Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/13292
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dc.contributor.authorSmyth, Mark Jen
dc.contributor.authorSayers, T Jen
dc.contributor.authorWiltrout, Ten
dc.contributor.authorPowers, J Cen
dc.contributor.authorTrapani, Joseph Aen
dc.date.accessioned2015-05-16T03:07:03Z
dc.date.available2015-05-16T03:07:03Z
dc.date.issued1993-12-01en
dc.identifier.citationJournal of Immunology (baltimore, Md. : 1950); 151(11): 6195-205en
dc.identifier.govdoc8245461en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/13292en
dc.description.abstractA cDNA clone encoding a human NK serine protease was obtained by screening a lambda-gt10 library from the Lopez NK leukemia with the rat natural killer Met-ase (RNK-Met-1) cDNA clone. In Northern blot analysis human Met-ase (Hu-Met-1) cDNA hybridized with a 0.9-kb mRNA in two human NK leukemia cell lines, unstimulated human PBMC, and untreated purified CD3-CD56+ large granular lymphocytes. Unlike other members of the granzyme family that are highly expressed in activated peripheral T cells, the Hu-Met-1 transcript was barely detected in a population of PMA and ionomycin or IL-2-treated high density T cells. Several in vitro cultured Burkitt lymphomas, chronic- and promyeloid leukemias, acute lymphoblastic leukemias, and colon and ovarian carcinomas and colon and ovarian carcinomas did not express Hu-Met-1 mRNA. Hu-Met-1 mRNA expression in a small number of human T cell tumor lines did not correlate with any particular phenotype or stage of development. The presence of Hu-Met-1 mRNA closely correlated with the Met-ase activity of cellular lysates prepared from these various human peripheral blood subsets and in vitro cultured cell lines. Met-ase activity detected in whole cell lysates of cytotoxic lymphocytes was associated with the cytoplasmic granules of these cells. The nucleotide sequence of the Hu-Met-1 cDNA clone encodes a predicted serine protease of 257 amino acids. The predicted protein is an active enzyme of 232 amino acids with a calculated unglycosylated m.w. of 27,100. Hu-Met-1 is 66% identical to RNK-Met-1 at the amino acid level. The human and rat mature protein sequences conserve the active site His, Asp, and Ser amino acids that form the catalytic triad of serine proteases, all 8 cysteine residues, and several amino acids critical in the formation of the substrate binding pocket. The gene for the Hu-Met-1 serine protease is located on chromosome 19, which distinguishes it from any other member of the human granzyme family.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherAnimalsen
dc.subject.otherBase Sequenceen
dc.subject.otherChromosome Mappingen
dc.subject.otherChromosomes, Human, Pair 19en
dc.subject.otherCloning, Molecularen
dc.subject.otherDNA, Complementary.isolation & purificationen
dc.subject.otherHumansen
dc.subject.otherKiller Cells, Natural.enzymologyen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherRNA, Messenger.analysisen
dc.subject.otherRatsen
dc.subject.otherSerine Endopeptidases.chemistry.geneticsen
dc.titleMet-ase: cloning and distinct chromosomal location of a serine protease preferentially expressed in human natural killer cells.en
dc.typeJournal Articleen
dc.identifier.journaltitleJournal of Immunology (Baltimore, Md. : 1950)en
dc.identifier.affiliationCellular Cytotoxicity Laboratory, Austin Research Institute, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages6195-205en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/8245461en
dc.type.austinJournal Articleen
item.fulltextNo Fulltext-
item.openairetypeJournal Article-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
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