The Experts below are selected from a list of 81921 Experts worldwide ranked by ideXlab platform
Grigory G Borisenko - One of the best experts on this subject based on the ideXlab platform.
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the Cyclooxygenase site but not the peroxidase site of Cyclooxygenase 2 is required for neurotoxicity in hypoxic and ischemic injury
Journal of Neurochemistry, 2010Co-Authors: Muzamil Ahmad, Jianfei Jiang, Hao Liu, Tetsuya Nagayama, Marie E Rose, Vladimir A Tyurin, Yulia Y Tyurina, Grigory G Borisenko, Natalia A Belikova, Jun ChenAbstract:Cyclooxygenase-2 activity has been implicated in the pathogenesis of ischemic injury, but the exact mechanisms responsible for its toxicity remain unclear. Infection of primary neurons with an adenovirus expressing wild type Cyclooxygenase-2 increased the susceptibility of neurons to hypoxia. Infection with an adenoviral vector expressing Cyclooxygenase-2 with a mutation at the Cyclooxygenase site did not increase susceptibility to hypoxia, whereas overexpression of Cyclooxygenase-2 with a mutation in the peroxidase site produced similar susceptibility to hypoxia as wild type Cyclooxygenase-2. Primary neuronal cultures obtained from transgenic mice bearing a mutation in the COX-2 cylooxygenase site were protected from hypoxia. Mice with a mutation in the Cyclooxygenase site had smaller infarctions 24h after 70 min of middle cerebral artery occlusion than wild type control mice. Cyclooxygenase-2 activity had no effect on the formation of protein carbonyls. Ascorbate radicals were detected by electron paramagnetic resonance as a product of recombinant Cyclooxygenase-2 activity and were blocked by Cyclooxygenase-2 inhibitors. Similarly, formation of ascorbate radicals was inhibited in the presence of Cyclooxygenase-2 inhibitors and in homogenates obtained from Cyclooxygenase-2 null mice. Taken together, these results indicate that the Cyclooxygenase activity of Cyclooxygenase-2 is necessary to exacerbate neuronal hypoxia/ischemia injury rather than the peroxidase activity of the enzyme.
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The Cyclooxygenase site, but not the peroxidase site of Cyclooxygenase‐2 is required for neurotoxicity in hypoxic and ischemic injury
Journal of neurochemistry, 2010Co-Authors: Muzamil Ahmad, Jianfei Jiang, Hao Liu, Tetsuya Nagayama, Marie E Rose, Vladimir A Tyurin, Yulia Y Tyurina, Grigory G BorisenkoAbstract:Cyclooxygenase-2 activity has been implicated in the pathogenesis of ischemic injury, but the exact mechanisms responsible for its toxicity remain unclear. Infection of primary neurons with an adenovirus expressing wild type Cyclooxygenase-2 increased the susceptibility of neurons to hypoxia. Infection with an adenoviral vector expressing Cyclooxygenase-2 with a mutation at the Cyclooxygenase site did not increase susceptibility to hypoxia, whereas overexpression of Cyclooxygenase-2 with a mutation in the peroxidase site produced similar susceptibility to hypoxia as wild type Cyclooxygenase-2. Primary neuronal cultures obtained from transgenic mice bearing a mutation in the COX-2 cylooxygenase site were protected from hypoxia. Mice with a mutation in the Cyclooxygenase site had smaller infarctions 24h after 70 min of middle cerebral artery occlusion than wild type control mice. Cyclooxygenase-2 activity had no effect on the formation of protein carbonyls. Ascorbate radicals were detected by electron paramagnetic resonance as a product of recombinant Cyclooxygenase-2 activity and were blocked by Cyclooxygenase-2 inhibitors. Similarly, formation of ascorbate radicals was inhibited in the presence of Cyclooxygenase-2 inhibitors and in homogenates obtained from Cyclooxygenase-2 null mice. Taken together, these results indicate that the Cyclooxygenase activity of Cyclooxygenase-2 is necessary to exacerbate neuronal hypoxia/ischemia injury rather than the peroxidase activity of the enzyme.
Muzamil Ahmad - One of the best experts on this subject based on the ideXlab platform.
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the Cyclooxygenase site but not the peroxidase site of Cyclooxygenase 2 is required for neurotoxicity in hypoxic and ischemic injury
Journal of Neurochemistry, 2010Co-Authors: Muzamil Ahmad, Jianfei Jiang, Hao Liu, Tetsuya Nagayama, Marie E Rose, Vladimir A Tyurin, Yulia Y Tyurina, Grigory G Borisenko, Natalia A Belikova, Jun ChenAbstract:Cyclooxygenase-2 activity has been implicated in the pathogenesis of ischemic injury, but the exact mechanisms responsible for its toxicity remain unclear. Infection of primary neurons with an adenovirus expressing wild type Cyclooxygenase-2 increased the susceptibility of neurons to hypoxia. Infection with an adenoviral vector expressing Cyclooxygenase-2 with a mutation at the Cyclooxygenase site did not increase susceptibility to hypoxia, whereas overexpression of Cyclooxygenase-2 with a mutation in the peroxidase site produced similar susceptibility to hypoxia as wild type Cyclooxygenase-2. Primary neuronal cultures obtained from transgenic mice bearing a mutation in the COX-2 cylooxygenase site were protected from hypoxia. Mice with a mutation in the Cyclooxygenase site had smaller infarctions 24h after 70 min of middle cerebral artery occlusion than wild type control mice. Cyclooxygenase-2 activity had no effect on the formation of protein carbonyls. Ascorbate radicals were detected by electron paramagnetic resonance as a product of recombinant Cyclooxygenase-2 activity and were blocked by Cyclooxygenase-2 inhibitors. Similarly, formation of ascorbate radicals was inhibited in the presence of Cyclooxygenase-2 inhibitors and in homogenates obtained from Cyclooxygenase-2 null mice. Taken together, these results indicate that the Cyclooxygenase activity of Cyclooxygenase-2 is necessary to exacerbate neuronal hypoxia/ischemia injury rather than the peroxidase activity of the enzyme.
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The Cyclooxygenase site, but not the peroxidase site of Cyclooxygenase‐2 is required for neurotoxicity in hypoxic and ischemic injury
Journal of neurochemistry, 2010Co-Authors: Muzamil Ahmad, Jianfei Jiang, Hao Liu, Tetsuya Nagayama, Marie E Rose, Vladimir A Tyurin, Yulia Y Tyurina, Grigory G BorisenkoAbstract:Cyclooxygenase-2 activity has been implicated in the pathogenesis of ischemic injury, but the exact mechanisms responsible for its toxicity remain unclear. Infection of primary neurons with an adenovirus expressing wild type Cyclooxygenase-2 increased the susceptibility of neurons to hypoxia. Infection with an adenoviral vector expressing Cyclooxygenase-2 with a mutation at the Cyclooxygenase site did not increase susceptibility to hypoxia, whereas overexpression of Cyclooxygenase-2 with a mutation in the peroxidase site produced similar susceptibility to hypoxia as wild type Cyclooxygenase-2. Primary neuronal cultures obtained from transgenic mice bearing a mutation in the COX-2 cylooxygenase site were protected from hypoxia. Mice with a mutation in the Cyclooxygenase site had smaller infarctions 24h after 70 min of middle cerebral artery occlusion than wild type control mice. Cyclooxygenase-2 activity had no effect on the formation of protein carbonyls. Ascorbate radicals were detected by electron paramagnetic resonance as a product of recombinant Cyclooxygenase-2 activity and were blocked by Cyclooxygenase-2 inhibitors. Similarly, formation of ascorbate radicals was inhibited in the presence of Cyclooxygenase-2 inhibitors and in homogenates obtained from Cyclooxygenase-2 null mice. Taken together, these results indicate that the Cyclooxygenase activity of Cyclooxygenase-2 is necessary to exacerbate neuronal hypoxia/ischemia injury rather than the peroxidase activity of the enzyme.
Jun Chen - One of the best experts on this subject based on the ideXlab platform.
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the Cyclooxygenase site but not the peroxidase site of Cyclooxygenase 2 is required for neurotoxicity in hypoxic and ischemic injury
Journal of Neurochemistry, 2010Co-Authors: Muzamil Ahmad, Jianfei Jiang, Hao Liu, Tetsuya Nagayama, Marie E Rose, Vladimir A Tyurin, Yulia Y Tyurina, Grigory G Borisenko, Natalia A Belikova, Jun ChenAbstract:Cyclooxygenase-2 activity has been implicated in the pathogenesis of ischemic injury, but the exact mechanisms responsible for its toxicity remain unclear. Infection of primary neurons with an adenovirus expressing wild type Cyclooxygenase-2 increased the susceptibility of neurons to hypoxia. Infection with an adenoviral vector expressing Cyclooxygenase-2 with a mutation at the Cyclooxygenase site did not increase susceptibility to hypoxia, whereas overexpression of Cyclooxygenase-2 with a mutation in the peroxidase site produced similar susceptibility to hypoxia as wild type Cyclooxygenase-2. Primary neuronal cultures obtained from transgenic mice bearing a mutation in the COX-2 cylooxygenase site were protected from hypoxia. Mice with a mutation in the Cyclooxygenase site had smaller infarctions 24h after 70 min of middle cerebral artery occlusion than wild type control mice. Cyclooxygenase-2 activity had no effect on the formation of protein carbonyls. Ascorbate radicals were detected by electron paramagnetic resonance as a product of recombinant Cyclooxygenase-2 activity and were blocked by Cyclooxygenase-2 inhibitors. Similarly, formation of ascorbate radicals was inhibited in the presence of Cyclooxygenase-2 inhibitors and in homogenates obtained from Cyclooxygenase-2 null mice. Taken together, these results indicate that the Cyclooxygenase activity of Cyclooxygenase-2 is necessary to exacerbate neuronal hypoxia/ischemia injury rather than the peroxidase activity of the enzyme.
David A Lubarsky - One of the best experts on this subject based on the ideXlab platform.
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pharmacology of Cyclooxygenase 2 inhibitors and preemptive analgesia in acute pain management
Current Opinion in Anesthesiology, 2008Co-Authors: Alan D Kaye, Amir Baluch, Aaron J Kaye, Gebhard Ralf, David A LubarskyAbstract:Purpose of reviewNSAIDs have served as analgesic, antiinflammatory, and antipyretic medicines for over a century. A novel class of NSAIDs, Cyclooxygenase-2 inhibitors, was introduced in 1999. All NSAIDs and aspirin inhibit active sites of Cyclooxygenase-1 and Cyclooxygenase-2. Recent studies have de
Jianfei Jiang - One of the best experts on this subject based on the ideXlab platform.
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the Cyclooxygenase site but not the peroxidase site of Cyclooxygenase 2 is required for neurotoxicity in hypoxic and ischemic injury
Journal of Neurochemistry, 2010Co-Authors: Muzamil Ahmad, Jianfei Jiang, Hao Liu, Tetsuya Nagayama, Marie E Rose, Vladimir A Tyurin, Yulia Y Tyurina, Grigory G Borisenko, Natalia A Belikova, Jun ChenAbstract:Cyclooxygenase-2 activity has been implicated in the pathogenesis of ischemic injury, but the exact mechanisms responsible for its toxicity remain unclear. Infection of primary neurons with an adenovirus expressing wild type Cyclooxygenase-2 increased the susceptibility of neurons to hypoxia. Infection with an adenoviral vector expressing Cyclooxygenase-2 with a mutation at the Cyclooxygenase site did not increase susceptibility to hypoxia, whereas overexpression of Cyclooxygenase-2 with a mutation in the peroxidase site produced similar susceptibility to hypoxia as wild type Cyclooxygenase-2. Primary neuronal cultures obtained from transgenic mice bearing a mutation in the COX-2 cylooxygenase site were protected from hypoxia. Mice with a mutation in the Cyclooxygenase site had smaller infarctions 24h after 70 min of middle cerebral artery occlusion than wild type control mice. Cyclooxygenase-2 activity had no effect on the formation of protein carbonyls. Ascorbate radicals were detected by electron paramagnetic resonance as a product of recombinant Cyclooxygenase-2 activity and were blocked by Cyclooxygenase-2 inhibitors. Similarly, formation of ascorbate radicals was inhibited in the presence of Cyclooxygenase-2 inhibitors and in homogenates obtained from Cyclooxygenase-2 null mice. Taken together, these results indicate that the Cyclooxygenase activity of Cyclooxygenase-2 is necessary to exacerbate neuronal hypoxia/ischemia injury rather than the peroxidase activity of the enzyme.
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The Cyclooxygenase site, but not the peroxidase site of Cyclooxygenase‐2 is required for neurotoxicity in hypoxic and ischemic injury
Journal of neurochemistry, 2010Co-Authors: Muzamil Ahmad, Jianfei Jiang, Hao Liu, Tetsuya Nagayama, Marie E Rose, Vladimir A Tyurin, Yulia Y Tyurina, Grigory G BorisenkoAbstract:Cyclooxygenase-2 activity has been implicated in the pathogenesis of ischemic injury, but the exact mechanisms responsible for its toxicity remain unclear. Infection of primary neurons with an adenovirus expressing wild type Cyclooxygenase-2 increased the susceptibility of neurons to hypoxia. Infection with an adenoviral vector expressing Cyclooxygenase-2 with a mutation at the Cyclooxygenase site did not increase susceptibility to hypoxia, whereas overexpression of Cyclooxygenase-2 with a mutation in the peroxidase site produced similar susceptibility to hypoxia as wild type Cyclooxygenase-2. Primary neuronal cultures obtained from transgenic mice bearing a mutation in the COX-2 cylooxygenase site were protected from hypoxia. Mice with a mutation in the Cyclooxygenase site had smaller infarctions 24h after 70 min of middle cerebral artery occlusion than wild type control mice. Cyclooxygenase-2 activity had no effect on the formation of protein carbonyls. Ascorbate radicals were detected by electron paramagnetic resonance as a product of recombinant Cyclooxygenase-2 activity and were blocked by Cyclooxygenase-2 inhibitors. Similarly, formation of ascorbate radicals was inhibited in the presence of Cyclooxygenase-2 inhibitors and in homogenates obtained from Cyclooxygenase-2 null mice. Taken together, these results indicate that the Cyclooxygenase activity of Cyclooxygenase-2 is necessary to exacerbate neuronal hypoxia/ischemia injury rather than the peroxidase activity of the enzyme.
