054:Lipid Peroxides / Q000378:metabolism*; D013379:Substrate Specificity
D000447:Aldehydes; D005609:Free Radicals; D008054:Lipid Peroxides; D000449:Aldehyde Reductase; D005978:Glutathione; C027576:4-hydroxy-2-nonenal