Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA85347 | ENA |
REPOSITORIES: ENA
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Project description:Comparison of gene expression data from thalidomide modulated- and unmodulated-MSCs from patients with idiopathic thrombocytopenic purpura (ITP). This experiment consists of 3 arrays.
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Project description:Whole blood transcriptional profiling of pediatric idiopathic thrombocytopenic purpura (ITP) patients comparing self-limited acute ITP patients with chronic ITP patients or progression-to-chronic ITP patients. Patient samples were collected during 3 different disease states: 8 samples from acute ITP pts (within 6 months of dx, during active disease), 4 samples from progression-to-chronic ITP pts (within 6 months of dx), and 14 samples from chronic ITP (after 6 months of dx).
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Project description:Genome wide expression in ADAMTS13-deficient thrombotic thrombocytopenic purpura TTP
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Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.
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Project description:RNA extracted at 240min. Samples are rRNA depleted. Expression measurement of Homo sapiens genes.
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