The Experts below are selected from a list of 138 Experts worldwide ranked by ideXlab platform
Allan D Butterfield - One of the best experts on this subject based on the ideXlab platform.
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Increased Protein Oxidation and Decreased Creatine Kinase BB Expression and Activity after Spinal
2013Co-Authors: Cord Contusion Injury, Allan D Butterfield, Marina Aksenova, Shu-xin Zhang, Mark Underwood, James W. GeddesAbstract:Traumatic injury to the spinal cord triggers several secondary effects, including oxidative stress and compromised energy metabolism, which play a major role in biochemical and pathological changes in spinal cord tissue. Free radical generation and lipid peroxidation have been shown to be early events subsequent to spinal cord injury. In the present study, we demonstrated that protein oxidation increases in rat spinal cord tissue after experimental injury. As early as 1 h after injury, the level of protein carbonyls at the injury epicenter was significantly higher than in control (169%, p, 0.05) and increased gradually over the next 4 weeks to 1260 % of control level. Both caudal and rostral parts of the injured spinal cord demonstrated a mild increase of protein carbonyls by 4 weeks postinjury (135–138%, p, 0.05). Immunocytochemical analysis of protein carbonyls in the spinal cord cross-sections showed increased protein carbonyl immunoreactivity in the epicenter section compared to rostral and caudal sections of the same animal or control laminectomy animals. Increased protein carbonyl formation in damaged spinal cord tissue was associated with changes in activity and expression of an oxidative sensitive enzyme, Creatine Kinase BB, which plays an important role in the maintenance of ATP level in the CNS tissue. Damage to CK function in the CNS may severely aggravate the impairment of energy metabolism. The results of our study indicate that events associated with oxidative damage are triggered immediately after spinal cord trauma but continue to occur over the subsequent 4 weeks. These results suggest that antioxidant therapeutic strategies may be beneficial to lessen the consequences of the injury and potentially improve the restoration of neurological function. Key words: Creatine Kinase; oxidative stress; protein oxidation; spinal cord injur
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proteomic identification of oxidatively modified proteins in alzheimer s disease brain part i Creatine Kinase BB glutamine synthase and ubiquitin carboxy terminal hydrolase l 1
Free Radical Biology and Medicine, 2002Co-Authors: Alessandra Castegna, Michael Y Aksenov, Marina V Aksenova, Visith Thongboonkerd, Jon B Klein, William M Pierce, Rosemarie M Booze, William R Markesbery, Allan D ButterfieldAbstract:Abstract Oxidative alterations of proteins by reactive oxygen species (ROS) have been implicated in the progression of aging and age-related neurodegenerative disorders such as Alzheimer’s disease (AD). Protein carbonyls, a marker of protein oxidation, are increased in AD brain, indicating that oxidative modification of proteins is relevant in AD. Oxidative damage can lead to several events such as loss in specific protein function, abnormal protein clearance, depletion of the cellular redox-balance and interference with the cell cycle, and, ultimately, to neuronal death. Identification of specific targets of protein oxidation represents a crucial step in establishing a relationship between oxidative modification and neuronal death in AD, and was partially achieved previously in our laboratory through immunochemical detection of Creatine Kinase BB and β-actin as specifically oxidized proteins in AD brain versus control brain. However, this process is laborious, requires the availability of specific antibodies, and, most importantly, requires a reasonable guess as to the identity of the protein in the first place. In this study, we present the first proteomics approach to identify specifically oxidized proteins in AD, by coupling 2D fingerprinting with immunological detection of carbonyls and identification of proteins by mass spectrometry. The powerful techniques, emerging from application of proteomics to neurodegenerative disease, reveal the presence of specific targets of protein oxidation in Alzheimer’s disease (AD) brain: Creatine Kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. These results are discussed with reference to potential involvement of these oxidatively modified proteins in neurodegeneration in AD brain. Proteomics offers a rapid means of identifying oxidatively modified proteins in aging and age-related neurodegenerative disorders without the limitations of the immunochemical detection method.
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proteomic identification of oxidatively modified proteins in alzheimer s disease brain part i Creatine Kinase BB glutamine synthase and ubiquitin carboxy terminal hydrolase l 1
Free Radical Biology and Medicine, 2002Co-Authors: Alessandra Castegna, Michael Y Aksenov, Marina V Aksenova, Visith Thongboonkerd, Jon B Klein, William M Pierce, Rosemarie M Booze, William R Markesbery, Allan D ButterfieldAbstract:Oxidative alterations of proteins by reactive oxygen species (ROS) have been implicated in the progression of aging and age-related neurodegenerative disorders such as Alzheimer's disease (AD). Protein carbonyls, a marker of protein oxidation, are increased in AD brain, indicating that oxidative modification of proteins is relevant in AD. Oxidative damage can lead to several events such as loss in specific protein function, abnormal protein clearance, depletion of the cellular redox-balance and interference with the cell cycle, and, ultimately, to neuronal death. Identification of specific targets of protein oxidation represents a crucial step in establishing a relationship between oxidative modification and neuronal death in AD, and was partially achieved previously in our laboratory through immunochemical detection of Creatine Kinase BB and beta-actin as specifically oxidized proteins in AD brain versus control brain. However, this process is laborious, requires the availability of specific antibodies, and, most importantly, requires a reasonable guess as to the identity of the protein in the first place. In this study, we present the first proteomics approach to identify specifically oxidized proteins in AD, by coupling 2D fingerprinting with immunological detection of carbonyls and identification of proteins by mass spectrometry. The powerful techniques, emerging from application of proteomics to neurodegenerative disease, reveal the presence of specific targets of protein oxidation in Alzheimer's disease (AD) brain: Creatine Kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. These results are discussed with reference to potential involvement of these oxidatively modified proteins in neurodegeneration in AD brain. Proteomics offers a rapid means of identifying oxidatively modified proteins in aging and age-related neurodegenerative disorders without the limitations of the immunochemical detection method.
Alessandra Castegna - One of the best experts on this subject based on the ideXlab platform.
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proteomic identification of oxidatively modified proteins in alzheimer s disease brain part i Creatine Kinase BB glutamine synthase and ubiquitin carboxy terminal hydrolase l 1
Free Radical Biology and Medicine, 2002Co-Authors: Alessandra Castegna, Michael Y Aksenov, Marina V Aksenova, Visith Thongboonkerd, Jon B Klein, William M Pierce, Rosemarie M Booze, William R Markesbery, Allan D ButterfieldAbstract:Abstract Oxidative alterations of proteins by reactive oxygen species (ROS) have been implicated in the progression of aging and age-related neurodegenerative disorders such as Alzheimer’s disease (AD). Protein carbonyls, a marker of protein oxidation, are increased in AD brain, indicating that oxidative modification of proteins is relevant in AD. Oxidative damage can lead to several events such as loss in specific protein function, abnormal protein clearance, depletion of the cellular redox-balance and interference with the cell cycle, and, ultimately, to neuronal death. Identification of specific targets of protein oxidation represents a crucial step in establishing a relationship between oxidative modification and neuronal death in AD, and was partially achieved previously in our laboratory through immunochemical detection of Creatine Kinase BB and β-actin as specifically oxidized proteins in AD brain versus control brain. However, this process is laborious, requires the availability of specific antibodies, and, most importantly, requires a reasonable guess as to the identity of the protein in the first place. In this study, we present the first proteomics approach to identify specifically oxidized proteins in AD, by coupling 2D fingerprinting with immunological detection of carbonyls and identification of proteins by mass spectrometry. The powerful techniques, emerging from application of proteomics to neurodegenerative disease, reveal the presence of specific targets of protein oxidation in Alzheimer’s disease (AD) brain: Creatine Kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. These results are discussed with reference to potential involvement of these oxidatively modified proteins in neurodegeneration in AD brain. Proteomics offers a rapid means of identifying oxidatively modified proteins in aging and age-related neurodegenerative disorders without the limitations of the immunochemical detection method.
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proteomic identification of oxidatively modified proteins in alzheimer s disease brain part i Creatine Kinase BB glutamine synthase and ubiquitin carboxy terminal hydrolase l 1
Free Radical Biology and Medicine, 2002Co-Authors: Alessandra Castegna, Michael Y Aksenov, Marina V Aksenova, Visith Thongboonkerd, Jon B Klein, William M Pierce, Rosemarie M Booze, William R Markesbery, Allan D ButterfieldAbstract:Oxidative alterations of proteins by reactive oxygen species (ROS) have been implicated in the progression of aging and age-related neurodegenerative disorders such as Alzheimer's disease (AD). Protein carbonyls, a marker of protein oxidation, are increased in AD brain, indicating that oxidative modification of proteins is relevant in AD. Oxidative damage can lead to several events such as loss in specific protein function, abnormal protein clearance, depletion of the cellular redox-balance and interference with the cell cycle, and, ultimately, to neuronal death. Identification of specific targets of protein oxidation represents a crucial step in establishing a relationship between oxidative modification and neuronal death in AD, and was partially achieved previously in our laboratory through immunochemical detection of Creatine Kinase BB and beta-actin as specifically oxidized proteins in AD brain versus control brain. However, this process is laborious, requires the availability of specific antibodies, and, most importantly, requires a reasonable guess as to the identity of the protein in the first place. In this study, we present the first proteomics approach to identify specifically oxidized proteins in AD, by coupling 2D fingerprinting with immunological detection of carbonyls and identification of proteins by mass spectrometry. The powerful techniques, emerging from application of proteomics to neurodegenerative disease, reveal the presence of specific targets of protein oxidation in Alzheimer's disease (AD) brain: Creatine Kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. These results are discussed with reference to potential involvement of these oxidatively modified proteins in neurodegeneration in AD brain. Proteomics offers a rapid means of identifying oxidatively modified proteins in aging and age-related neurodegenerative disorders without the limitations of the immunochemical detection method.
Lars G Svensson - One of the best experts on this subject based on the ideXlab platform.
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brain protection via cerebral retrograde perfusion during aortic arch aneurysm repair
The Annals of Thoracic Surgery, 1993Co-Authors: Hazim J Safi, Heather W Brien, Jeffrey N Winter, Angela C Thomas, Robert L Maulsby, Harold K Doerr, Lars G SvenssonAbstract:Abstract Eleven patients underwent resection and graft replacement of ascending and aortic arch aneurysms. Retrograde cerebral perfusion was used during the procedures to minimize cerebral ischemia. Retrograde cerebral perfusion (15 ° to 24 °C) was administered through the superior vena cava. The mean cerebral ischemic time was 35 minutes (range, 11 to 71 minutes). Throughout retrograde cerebral perfusion, blood samples were drawn from the innominate and left carotid arteries at 1, 5, and every 10 minutes thereafter for analysis of arterial oxygen content, total Creatine Kinase level, and Creatine Kinase BB fraction. All patients survived. All except 1 awoke neurologically intact. In this patient, electroencephalogram and transcranial Doppler studies conducted before circulatory arrest were consistent with embolic phenomena. There was no significant difference between the current group's intraoperative electroencephalograms and those of a similar historical group. Postoperative complications included transient renal failure, myasthenia gravis, cholecystitis, premature atrial contractions, atrial fibrillation, and vocal cord paralysis. The Creatine Kinase BB fraction range was 1.8 to 13.4. The increase of total Creatine Kinase level was due to MM fraction. Retrograde cerebral perfusion during circulatory arrest is a valuable adjunct for protecting the brain. The Creatine Kinase BB band was not a good marker to detect brain injury. With continued use of this technique and accumulation of a larger series, we may better define the role of retrograde cerebral perfusion in brain protection.
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Brain protection via cerebral retrograde perfusion during aortic arch aneurysm repair.
The Annals of thoracic surgery, 1993Co-Authors: Hazim J Safi, Heather W Brien, Jeffrey N Winter, Angela C Thomas, Robert L Maulsby, Harold K Doerr, Lars G SvenssonAbstract:Eleven patients underwent resection and graft replacement of ascending and aortic arch aneurysms. Retrograde cerebral perfusion was used during the procedures to minimize cerebral ischemia. Retrograde cerebral perfusion (15 degrees to 24 degrees C) was administered through the superior vena cava. The mean cerebral ischemic time was .35 minutes (range, 11 to 71 minutes). Throughout retrograde cerebral perfusion, blood samples were drawn from the innominate and left carotid arteries at 1, 5, and every 10 minutes thereafter for analysis of arterial oxygen content, total Creatine Kinase level, and Creatine Kinase BB fraction. All patients survived. All except 1 awoke neurologically intact. In this patient, electroencephalogram and transcranial Doppler studies conducted before circulatory arrest were consistent with embolic phenomena. There was no significant difference between the current group's intraoperative electroencephalograms and those of a similar historical group. Postoperative complications included transient renal failure, myasthenia gravis, cholecystitis, premature atrial contractions, atrial fibrillation, and vocal cord paralysis. The Creatine Kinase BB fraction range was 1.8 to 13.4. The increase of total Creatine Kinase level was due to MM fraction. Retrograde cerebral perfusion during circulatory arrest is a valuable adjunct for protecting the brain. The Creatine Kinase BB band was not a good marker to detect brain injury. With continued use of this technique and accumulation of a larger series, we may better define the role of retrograde cerebral perfusion in brain protection.
E. Simmonds - One of the best experts on this subject based on the ideXlab platform.
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first day serum Creatine Kinase BB isoenzyme in high risk infants
European Journal of Pediatrics, 1991Co-Authors: R. A. Primhak, E. SimmondsAbstract:Serum Creatine Kinase BB (CK-BB) on the 1st day of life was measured by radioimmunoassay in 37 very low birth weight (VLBW) infats, 14 severely asphyxiated infants and 24 controls. The 31 survivors from the two high-risk groups were followed up for 12 months or more. VLBW non-survivors (n=14) had significantly higher mean CK-BB levels than survivors (n=23), (P<0.05). However, if only survivors were considered, CK-BB was a poor discriminator of outcome in either study group. First day serum CK-BB is not a useful predictor of neurodevelopmental outcome in surviving high-risk infants.
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First day serum Creatine Kinase BB isoenzyme in high-risk infants.
European journal of pediatrics, 1991Co-Authors: R. A. Primhak, E. SimmondsAbstract:Serum Creatine Kinase BB (CK-BB) on the 1st day of life was measured by radioimmunoassay in 37 very low birth weight (VLBW) infats, 14 severely asphyxiated infants and 24 controls. The 31 survivors from the two high-risk groups were followed up for 12 months or more. VLBW non-survivors (n=14) had significantly higher mean CK-BB levels than survivors (n=23), (P
Michael Y Aksenov - One of the best experts on this subject based on the ideXlab platform.
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proteomic identification of oxidatively modified proteins in alzheimer s disease brain part i Creatine Kinase BB glutamine synthase and ubiquitin carboxy terminal hydrolase l 1
Free Radical Biology and Medicine, 2002Co-Authors: Alessandra Castegna, Michael Y Aksenov, Marina V Aksenova, Visith Thongboonkerd, Jon B Klein, William M Pierce, Rosemarie M Booze, William R Markesbery, Allan D ButterfieldAbstract:Abstract Oxidative alterations of proteins by reactive oxygen species (ROS) have been implicated in the progression of aging and age-related neurodegenerative disorders such as Alzheimer’s disease (AD). Protein carbonyls, a marker of protein oxidation, are increased in AD brain, indicating that oxidative modification of proteins is relevant in AD. Oxidative damage can lead to several events such as loss in specific protein function, abnormal protein clearance, depletion of the cellular redox-balance and interference with the cell cycle, and, ultimately, to neuronal death. Identification of specific targets of protein oxidation represents a crucial step in establishing a relationship between oxidative modification and neuronal death in AD, and was partially achieved previously in our laboratory through immunochemical detection of Creatine Kinase BB and β-actin as specifically oxidized proteins in AD brain versus control brain. However, this process is laborious, requires the availability of specific antibodies, and, most importantly, requires a reasonable guess as to the identity of the protein in the first place. In this study, we present the first proteomics approach to identify specifically oxidized proteins in AD, by coupling 2D fingerprinting with immunological detection of carbonyls and identification of proteins by mass spectrometry. The powerful techniques, emerging from application of proteomics to neurodegenerative disease, reveal the presence of specific targets of protein oxidation in Alzheimer’s disease (AD) brain: Creatine Kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. These results are discussed with reference to potential involvement of these oxidatively modified proteins in neurodegeneration in AD brain. Proteomics offers a rapid means of identifying oxidatively modified proteins in aging and age-related neurodegenerative disorders without the limitations of the immunochemical detection method.
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proteomic identification of oxidatively modified proteins in alzheimer s disease brain part i Creatine Kinase BB glutamine synthase and ubiquitin carboxy terminal hydrolase l 1
Free Radical Biology and Medicine, 2002Co-Authors: Alessandra Castegna, Michael Y Aksenov, Marina V Aksenova, Visith Thongboonkerd, Jon B Klein, William M Pierce, Rosemarie M Booze, William R Markesbery, Allan D ButterfieldAbstract:Oxidative alterations of proteins by reactive oxygen species (ROS) have been implicated in the progression of aging and age-related neurodegenerative disorders such as Alzheimer's disease (AD). Protein carbonyls, a marker of protein oxidation, are increased in AD brain, indicating that oxidative modification of proteins is relevant in AD. Oxidative damage can lead to several events such as loss in specific protein function, abnormal protein clearance, depletion of the cellular redox-balance and interference with the cell cycle, and, ultimately, to neuronal death. Identification of specific targets of protein oxidation represents a crucial step in establishing a relationship between oxidative modification and neuronal death in AD, and was partially achieved previously in our laboratory through immunochemical detection of Creatine Kinase BB and beta-actin as specifically oxidized proteins in AD brain versus control brain. However, this process is laborious, requires the availability of specific antibodies, and, most importantly, requires a reasonable guess as to the identity of the protein in the first place. In this study, we present the first proteomics approach to identify specifically oxidized proteins in AD, by coupling 2D fingerprinting with immunological detection of carbonyls and identification of proteins by mass spectrometry. The powerful techniques, emerging from application of proteomics to neurodegenerative disease, reveal the presence of specific targets of protein oxidation in Alzheimer's disease (AD) brain: Creatine Kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. These results are discussed with reference to potential involvement of these oxidatively modified proteins in neurodegeneration in AD brain. Proteomics offers a rapid means of identifying oxidatively modified proteins in aging and age-related neurodegenerative disorders without the limitations of the immunochemical detection method.