Regulation of cyclooxygenase and 12-lipoxygenase catalysis by phospholipid hydroperoxide glutathione peroxidase in A431 cells

C. J. Chen, H. S. Huang, S. B. Lin, W. C. Chang

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Regulation of arachidonate metabolism in human epidermoid carcinoma A431 cells by phospholipid hydroperoxide glutathione peroxidase (PHGPx) and cytosolic glutathione peroxidase (GPx1) was studied. In order to study the effect of reduced glutathione (GSH) on the catalysis regulation of these oxygenation enzymes, diethyl maleate was used to deplete the intracellular GSH. In the presence of 13-hydroperoxyoctadecadienoic acid, the enzymatic catalysis of cyclooxygenase and 12-lipoxygenase was significantly increased in the GSH-depleted cells. In terms of the inhibitory effect on 12-lipoxygenase, PHGPx was more sensitive to GSH concentrations than GPx1. Inhibition of PHGPx activity by the treatment of cells with antisense oligonucleotide of PHGPx mRNA increased the enzymatic catalysis of both cyclooxygenase and 12-lipoxygenase. In conclusion, the results indicate that catalysis of cyclooxygenase and 12-lipoxygenase in A431 cells was regulated by redox-reaction, and PHGPx seems to play an important role in the controlling of these reactions. (C) 2000 Harcourt Publishers Ltd.

Original languageEnglish
Pages (from-to)261-268
Number of pages8
JournalProstaglandins Leukotrienes and Essential Fatty Acids
Volume62
Issue number4
DOIs
Publication statusPublished - Apr 2000
Externally publishedYes

Fingerprint

phospholipid-hydroperoxide glutathione peroxidase
Arachidonate 12-Lipoxygenase
Prostaglandin-Endoperoxide Synthases
Catalysis
diethyl maleate
Oxygenation
Antisense Oligonucleotides
Redox reactions
Glutathione Peroxidase
Metabolism
Oxidation-Reduction
Glutathione
Squamous Cell Carcinoma
Cells
Messenger RNA
Acids

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Endocrinology, Diabetes and Metabolism

Cite this

Regulation of cyclooxygenase and 12-lipoxygenase catalysis by phospholipid hydroperoxide glutathione peroxidase in A431 cells. / Chen, C. J.; Huang, H. S.; Lin, S. B.; Chang, W. C.

In: Prostaglandins Leukotrienes and Essential Fatty Acids, Vol. 62, No. 4, 04.2000, p. 261-268.

Research output: Contribution to journalArticle

@article{f38251f9cf6646f6a7cf1e01c6a15ecf,
title = "Regulation of cyclooxygenase and 12-lipoxygenase catalysis by phospholipid hydroperoxide glutathione peroxidase in A431 cells",
abstract = "Regulation of arachidonate metabolism in human epidermoid carcinoma A431 cells by phospholipid hydroperoxide glutathione peroxidase (PHGPx) and cytosolic glutathione peroxidase (GPx1) was studied. In order to study the effect of reduced glutathione (GSH) on the catalysis regulation of these oxygenation enzymes, diethyl maleate was used to deplete the intracellular GSH. In the presence of 13-hydroperoxyoctadecadienoic acid, the enzymatic catalysis of cyclooxygenase and 12-lipoxygenase was significantly increased in the GSH-depleted cells. In terms of the inhibitory effect on 12-lipoxygenase, PHGPx was more sensitive to GSH concentrations than GPx1. Inhibition of PHGPx activity by the treatment of cells with antisense oligonucleotide of PHGPx mRNA increased the enzymatic catalysis of both cyclooxygenase and 12-lipoxygenase. In conclusion, the results indicate that catalysis of cyclooxygenase and 12-lipoxygenase in A431 cells was regulated by redox-reaction, and PHGPx seems to play an important role in the controlling of these reactions. (C) 2000 Harcourt Publishers Ltd.",
author = "Chen, {C. J.} and Huang, {H. S.} and Lin, {S. B.} and Chang, {W. C.}",
year = "2000",
month = "4",
doi = "10.1054/plef.2000.0153",
language = "English",
volume = "62",
pages = "261--268",
journal = "Prostaglandins Leukotrienes and Essential Fatty Acids",
issn = "0952-3278",
publisher = "Churchill Livingstone",
number = "4",

}

TY - JOUR

T1 - Regulation of cyclooxygenase and 12-lipoxygenase catalysis by phospholipid hydroperoxide glutathione peroxidase in A431 cells

AU - Chen, C. J.

AU - Huang, H. S.

AU - Lin, S. B.

AU - Chang, W. C.

PY - 2000/4

Y1 - 2000/4

N2 - Regulation of arachidonate metabolism in human epidermoid carcinoma A431 cells by phospholipid hydroperoxide glutathione peroxidase (PHGPx) and cytosolic glutathione peroxidase (GPx1) was studied. In order to study the effect of reduced glutathione (GSH) on the catalysis regulation of these oxygenation enzymes, diethyl maleate was used to deplete the intracellular GSH. In the presence of 13-hydroperoxyoctadecadienoic acid, the enzymatic catalysis of cyclooxygenase and 12-lipoxygenase was significantly increased in the GSH-depleted cells. In terms of the inhibitory effect on 12-lipoxygenase, PHGPx was more sensitive to GSH concentrations than GPx1. Inhibition of PHGPx activity by the treatment of cells with antisense oligonucleotide of PHGPx mRNA increased the enzymatic catalysis of both cyclooxygenase and 12-lipoxygenase. In conclusion, the results indicate that catalysis of cyclooxygenase and 12-lipoxygenase in A431 cells was regulated by redox-reaction, and PHGPx seems to play an important role in the controlling of these reactions. (C) 2000 Harcourt Publishers Ltd.

AB - Regulation of arachidonate metabolism in human epidermoid carcinoma A431 cells by phospholipid hydroperoxide glutathione peroxidase (PHGPx) and cytosolic glutathione peroxidase (GPx1) was studied. In order to study the effect of reduced glutathione (GSH) on the catalysis regulation of these oxygenation enzymes, diethyl maleate was used to deplete the intracellular GSH. In the presence of 13-hydroperoxyoctadecadienoic acid, the enzymatic catalysis of cyclooxygenase and 12-lipoxygenase was significantly increased in the GSH-depleted cells. In terms of the inhibitory effect on 12-lipoxygenase, PHGPx was more sensitive to GSH concentrations than GPx1. Inhibition of PHGPx activity by the treatment of cells with antisense oligonucleotide of PHGPx mRNA increased the enzymatic catalysis of both cyclooxygenase and 12-lipoxygenase. In conclusion, the results indicate that catalysis of cyclooxygenase and 12-lipoxygenase in A431 cells was regulated by redox-reaction, and PHGPx seems to play an important role in the controlling of these reactions. (C) 2000 Harcourt Publishers Ltd.

UR - http://www.scopus.com/inward/record.url?scp=0034095722&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034095722&partnerID=8YFLogxK

U2 - 10.1054/plef.2000.0153

DO - 10.1054/plef.2000.0153

M3 - Article

C2 - 10882192

AN - SCOPUS:0034095722

VL - 62

SP - 261

EP - 268

JO - Prostaglandins Leukotrienes and Essential Fatty Acids

JF - Prostaglandins Leukotrienes and Essential Fatty Acids

SN - 0952-3278

IS - 4

ER -