The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Veronique Jubiermaurin - One of the best experts on this subject based on the ideXlab platform.
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different roles of the two high oxygen affinity terminal Oxidases of brucella suis cytochrome c Oxidase but not ubiquinol Oxidase is required for persistence in mice
Infection and Immunity, 2007Co-Authors: María Pilar Jiménez De Bagüés, Jean-pierre Liautard, Severine Loiselmeyer, Veronique JubiermaurinAbstract:The survival of Brucella suis mutant strains in mice demonstrated different roles of the two high-oxygen-affinity terminal Oxidases. The cbb3-type cytochrome c Oxidase was essential for chronic infection in oxygen-deficient organs. Lack of the cytochrome bd ubiquinol Oxidase led to hypervirulence of bacteria, which could rely on nitrite accumulation inhibiting the inducible nitric oxide synthase of the host.
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differential use of the two high oxygen affinity terminal Oxidases of brucella suis for in vitro and intramacrophagic multiplication
Infection and Immunity, 2005Co-Authors: Severine Loiselmeyer, Jean-pierre Liautard, Stephan Köhler, María Pilar Jiménez De Bagüés, Veronique JubiermaurinAbstract:Expression of the high-oxygen-affinity cytochrome cbb3 and cytochrome bd ubiquinol Oxidases of Brucella suis was studied in vitro and in the intramacrophagic niche, which was previously proposed to be oxygen limited. The cytochrome cbb3 Oxidase was exclusively expressed in vitro, whereas the cytochrome bd Oxidase was preferentially used inside macrophages and contributed to intracellular bacterial replication.
Severine Loiselmeyer - One of the best experts on this subject based on the ideXlab platform.
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different roles of the two high oxygen affinity terminal Oxidases of brucella suis cytochrome c Oxidase but not ubiquinol Oxidase is required for persistence in mice
Infection and Immunity, 2007Co-Authors: María Pilar Jiménez De Bagüés, Jean-pierre Liautard, Severine Loiselmeyer, Veronique JubiermaurinAbstract:The survival of Brucella suis mutant strains in mice demonstrated different roles of the two high-oxygen-affinity terminal Oxidases. The cbb3-type cytochrome c Oxidase was essential for chronic infection in oxygen-deficient organs. Lack of the cytochrome bd ubiquinol Oxidase led to hypervirulence of bacteria, which could rely on nitrite accumulation inhibiting the inducible nitric oxide synthase of the host.
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differential use of the two high oxygen affinity terminal Oxidases of brucella suis for in vitro and intramacrophagic multiplication
Infection and Immunity, 2005Co-Authors: Severine Loiselmeyer, Jean-pierre Liautard, Stephan Köhler, María Pilar Jiménez De Bagüés, Veronique JubiermaurinAbstract:Expression of the high-oxygen-affinity cytochrome cbb3 and cytochrome bd ubiquinol Oxidases of Brucella suis was studied in vitro and in the intramacrophagic niche, which was previously proposed to be oxygen limited. The cytochrome cbb3 Oxidase was exclusively expressed in vitro, whereas the cytochrome bd Oxidase was preferentially used inside macrophages and contributed to intracellular bacterial replication.
Jean-pierre Liautard - One of the best experts on this subject based on the ideXlab platform.
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different roles of the two high oxygen affinity terminal Oxidases of brucella suis cytochrome c Oxidase but not ubiquinol Oxidase is required for persistence in mice
Infection and Immunity, 2007Co-Authors: María Pilar Jiménez De Bagüés, Jean-pierre Liautard, Severine Loiselmeyer, Veronique JubiermaurinAbstract:The survival of Brucella suis mutant strains in mice demonstrated different roles of the two high-oxygen-affinity terminal Oxidases. The cbb3-type cytochrome c Oxidase was essential for chronic infection in oxygen-deficient organs. Lack of the cytochrome bd ubiquinol Oxidase led to hypervirulence of bacteria, which could rely on nitrite accumulation inhibiting the inducible nitric oxide synthase of the host.
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differential use of the two high oxygen affinity terminal Oxidases of brucella suis for in vitro and intramacrophagic multiplication
Infection and Immunity, 2005Co-Authors: Severine Loiselmeyer, Jean-pierre Liautard, Stephan Köhler, María Pilar Jiménez De Bagüés, Veronique JubiermaurinAbstract:Expression of the high-oxygen-affinity cytochrome cbb3 and cytochrome bd ubiquinol Oxidases of Brucella suis was studied in vitro and in the intramacrophagic niche, which was previously proposed to be oxygen limited. The cytochrome cbb3 Oxidase was exclusively expressed in vitro, whereas the cytochrome bd Oxidase was preferentially used inside macrophages and contributed to intracellular bacterial replication.
Kathy K Griendling - One of the best experts on this subject based on the ideXlab platform.
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combating oxidative stress in vascular disease nadph Oxidases as therapeutic targets
Nature Reviews Drug Discovery, 2011Co-Authors: Grant R Drummond, Stavros Selemidis, Kathy K Griendling, Christopher G SobeyAbstract:NADPH Oxidases are a family of enzymes that generate reactive oxygen species (ROS). The NOX1 (NADPH Oxidase 1) and NOX2 Oxidases are the major sources of ROS in the artery wall in conditions such as hypertension, hypercholesterolaemia, diabetes and ageing, and so they are important contributors to the oxidative stress, endothelial dysfunction and vascular inflammation that underlies arterial remodelling and atherogenesis. In this Review, we advance the concept that compared to the use of conventional antioxidants, inhibiting NOX1 and NOX2 Oxidases is a superior approach for combating oxidative stress. We briefly describe some common and emerging putative NADPH Oxidase inhibitors. In addition, we highlight the crucial role of the NADPH Oxidase regulatory subunit, p47phox, in the activity of vascular NOX1 and NOX2 Oxidases, and suggest how a better understanding of its specific molecular interactions may enable the development of novel isoform-selective drugs to prevent or treat cardiovascular diseases.
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the vascular nad p h Oxidases as therapeutic targets in cardiovascular diseases
Trends in Pharmacological Sciences, 2003Co-Authors: Hua Cai, Kathy K Griendling, David G HarrisonAbstract:Abstract Activation of vascular NAD(P)H Oxidases and the production of reactive oxygen species (ROS) by these enzyme systems are common in cardiovascular disease. In the past several years, a new family of NAD(P)H Oxidase subunits, known as the non-phagocytic NAD(P)H Oxidase (NOX) proteins, have been discovered and shown to play a role in vascular tissues. Recent studies make clearer the mechanisms of activation of the endothelial and vascular smooth muscle NAD(P)H Oxidases. ROS produced following angiotensin II-mediated stimulation of NAD(P)H Oxidases signal through pathways such as mitogen-activated protein kinases, tyrosine kinases and transcription factors, and lead to events such as inflammation, hypertrophy, remodeling and angiogenesis. Studies in mice that are deficient in p47 phox and gp91 phox (also known as NOX2) NAD(P)H Oxidase subunits show that ROS produced by these Oxidases contribute to cardiovascular diseases including atherosclerosis and hypertension. Recently, efforts have been devoted to developing inhibitors of NAD(P)H Oxidases that will provide useful experimental tools and might have therapeutic potential in the treatment of human diseases.
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angiotensin ii stimulates nadh and nadph Oxidase activity in cultured vascular smooth muscle cells
Circulation Research, 1994Co-Authors: Kathy K Griendling, C A Minieri, J D Ollerenshaw, R W AlexanderAbstract:The signaling pathways involved in the long-term metabolic effects of angiotensin II (Ang II) in vascular smooth muscle cells are incompletely understood but include the generation of molecules likely to affect Oxidase activity. We examined the ability of Ang II to stimulate superoxide anion formation and investigated the identity of the Oxidases responsible for its production. Treatment of vascular smooth muscle cells with Ang II for 4 to 6 hours caused a 2.7 +/- 0.4-fold increase in intracellular superoxide anion formation as detected by lucigenin assay. This superoxide appeared to result from activation of both the NADPH and NADH Oxidases. NADPH Oxidase activity increased from 3.23 +/- 0.61 to 11.80 +/- 1.72 nmol O2-/min per milligram protein after 4 hours of Ang II, whereas NADH Oxidase activity increased from 16.76 +/- 2.13 to 45.00 +/- 4.57 nmol O2-/min per milligram protein. The NADPH Oxidase activity was stimulated by exogenous phosphatidic and arachidonic acids and was partially inhibited by the ...
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angiotensin ii stimulates nadh and nadph Oxidase activity in cultured vascular smooth muscle cells
Circulation Research, 1994Co-Authors: Kathy K Griendling, C A Minieri, J D Ollerenshaw, R W AlexanderAbstract:The signaling pathways involved in the long-term metabolic effects of angiotensin II (Ang II) in vascular smooth muscle cells are incompletely understood but include the generation of molecules likely to affect Oxidase activity. We examined the ability of Ang II to stimulate superoxide anion formation and investigated the identity of the Oxidases responsible for its production. Treatment of vascular smooth muscle cells with Ang II for 4 to 6 hours caused a 2.7 +/- 0.4-fold increase in intracellular superoxide anion formation as detected by lucigenin assay. This superoxide appeared to result from activation of both the NADPH and NADH Oxidases. NADPH Oxidase activity increased from 3.23 +/- 0.61 to 11.80 +/- 1.72 nmol O2-/min per milligram protein after 4 hours of Ang II, whereas NADH Oxidase activity increased from 16.76 +/- 2.13 to 45.00 +/- 4.57 nmol O2-/min per milligram protein. The NADPH Oxidase activity was stimulated by exogenous phosphatidic and arachidonic acids and was partially inhibited by the specific inhibitor diphenylene iodinium. NADH Oxidase activity was increased by arachidonic and linoleic acids, was insensitive to exogenous phosphatidic acid, and was inhibited by high concentrations of quinacrine. Both of these Oxidases appear to reside in the plasma membrane, on the basis of migration of the activity after cellular fractionation and their apparent insensitivity to the mitochondrial poison KCN. These observations suggest that Ang II specifically activates enzyme systems that promote superoxide generation and raise the possibility that these pathways function as second messengers for long-term responses, such as hypertrophy or hyperplasia.
María Pilar Jiménez De Bagüés - One of the best experts on this subject based on the ideXlab platform.
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different roles of the two high oxygen affinity terminal Oxidases of brucella suis cytochrome c Oxidase but not ubiquinol Oxidase is required for persistence in mice
Infection and Immunity, 2007Co-Authors: María Pilar Jiménez De Bagüés, Jean-pierre Liautard, Severine Loiselmeyer, Veronique JubiermaurinAbstract:The survival of Brucella suis mutant strains in mice demonstrated different roles of the two high-oxygen-affinity terminal Oxidases. The cbb3-type cytochrome c Oxidase was essential for chronic infection in oxygen-deficient organs. Lack of the cytochrome bd ubiquinol Oxidase led to hypervirulence of bacteria, which could rely on nitrite accumulation inhibiting the inducible nitric oxide synthase of the host.
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differential use of the two high oxygen affinity terminal Oxidases of brucella suis for in vitro and intramacrophagic multiplication
Infection and Immunity, 2005Co-Authors: Severine Loiselmeyer, Jean-pierre Liautard, Stephan Köhler, María Pilar Jiménez De Bagüés, Veronique JubiermaurinAbstract:Expression of the high-oxygen-affinity cytochrome cbb3 and cytochrome bd ubiquinol Oxidases of Brucella suis was studied in vitro and in the intramacrophagic niche, which was previously proposed to be oxygen limited. The cytochrome cbb3 Oxidase was exclusively expressed in vitro, whereas the cytochrome bd Oxidase was preferentially used inside macrophages and contributed to intracellular bacterial replication.
