Identification of a lipoxygenase inhibitor in A431 cells as a phospholipid hydroperoxide glutathione peroxidase

FEBS Letters
H S HuangW C Chang

Abstract

An endogenous lipoxygenase inhibitor, purified from the cytosol of human epidermoid carcinoma A431 cells, was analyzed by N-terminal microsequencing and mass spectrometric analysis. The inhibitor was purified by SDS-PAGE, then subjected to in-gel CNBr cleavage and trypsin digestion. The N-terminal sequence data obtained from a 6-8 kDa band of in-gel CNBr cleavage and the three isolated peptides of in-gel trypsin digestion, and the C-terminal peptide sequence from matrix-assisted laser desorption ionization mass spectrometry matched the sequence of human phospholipid hydroperoxide glutathione peroxidase. The purified inhibitor exhibited peroxidase activity using phosphatidylcholine hydroperoxides as the substrate. We therefore concluded that the lipoxygenase inhibitor present in A431 cells was a phospholipid hydroperoxide glutathione peroxidase.

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Citations

Aug 14, 1999·International Journal of Cancer. Journal International Du Cancer·S NigamS Yamamoto
Nov 16, 2002·Prostaglandins & Other Lipid Mediators·Olof Rådmark
Jul 11, 2002·Free Radical Biology & Medicine·Hartmut Kühn, Astrid Borchert
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May 24, 2005·Biochemical Pharmacology·Oliver Werz, Dieter Steinhilber
Sep 6, 2003·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Ching-Jiunn ChenWen-Chang Chang
Oct 20, 2018·Frontiers in Pharmacology·Cong LiLuhua Lai
Jul 6, 2000·Prostaglandins, Leukotrienes, and Essential Fatty Acids·C J ChenW C Chang

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