The Experts below are selected from a list of 219 Experts worldwide ranked by ideXlab platform

Arie B Vaandrager - One of the best experts on this subject based on the ideXlab platform.

  • equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
    Molecular Genetics and Metabolism, 2007
    Co-Authors: C M Westermann, M G M De Sainvan Der Velden, J H Van Der Kolk, Ruud Berger, I D Wijnberg, J P Koeman, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B Vaandrager
    Abstract:

    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.

C M Westermann - One of the best experts on this subject based on the ideXlab platform.

  • equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
    Molecular Genetics and Metabolism, 2007
    Co-Authors: C M Westermann, M G M De Sainvan Der Velden, J H Van Der Kolk, Ruud Berger, I D Wijnberg, J P Koeman, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B Vaandrager
    Abstract:

    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.

Christa Kuehn - One of the best experts on this subject based on the ideXlab platform.

  • Selection signatures in four German warmblood horse breeds: Tracing breeding history in the modern sport horse
    PLOS ONE, 2019
    Co-Authors: Wietje Nolte, Georg Thaller, Christa Kuehn
    Abstract:

    The study of selection signatures helps to find genomic regions that have been under selective pressure and might host genes or variants that modulate important phenotypes. Such knowledge improves our understanding of how breeding programmes have shaped the genomes of livestock. In this study, 942 stallions were included from four, exemplarily chosen, German warmblood breeds with divergent historical and recent selection focus and different crossbreeding policies: Trakehner (N = 44), Holsteiner (N = 358), Hanoverian (N = 319) and Oldenburger (N = 221). Those breeds are nowadays bred for athletic performance and aptitude for show-jumping, dressage or eventing, with a particular focus of Holsteiner on the first discipline. Blood samples were collected during the health exams of the stallion preselections before licensing and were genotyped with the Illumina EquineSNP50 BeadChip. Autosomal markers were used for a multi-method search for signals of positive selection. Analyses within and across breeds were conducted by using the integrated Haplotype Score (iHS), cross-population Extended Haplotype Homozygosity (xpEHH) and Runs of Homozygosity (ROH). Oldenburger and Hanoverian showed very similar iHS signatures, but breed specificities were detected on multiple chromosomes with the xpEHH. The Trakehner clustered as a distinct group in a principal component analysis and also showed the highest number of ROHs, which reflects their historical bottleneck. Beside breed specific differences, we found shared selection signals in an across breed iHS analysis on chromosomes 1, 4 and 7. After investigation of these iHS signals and shared ROH for potential functional candidate genes and affected pathways including enrichment analyses, we suggest that genes affecting muscle functionality (TPM1, TMOD2-3, MYO5A, MYO5C), energy metabolism and growth (AEBP1, RALGAPA2, IGFBP1, IGFBP3-4), embryonic development (HOXB-complex) and fertility (THEGL, ZPBP1-2, TEX14, ZP1, SUN3 and CFAP61) have been targeted by selection in all breeds. Our findings also indicate selection pressure on KITLG, which is well-documented for influencing pigmentation.

  • Breed-specific genome-wide integrated Haplotype Score (iHS) plots within four warmblood horse breeds.
    2019
    Co-Authors: Wietje Nolte, Georg Thaller, Christa Kuehn
    Abstract:

    Genome-wide breed-specific iHS plots for Trakehner (A), Holsteiner (B), Hanoverian (C) and Oldenburger (D) with a significance threshold of -log10(p) ≥ 4.0.

  • Genome-wide integrated Haplotype Score (iHS) plot across four warmblood horse breeds.
    2019
    Co-Authors: Wietje Nolte, Georg Thaller, Christa Kuehn
    Abstract:

    Genome-wide iHS plot for all individuals (N = 942) across the four breeds Trakehner, Holsteiner, Hanoverian and Oldenburger with a significance threshold of -log10(p) ≥ 4.0.

  • Cross-population Extended Haplotype Homozygosity (xpEHH) plot for four warmblood horse breeds.
    2019
    Co-Authors: Wietje Nolte, Georg Thaller, Christa Kuehn
    Abstract:

    Comparison of one breed with the three others together as control for Trakehner (A), Holsteiner (B), Hanoverian (C)and Oldenburger (D) with a significance threshold of -log10(p) ≥ 4.0.

  • Principal Component Analysis (PCA) based on genotype data for four German warmblood horse breeds.
    2019
    Co-Authors: Wietje Nolte, Georg Thaller, Christa Kuehn
    Abstract:

    Based on a genomic relationship matrix, eigenvalues were calculated and the first two components used for a colour-coded clustering of the breeds Hanoverian (N = 319), Holsteiner (N = 358), Oldenburger (N = 221), and Trakehner (N = 44).

M G M De Sainvan Der Velden - One of the best experts on this subject based on the ideXlab platform.

  • equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
    Molecular Genetics and Metabolism, 2007
    Co-Authors: C M Westermann, M G M De Sainvan Der Velden, J H Van Der Kolk, Ruud Berger, I D Wijnberg, J P Koeman, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B Vaandrager
    Abstract:

    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 H Van Der Kolk - One of the best experts on this subject based on the ideXlab platform.

  • equine biochemical multiple acyl coa dehydrogenase deficiency madd as a cause of rhabdomyolysis
    Molecular Genetics and Metabolism, 2007
    Co-Authors: C M Westermann, M G M De Sainvan Der Velden, J H Van Der Kolk, Ruud Berger, I D Wijnberg, J P Koeman, R J A Wanders, Johannes A Lenstra, N Testerink, Arie B Vaandrager
    Abstract:

    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.