Lipid Peroxidation Product, 4-Hydroxynonenal and Its Conjugate with GSH Are Excellent Substrates of Bovine Lens Aldose Reductase

S. Srivastava, A. Chandra, A. Bhatnagar, Satish Srivastava, Naseem Ansari

Research output: Contribution to journalArticle

152 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)741-746
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume217
Issue number3
DOIs
StatePublished - Dec 26 1995

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Aldehyde Reductase
Lipid Peroxidation
Lenses
Lipids
Substrates
Aldehydes
Detoxification
Oxidative stress
Lipid Peroxides
Poisons
4-hydroxy-2-nonenal
Glutathione
Oxidative Stress
Degradation
Enzymes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology
  • Biophysics
  • Biochemistry

Cite this

Lipid Peroxidation Product, 4-Hydroxynonenal and Its Conjugate with GSH Are Excellent Substrates of Bovine Lens Aldose Reductase. / Srivastava, S.; Chandra, A.; Bhatnagar, A.; Srivastava, Satish; Ansari, Naseem.

In: Biochemical and Biophysical Research Communications, Vol. 217, No. 3, 26.12.1995, p. 741-746.

Research output: Contribution to journalArticle

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