The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Arie B Vaandrager - One of the best experts on this subject based on the ideXlab platform.
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equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
Molecular Genetics and Metabolism, 2007Co-Authors: C M Westermann, J. P. Koeman, Monique G M De Sainvan Der Velden, Johannes H Van Der Kolk, Ruud Berger, I D Wijnberg, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B VaandragerAbstract:Two horses (a 7-year-old Groninger warmblood gelding and a six-month-old Trakehner mare) with pathologically confirmed rhabdomyolysis were diagnosed as suffering from multiple acyl-CoA dehydrogenase deficiency (MADD). This disorder has not been recognised in animals before. Clinical signs of both horses were a stiff, insecure gait, myoglobinuria, and finally recumbency. Urine, plasma, and muscle tissues were investigated. Analysis of plasma showed hyperglycemia, lactic acidemia, increased activity of muscle enzymes (ASAT, LDH, CK), and impaired kidney function (increased urea and creatinine). The most remarkable findings of organic acids in urine of both horses were increased lactic acid, ethylmalonic acid (EMA), 2-methylsuccinic acid, butyrylglycine (iso)valerylglycine, and hexanoylglycine. EMA was also increased in plasma of both animals. Furthermore, the profile of acylcarnitines in plasma from both animals showed a substantial elevation of C4-, C5-, C6-, C8-, and C5-DC-carnitine. Concentrations of acylcarnitines in urine of both animals revealed increased excretions of C2-, C3-, C4-, C5-, C6-, C5-OH-, C8-, C10:1-, C10-, and C5-DC-carnitine. In addition, concentrations of free carnitine were also increased. Quantitative biochemical measurement of enzyme activities in muscle tissue showed deficiencies of short-chain acyl-CoA dehydrogenase (SCAD), medium-chain acyl-CoA dehydrogenase (MCAD), and isovaleryl-CoA dehydrogenase (IVD) also indicating MADD. Histology revealed extensive rhabdomyolysis with microvesicular lipidosis predominantly in type 1 muscle fibers and mitochondrial damage. However, the ETF and ETF-QO activities were within normal limits indicating the metabolic disorder to be acquired rather than inherited. To our knowledge, these are the first cases of biochemical MADD reported in equine medicine.
Jeff Th. M. De Hosson - One of the best experts on this subject based on the ideXlab platform.
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Microstructural characterization of Co-based coating deposited by low power pulse laser cladding
Journal of Materials Science, 2013Co-Authors: A. Farnia, F. Malek Ghaini, V. Ocelík, Jeff Th. M. De HossonAbstract:A detailed microstructural study of Stellite 6 coating deposited on a low carbon ferritic steel substrate using preplaced powder method and low power Nd:YAG pulse laser is performed. The grain structure and solidification texture of the coating are investigated by orientation imaging microscopy (OIM) and scanning electron microscopy. In addition, the effect of consecutive pulses on the microstructure of the coating is examined. The orientation relationship (OR) at coating/substrate interface and the solid state phase transformation in heat-affected zone are studied as well as the Vickers microhardness profile measurement in order to support the microstructural observations. An important conclusion is reached that the shape of solidification front during pulsed laser cladding is similar to the shape of solidification front during continuous cladding with a doubled laser beam scanning speed. Further, OIM reveals the Greninger–Troiano OR between the face centered cubic coating and bcc substrate grains. It is concluded that at the moment of solidification epitaxial growth of the grains in the coating occur on the austenitic grains of the substrate and that an austenite–ferrite transformation occurs in the heat-affected zone upon subsequent cooling.
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Microstructure and properties of laser clad coatings studied by orientation imaging microscopy
Acta Materialia, 2010Co-Authors: Vaclav Ocelik, Ivan Furar, Jeff Th. M. De HossonAbstract:In this work orientation imaging microscopy (OIM), based on electron backscatter diffraction in scanning electron microscopy, was employed to examine in detail the relationship between laser cladding processing parameters and he properties and the microstructure of single and overlapping laser tracks. The study was performed on thick (similar to 1 mm) Co-based coatings prepared by 2 kW Nd:YAG laser cladding a 42CrMo4 steel substrate using different laser beam scanning speeds (1.0-15 mm s(-1)). It was found that the directional growth of individual primary grains led to the formation of a typical solidification fiber texture. The dependence of this texture on the processing speed and the shape of the solidification front were investigated in detail. Strong epitaxial growth of Co grains on austenitic steel substrate grains was found, which did not depend on the laser beam scanning velocity. During laser cladding a strong temperature gradient exists just below the coating-substrate interface that promotes the formation of a Greninger-Troiano orientation relationship between martensitic plates and the original austenitic grain inside the heat affected zone: {1 1 1}(gamma) approximate to 1 degrees to {1 1 0}(alpha) and ((1) over bar 2 (1) over bar)(gamma) approximate to 2 degrees to (1 (1) over bar 0)(alpha). Relatively drastic changes in grain size at the internal coating interfaces did not exhibit sharp changes in microhardness. (C) 2010 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
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Microstructure and properties of laser clad coatings studied by orientation imaging microscopy
2010Co-Authors: Ocelík V., Furár I., Jeff Th. M. De HossonAbstract:In this work orientation imaging microscopy (OIM), based on electron backscatter diffraction in scanning electron microscopy, was employed to examine in detail the relationship between laser cladding processing parameters and he properties and the microstructure of single and overlapping laser tracks. The study was performed on thick (~1 mm) Co-based coatings prepared by 2 kW Nd:YAG laser cladding a 42CrMo4 steel substrate using different laser beam scanning speeds (1.0–15 mm s–1). It was found that the directional growth of individual primary grains led to the formation of a typical solidification fiber texture. The dependence of this texture on the processing speed and the shape of the solidification front were investigated in detail. Strong epitaxial growth of Co grains on austenitic steel substrate grains was found, which did not depend on the laser beam scanning velocity. During laser cladding a strong temperature gradient exists just below the coating–substrate interface that promotes the formation of a Greninger–Troiano orientation relationship between martensitic plates and the original austenitic grain inside the heat affected zone: {1 1 1}γ ≈ 1° to {1 1 0}α and γ ≈ 2° to α. Relatively drastic changes in grain size at the internal coating interfaces did not exhibit sharp changes in microhardness.
C M Westermann - One of the best experts on this subject based on the ideXlab platform.
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equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
Molecular Genetics and Metabolism, 2007Co-Authors: C M Westermann, J. P. Koeman, Monique G M De Sainvan Der Velden, Johannes H Van Der Kolk, Ruud Berger, I D Wijnberg, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B VaandragerAbstract:Two horses (a 7-year-old Groninger warmblood gelding and a six-month-old Trakehner mare) with pathologically confirmed rhabdomyolysis were diagnosed as suffering from multiple acyl-CoA dehydrogenase deficiency (MADD). This disorder has not been recognised in animals before. Clinical signs of both horses were a stiff, insecure gait, myoglobinuria, and finally recumbency. Urine, plasma, and muscle tissues were investigated. Analysis of plasma showed hyperglycemia, lactic acidemia, increased activity of muscle enzymes (ASAT, LDH, CK), and impaired kidney function (increased urea and creatinine). The most remarkable findings of organic acids in urine of both horses were increased lactic acid, ethylmalonic acid (EMA), 2-methylsuccinic acid, butyrylglycine (iso)valerylglycine, and hexanoylglycine. EMA was also increased in plasma of both animals. Furthermore, the profile of acylcarnitines in plasma from both animals showed a substantial elevation of C4-, C5-, C6-, C8-, and C5-DC-carnitine. Concentrations of acylcarnitines in urine of both animals revealed increased excretions of C2-, C3-, C4-, C5-, C6-, C5-OH-, C8-, C10:1-, C10-, and C5-DC-carnitine. In addition, concentrations of free carnitine were also increased. Quantitative biochemical measurement of enzyme activities in muscle tissue showed deficiencies of short-chain acyl-CoA dehydrogenase (SCAD), medium-chain acyl-CoA dehydrogenase (MCAD), and isovaleryl-CoA dehydrogenase (IVD) also indicating MADD. Histology revealed extensive rhabdomyolysis with microvesicular lipidosis predominantly in type 1 muscle fibers and mitochondrial damage. However, the ETF and ETF-QO activities were within normal limits indicating the metabolic disorder to be acquired rather than inherited. To our knowledge, these are the first cases of biochemical MADD reported in equine medicine.
Johannes A Lenstra - One of the best experts on this subject based on the ideXlab platform.
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equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
Molecular Genetics and Metabolism, 2007Co-Authors: C M Westermann, J. P. Koeman, Monique G M De Sainvan Der Velden, Johannes H Van Der Kolk, Ruud Berger, I D Wijnberg, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B VaandragerAbstract:Two horses (a 7-year-old Groninger warmblood gelding and a six-month-old Trakehner mare) with pathologically confirmed rhabdomyolysis were diagnosed as suffering from multiple acyl-CoA dehydrogenase deficiency (MADD). This disorder has not been recognised in animals before. Clinical signs of both horses were a stiff, insecure gait, myoglobinuria, and finally recumbency. Urine, plasma, and muscle tissues were investigated. Analysis of plasma showed hyperglycemia, lactic acidemia, increased activity of muscle enzymes (ASAT, LDH, CK), and impaired kidney function (increased urea and creatinine). The most remarkable findings of organic acids in urine of both horses were increased lactic acid, ethylmalonic acid (EMA), 2-methylsuccinic acid, butyrylglycine (iso)valerylglycine, and hexanoylglycine. EMA was also increased in plasma of both animals. Furthermore, the profile of acylcarnitines in plasma from both animals showed a substantial elevation of C4-, C5-, C6-, C8-, and C5-DC-carnitine. Concentrations of acylcarnitines in urine of both animals revealed increased excretions of C2-, C3-, C4-, C5-, C6-, C5-OH-, C8-, C10:1-, C10-, and C5-DC-carnitine. In addition, concentrations of free carnitine were also increased. Quantitative biochemical measurement of enzyme activities in muscle tissue showed deficiencies of short-chain acyl-CoA dehydrogenase (SCAD), medium-chain acyl-CoA dehydrogenase (MCAD), and isovaleryl-CoA dehydrogenase (IVD) also indicating MADD. Histology revealed extensive rhabdomyolysis with microvesicular lipidosis predominantly in type 1 muscle fibers and mitochondrial damage. However, the ETF and ETF-QO activities were within normal limits indicating the metabolic disorder to be acquired rather than inherited. To our knowledge, these are the first cases of biochemical MADD reported in equine medicine.
J. P. Koeman - One of the best experts on this subject based on the ideXlab platform.
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equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
Molecular Genetics and Metabolism, 2007Co-Authors: C M Westermann, J. P. Koeman, Monique G M De Sainvan Der Velden, Johannes H Van Der Kolk, Ruud Berger, I D Wijnberg, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B VaandragerAbstract:Two horses (a 7-year-old Groninger warmblood gelding and a six-month-old Trakehner mare) with pathologically confirmed rhabdomyolysis were diagnosed as suffering from multiple acyl-CoA dehydrogenase deficiency (MADD). This disorder has not been recognised in animals before. Clinical signs of both horses were a stiff, insecure gait, myoglobinuria, and finally recumbency. Urine, plasma, and muscle tissues were investigated. Analysis of plasma showed hyperglycemia, lactic acidemia, increased activity of muscle enzymes (ASAT, LDH, CK), and impaired kidney function (increased urea and creatinine). The most remarkable findings of organic acids in urine of both horses were increased lactic acid, ethylmalonic acid (EMA), 2-methylsuccinic acid, butyrylglycine (iso)valerylglycine, and hexanoylglycine. EMA was also increased in plasma of both animals. Furthermore, the profile of acylcarnitines in plasma from both animals showed a substantial elevation of C4-, C5-, C6-, C8-, and C5-DC-carnitine. Concentrations of acylcarnitines in urine of both animals revealed increased excretions of C2-, C3-, C4-, C5-, C6-, C5-OH-, C8-, C10:1-, C10-, and C5-DC-carnitine. In addition, concentrations of free carnitine were also increased. Quantitative biochemical measurement of enzyme activities in muscle tissue showed deficiencies of short-chain acyl-CoA dehydrogenase (SCAD), medium-chain acyl-CoA dehydrogenase (MCAD), and isovaleryl-CoA dehydrogenase (IVD) also indicating MADD. Histology revealed extensive rhabdomyolysis with microvesicular lipidosis predominantly in type 1 muscle fibers and mitochondrial damage. However, the ETF and ETF-QO activities were within normal limits indicating the metabolic disorder to be acquired rather than inherited. To our knowledge, these are the first cases of biochemical MADD reported in equine medicine.
