Cytochrome P450 dependent metabolism of arachidonic acid in bovine corneal epithelium |
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| Authors: | M L Schwartzman N G Abraham J Masferrer M W Dunn J C McGiff |
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| Institution: | 1. Department of Pharmacology, New York Medical College, Valhalla, New York 10595 USA;2. Department of Medicine, New York Medical College, Valhalla, New York 10595 USA;3. New York Eye and Ear Infirmary, New York, New York, USA;4. Department of Pediatrics, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan;2. Center for Advanced Medicine and Clinical Research, Nagoya University Hospital, Nagoya 466-8550, Japan;11. Department of Pediatrics Kumamoto University, Kumamoto 860-8556, Japan;8. Department of Dermatology and Plastic Surgery, Faculty of Life Sciences, Kumamoto University, Kumamoto 860-8556, Japan;1. Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea;2. Graduate School of Nanoscience and Technology, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea;3. Department of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea;1. From the Department of Ophthalmology, Boston Children’s Hospital, Harvard Medical School, Boston, MA (ZF, ZS, YS, J-SJ, CGH, RZC, LPE, KT, JC, and LEHS); the Department of Ophthalmology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden (CAL and AH); the Department of Pediatrics, Institute of Clinical Sciences Lund, Lund University and Skåne University Hospital, Lund, Sweden (DL and IHP); and National Eye Institute, Division of Epidemiology and Clinical Research Clinical Trials Branch, National Eye Institute, NIH, Bethesda, MD (JPS). |
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| Abstract: | Microsomes prepared from bovine corneal epithelium metabolized 14C-arachidonic acid into two unidentified products, separated by thin-layer chromatography and called Peaks I and II. Each peak was further separated by high performance liquid chromatography into two metabolites. The formation of these metabolites was dependent on the addition of NADPH and inhibited by carbon monoxide and SKF-525A, suggesting a cytochrome P450-dependent mechanism. The presence of cytochrome P450 in the corneal epithelium was assessed directly by measurement of the carbon monoxide reduced spectrum and indirectly by measuring aryl hydrocarbon hydroxylase activity. The activity of aryl hydrocarbon hydroxylase was protein- and NADPH-dependent and was inhibited by SKF-525A. |
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