TY - JOUR
T1 - Lipid peroxidation product, 4-Hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase
AU - Srivastava, Sanjay
AU - Chandra, Animesh
AU - Bhatnagar, Aruni
AU - Srivastava, Satish K.
AU - Ansari, Naseem H.
PY - 1995/12/26
Y1 - 1995/12/26
N2 - 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 ≃ 9 μM for HNE and 34 μM 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.
AB - 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 ≃ 9 μM for HNE and 34 μM 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.
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U2 - 10.1006/bbrc.1995.2835
DO - 10.1006/bbrc.1995.2835
M3 - Article
C2 - 8554593
AN - SCOPUS:0029562272
SN - 0006-291X
VL - 217
SP - 741
EP - 746
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -