Hyperoxia-induced NAD(P)H oxidase activation and regulation by MAP kinases in human lung endothelial cells
1 Division of Pulmonary and Critical Care Medicine and Division of Cardiology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore 21224; and 2 Division of Infectious Disease, University of Maryland School of Medicine, Baltimore, Maryland 21201 Hyperoxia increases reacti...
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| Veröffentlicht in: | American journal of physiology. Lung cellular and molecular physiology 2003-01, Vol.284 (1), p.26-L38 |
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| container_title | American journal of physiology. Lung cellular and molecular physiology |
| container_volume | 284 |
| creator | Parinandi, Narasimham L Kleinberg, Michael A Usatyuk, Peter V Cummings, Rhett J Pennathur, Arjun Cardounel, Arturo J Zweier, Jay L Garcia, Joe G. N Natarajan, Viswanathan |
| description | 1 Division of Pulmonary and Critical Care Medicine and
Division of Cardiology, Department of Medicine, Johns Hopkins
University School of Medicine, Baltimore 21224; and 2 Division
of Infectious Disease, University of Maryland School of Medicine,
Baltimore, Maryland 21201
Hyperoxia increases
reactive oxygen species (ROS) production in vascular endothelium;
however, the mechanisms involved in ROS generation are not well
characterized. We determined the role and regulation of NAD(P)H oxidase
in hyperoxia-induced ROS formation in human pulmonary artery
endothelial cells (HPAECs). Exposure of HPAECs to hyperoxia for 1, 3, and 12 h increased the generation of superoxide anion, which was
blocked by diphenyleneiodonium but not by rotenone or oxypurinol.
Furthermore, hyperoxia enhanced NADPH- and NADH-dependent and
superoxide dismutase- or diphenyleneiodonium-inhibitable ROS production
in HPAECs. Immunohistocytochemistry and Western blotting revealed the
presence of gp91, p67 phox, p22 phox, and p47 phox subcomponents of
NADPH oxidase in HPAECs. Transfection of HPAECs with p22 phox antisense
plasmid inhibited hyperoxia-induced ROS production. Exposure of HPAECs
to hyperoxia activated p38 MAPK and ERK, and inhibition of p38 MAPK and
MEK1/2 attenuated the hyperoxia-induced ROS generation. These results
suggest a role for MAPK in regulating hyperoxia-induced NAD(P)H oxidase activation in HPAECs.
reactive oxygen species; lung vascular endothelial cells; mitogen-activated protein kinases |
| doi_str_mv | 10.1152/ajplung.00123.2002 |
| format | Article |
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Division of Cardiology, Department of Medicine, Johns Hopkins
University School of Medicine, Baltimore 21224; and 2 Division
of Infectious Disease, University of Maryland School of Medicine,
Baltimore, Maryland 21201
Hyperoxia increases
reactive oxygen species (ROS) production in vascular endothelium;
however, the mechanisms involved in ROS generation are not well
characterized. We determined the role and regulation of NAD(P)H oxidase
in hyperoxia-induced ROS formation in human pulmonary artery
endothelial cells (HPAECs). Exposure of HPAECs to hyperoxia for 1, 3, and 12 h increased the generation of superoxide anion, which was
blocked by diphenyleneiodonium but not by rotenone or oxypurinol.
Furthermore, hyperoxia enhanced NADPH- and NADH-dependent and
superoxide dismutase- or diphenyleneiodonium-inhibitable ROS production
in HPAECs. Immunohistocytochemistry and Western blotting revealed the
presence of gp91, p67 phox, p22 phox, and p47 phox subcomponents of
NADPH oxidase in HPAECs. Transfection of HPAECs with p22 phox antisense
plasmid inhibited hyperoxia-induced ROS production. Exposure of HPAECs
to hyperoxia activated p38 MAPK and ERK, and inhibition of p38 MAPK and
MEK1/2 attenuated the hyperoxia-induced ROS generation. These results
suggest a role for MAPK in regulating hyperoxia-induced NAD(P)H oxidase activation in HPAECs.
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Division of Cardiology, Department of Medicine, Johns Hopkins
University School of Medicine, Baltimore 21224; and 2 Division
of Infectious Disease, University of Maryland School of Medicine,
Baltimore, Maryland 21201
Hyperoxia increases
reactive oxygen species (ROS) production in vascular endothelium;
however, the mechanisms involved in ROS generation are not well
characterized. We determined the role and regulation of NAD(P)H oxidase
in hyperoxia-induced ROS formation in human pulmonary artery
endothelial cells (HPAECs). Exposure of HPAECs to hyperoxia for 1, 3, and 12 h increased the generation of superoxide anion, which was
blocked by diphenyleneiodonium but not by rotenone or oxypurinol.
Furthermore, hyperoxia enhanced NADPH- and NADH-dependent and
superoxide dismutase- or diphenyleneiodonium-inhibitable ROS production
in HPAECs. Immunohistocytochemistry and Western blotting revealed the
presence of gp91, p67 phox, p22 phox, and p47 phox subcomponents of
NADPH oxidase in HPAECs. Transfection of HPAECs with p22 phox antisense
plasmid inhibited hyperoxia-induced ROS production. Exposure of HPAECs
to hyperoxia activated p38 MAPK and ERK, and inhibition of p38 MAPK and
MEK1/2 attenuated the hyperoxia-induced ROS generation. These results
suggest a role for MAPK in regulating hyperoxia-induced NAD(P)H oxidase activation in HPAECs.
reactive oxygen species; lung vascular endothelial cells; mitogen-activated protein kinases</description><subject>Antisense Elements (Genetics) - pharmacology</subject><subject>Cells, Cultured</subject><subject>Endothelium, Vascular - enzymology</subject><subject>Enzyme Activation - physiology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Humans</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Hyperoxia - enzymology</subject><subject>Hyperoxia - physiopathology</subject><subject>Membrane Transport Proteins</subject><subject>Mitogen-Activated Protein Kinases - physiology</subject><subject>NADPH Dehydrogenase - genetics</subject><subject>NADPH Oxidases - metabolism</subject><subject>NADPH Oxidases - physiology</subject><subject>Onium Compounds - pharmacology</subject><subject>Phagocytosis - physiology</subject><subject>Phosphoproteins - genetics</subject><subject>Pulmonary Artery - enzymology</subject><subject>Reactive Oxygen Species - antagonists & inhibitors</subject><subject>Reactive Oxygen Species - metabolism</subject><issn>1040-0605</issn><issn>1522-1504</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEFv1DAQhS1UREvpH-BQ-VRRiSxjx3a8x1VpWaSl7aE9W07sbLz1OmmcQPPv8bJbOHEaz_h7T08PoY8EZoRw-kVvOj-G9QyA0HxGAegbdJI-aEY4sKP0BgYZCODH6H2MGwDgAOIdOk68lLkQJ2iznDrbty9OZy6YsbIG3y6-frq_XOJ0NDparKvB_dSDawPWweDerke_X8sJ_1jc4ycXEhexC7gZtzrgXSpsg2mHxnqnPa6s9_EDeltrH-3ZYZ6ix5vrh6tltrr79v1qscoqxsmQiYoZZmwBeWmEqVhui7mRumac8zKXtOaSczGnOdB5WXAiirk2XBS1pBKAifwUXex9u759Hm0c1NbFXQIdbDtGVVApQUiWQLoHq76Nsbe16nq31f2kCKhdw-rQsPrTsNo1nETnB_ex3FrzT3KoNAFyDzRu3fxyvVVdM0XX-nY9qZvR-wf7Mrw6U8kUUSsqVGfqJP38f-lrlr-S_DeZ5Jzx</recordid><startdate>20030101</startdate><enddate>20030101</enddate><creator>Parinandi, Narasimham L</creator><creator>Kleinberg, Michael A</creator><creator>Usatyuk, Peter V</creator><creator>Cummings, Rhett J</creator><creator>Pennathur, Arjun</creator><creator>Cardounel, Arturo J</creator><creator>Zweier, Jay L</creator><creator>Garcia, Joe G. N</creator><creator>Natarajan, Viswanathan</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20030101</creationdate><title>Hyperoxia-induced NAD(P)H oxidase activation and regulation by MAP kinases in human lung endothelial cells</title><author>Parinandi, Narasimham L ; Kleinberg, Michael A ; Usatyuk, Peter V ; Cummings, Rhett J ; Pennathur, Arjun ; Cardounel, Arturo J ; Zweier, Jay L ; Garcia, Joe G. N ; Natarajan, Viswanathan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-6c4d4de703bd6dc43e79d8af4555b382f58556923029b751679ad567f82800463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Antisense Elements (Genetics) - pharmacology</topic><topic>Cells, Cultured</topic><topic>Endothelium, Vascular - enzymology</topic><topic>Enzyme Activation - physiology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Humans</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Hyperoxia - enzymology</topic><topic>Hyperoxia - physiopathology</topic><topic>Membrane Transport Proteins</topic><topic>Mitogen-Activated Protein Kinases - physiology</topic><topic>NADPH Dehydrogenase - genetics</topic><topic>NADPH Oxidases - metabolism</topic><topic>NADPH Oxidases - physiology</topic><topic>Onium Compounds - pharmacology</topic><topic>Phagocytosis - physiology</topic><topic>Phosphoproteins - genetics</topic><topic>Pulmonary Artery - enzymology</topic><topic>Reactive Oxygen Species - antagonists & inhibitors</topic><topic>Reactive Oxygen Species - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Parinandi, Narasimham L</creatorcontrib><creatorcontrib>Kleinberg, Michael A</creatorcontrib><creatorcontrib>Usatyuk, Peter V</creatorcontrib><creatorcontrib>Cummings, Rhett J</creatorcontrib><creatorcontrib>Pennathur, Arjun</creatorcontrib><creatorcontrib>Cardounel, Arturo J</creatorcontrib><creatorcontrib>Zweier, Jay L</creatorcontrib><creatorcontrib>Garcia, Joe G. 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N</au><au>Natarajan, Viswanathan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hyperoxia-induced NAD(P)H oxidase activation and regulation by MAP kinases in human lung endothelial cells</atitle><jtitle>American journal of physiology. Lung cellular and molecular physiology</jtitle><addtitle>Am J Physiol Lung Cell Mol Physiol</addtitle><date>2003-01-01</date><risdate>2003</risdate><volume>284</volume><issue>1</issue><spage>26</spage><epage>L38</epage><pages>26-L38</pages><issn>1040-0605</issn><eissn>1522-1504</eissn><abstract>1 Division of Pulmonary and Critical Care Medicine and
Division of Cardiology, Department of Medicine, Johns Hopkins
University School of Medicine, Baltimore 21224; and 2 Division
of Infectious Disease, University of Maryland School of Medicine,
Baltimore, Maryland 21201
Hyperoxia increases
reactive oxygen species (ROS) production in vascular endothelium;
however, the mechanisms involved in ROS generation are not well
characterized. We determined the role and regulation of NAD(P)H oxidase
in hyperoxia-induced ROS formation in human pulmonary artery
endothelial cells (HPAECs). Exposure of HPAECs to hyperoxia for 1, 3, and 12 h increased the generation of superoxide anion, which was
blocked by diphenyleneiodonium but not by rotenone or oxypurinol.
Furthermore, hyperoxia enhanced NADPH- and NADH-dependent and
superoxide dismutase- or diphenyleneiodonium-inhibitable ROS production
in HPAECs. Immunohistocytochemistry and Western blotting revealed the
presence of gp91, p67 phox, p22 phox, and p47 phox subcomponents of
NADPH oxidase in HPAECs. Transfection of HPAECs with p22 phox antisense
plasmid inhibited hyperoxia-induced ROS production. Exposure of HPAECs
to hyperoxia activated p38 MAPK and ERK, and inhibition of p38 MAPK and
MEK1/2 attenuated the hyperoxia-induced ROS generation. These results
suggest a role for MAPK in regulating hyperoxia-induced NAD(P)H oxidase activation in HPAECs.
reactive oxygen species; lung vascular endothelial cells; mitogen-activated protein kinases</abstract><cop>United States</cop><pmid>12388366</pmid><doi>10.1152/ajplung.00123.2002</doi><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1040-0605 |
| ispartof | American journal of physiology. Lung cellular and molecular physiology, 2003-01, Vol.284 (1), p.26-L38 |
| issn | 1040-0605 1522-1504 |
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| source | MEDLINE; American Physiological Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Antisense Elements (Genetics) - pharmacology Cells, Cultured Endothelium, Vascular - enzymology Enzyme Activation - physiology Enzyme Inhibitors - pharmacology Humans Hydrogen Peroxide - metabolism Hyperoxia - enzymology Hyperoxia - physiopathology Membrane Transport Proteins Mitogen-Activated Protein Kinases - physiology NADPH Dehydrogenase - genetics NADPH Oxidases - metabolism NADPH Oxidases - physiology Onium Compounds - pharmacology Phagocytosis - physiology Phosphoproteins - genetics Pulmonary Artery - enzymology Reactive Oxygen Species - antagonists & inhibitors Reactive Oxygen Species - metabolism |
| title | Hyperoxia-induced NAD(P)H oxidase activation and regulation by MAP kinases in human lung endothelial cells |
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