Project description:To investigate the gene expression differences between the stroma and glands in the transitional and peripheral zones of the prostate Laser microdissection of prostate cancer tissues to separate glands from stroma followed by RNA extraction from the glands and whole Genome Microarray. We have pooled normal glands and stroma out of the transitional and peripheral zones from 10 patients after radical prostatectomy
Project description:To investigate the gene expression differences between the stroma and glands in the transitional and peripheral zones of the prostate
Project description:To investigate the gene expression differences between the normal peripheral zone glands compared to the moderatly and poorly differentiated tumor glands of the prostate. Laser microdissection of prostate cancer tissues to separate glands from stroma followed by RNA extraction from the glands and whole Genome Microarray. We have pooled normal glands from 10 patients, moderately differentiated tumor from 5 patients and poorly differentiated tumors from 4 patients with prostate carcinomas.
Project description:This is an analysis of stroma from 17 Grade 3 reactive stroma prostate cancer tissues and matched normal peripheral zone tissues. Keywords: two group comparison Laser capture microdissection and expression array analysis of stroma from 17 Grade 3 reactive stroma prostate cancer tissues and matched normal peripheral zone tissues.
Project description:This is an analysis of stroma from 17 Grade 3 reactive stroma prostate cancer tissues and matched normal peripheral zone tissues. Keywords: two group comparison
Project description:The identification of cellular and functional heterogeneity within the prostate and between the transitional zone (TZ) and peripheral zone (PZ) is critical for understanding the spatial distribution of prostate diseases. Three paired human prostate PZ and TZ tissue samples were used for scRNA-seq.
Project description:To investigate the gene expression differences between the normal peripheral zone glands compared to the moderatly and poorly differentiated tumor glands of the prostate.
Project description:1,322 morphologically unidentified fragmentary bone specimens were analyzed using MALDI-TOF and a subset of 341 bone specimens with LC-MS/MS in order to characterize their proteome for species identification and potential hominin specimens related to the LRJ transitional period derived from the site Ilsenhöhle Ranis, Germany (50°39.7563’N, 11°33.9139’E).
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.
