Expression in hepatomas and chromosomal localization of rat protein phosphatase 5 gene. 2000

H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University, Kita-15, Nishi-7, Kita-ku, Sapporo 060-0815, Japan.

The serine/threonine protein phosphatase type 5 (PP5) gene expression was ubiquitously observed among all the tissues examined, but being at the lowest level in the liver. The levels of PP5 mRNA were markedly elevated in rat highly malignant ascites hepatomas, while those in several rat primary hepatomas were slightly increased and those in the regenerating livers were not elevated at all compared to the control liver. The PP5 gene was mapped to rat chromosome 1q22.1. This region has been identified to have linkage homology among human, mouse and rat, and is known to be associated with several tumor types. Taken together, the present results strongly suggest important roles of PP5 in tumorigenesis.

UI MeSH Term Description Entries
D008114 Liver Neoplasms, Experimental Experimentally induced tumors of the LIVER. Hepatoma, Experimental,Hepatoma, Morris,Hepatoma, Novikoff,Experimental Hepatoma,Experimental Hepatomas,Experimental Liver Neoplasms,Hepatomas, Experimental,Neoplasms, Experimental Liver,Experimental Liver Neoplasm,Liver Neoplasm, Experimental,Morris Hepatoma,Novikoff Hepatoma
D008115 Liver Regeneration Repair or renewal of hepatic tissue. Liver Regenerations,Regeneration, Liver,Regenerations, Liver
D009363 Neoplasm Proteins Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm. Proteins, Neoplasm
D009687 Nuclear Proteins Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus. Nucleolar Protein,Nucleolar Proteins,Nuclear Protein,Protein, Nuclear,Protein, Nucleolar,Proteins, Nuclear,Proteins, Nucleolar
D009928 Organ Specificity Characteristic restricted to a particular organ of the body, such as a cell type, metabolic response or expression of a particular protein or antigen. Tissue Specificity,Organ Specificities,Specificities, Organ,Specificities, Tissue,Specificity, Organ,Specificity, Tissue,Tissue Specificities
D010749 Phosphoprotein Phosphatases A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) Phosphoprotein Phosphatase,Phosphoprotein Phosphohydrolase,Protein Phosphatase,Protein Phosphatases,Casein Phosphatase,Ecto-Phosphoprotein Phosphatase,Nuclear Protein Phosphatase,Phosphohistone Phosphatase,Phosphoprotein Phosphatase-2C,Phosphoseryl-Protein Phosphatase,Protein Phosphatase C,Protein Phosphatase C-I,Protein Phosphatase C-II,Protein Phosphatase H-II,Protein-Serine-Threonine Phosphatase,Protein-Threonine Phosphatase,Serine-Threonine Phosphatase,Threonine Phosphatase,Ecto Phosphoprotein Phosphatase,Phosphatase C, Protein,Phosphatase C-I, Protein,Phosphatase C-II, Protein,Phosphatase H-II, Protein,Phosphatase, Casein,Phosphatase, Ecto-Phosphoprotein,Phosphatase, Nuclear Protein,Phosphatase, Phosphohistone,Phosphatase, Phosphoprotein,Phosphatase, Phosphoseryl-Protein,Phosphatase, Protein,Phosphatase, Protein-Serine-Threonine,Phosphatase, Protein-Threonine,Phosphatase, Serine-Threonine,Phosphatase, Threonine,Phosphatase-2C, Phosphoprotein,Phosphatases, Phosphoprotein,Phosphatases, Protein,Phosphohydrolase, Phosphoprotein,Phosphoprotein Phosphatase 2C,Phosphoseryl Protein Phosphatase,Protein Phosphatase C I,Protein Phosphatase C II,Protein Phosphatase H II,Protein Phosphatase, Nuclear,Protein Serine Threonine Phosphatase,Protein Threonine Phosphatase,Serine Threonine Phosphatase
D002471 Cell Transformation, Neoplastic Cell changes manifested by escape from control mechanisms, increased growth potential, alterations in the cell surface, karyotypic abnormalities, morphological and biochemical deviations from the norm, and other attributes conferring the ability to invade, metastasize, and kill. Neoplastic Transformation, Cell,Neoplastic Cell Transformation,Transformation, Neoplastic Cell,Tumorigenic Transformation,Cell Neoplastic Transformation,Cell Neoplastic Transformations,Cell Transformations, Neoplastic,Neoplastic Cell Transformations,Neoplastic Transformations, Cell,Transformation, Cell Neoplastic,Transformation, Tumorigenic,Transformations, Cell Neoplastic,Transformations, Neoplastic Cell,Transformations, Tumorigenic,Tumorigenic Transformations
D002874 Chromosome Mapping Any method used for determining the location of and relative distances between genes on a chromosome. Gene Mapping,Linkage Mapping,Genome Mapping,Chromosome Mappings,Gene Mappings,Genome Mappings,Linkage Mappings,Mapping, Chromosome,Mapping, Gene,Mapping, Genome,Mapping, Linkage,Mappings, Chromosome,Mappings, Gene,Mappings, Genome,Mappings, Linkage
D004790 Enzyme Induction An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis. Induction, Enzyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
January 1996, Biochemical and biophysical research communications,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
April 1995, The Biochemical journal,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
June 2001, Brain research. Molecular brain research,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
April 1990, European journal of biochemistry,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
September 1991, FEBS letters,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
July 1995, Genomics,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
September 2006, Brain research,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
February 1993, International journal of oncology,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
January 1967, Kumamoto Igakkai zasshi. The Journal of the Kumamoto Medical Society,
H Shirato, and H Shima, and H Nakagama, and H Fukuda, and Y Watanabe, and K Ogawa, and Y Matsuda, and K Kikuchi
January 2000, Gene,
Copied contents to your clipboard!