Lipid peroxidation product, 4-Hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase

Sanjay Srivastava; Animesh Chandra; Aruni Bhatnagar; Satish K. Srivastava; Naseem H. Ansari

doi:10.1006/bbrc.1995.2835

Lipid peroxidation product, 4-Hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase

Sanjay Srivastava, Animesh Chandra, Aruni Bhatnagar, Satish K. Srivastava, Naseem H. Ansari

Research output: Contribution to journal › Article › peer-review

170 Scopus citations

Abstract

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 K_m 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.

Original language	English (US)
Pages (from-to)	741-746
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	217
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1995.2835
State	Published - Dec 26 1995
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Lipid peroxidation product, 4-Hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase",

abstract = "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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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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Lipid peroxidation product, 4-Hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase

Abstract

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