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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1997-3-7
|
| pubmed:abstractText |
Murine IL-2-activated, adherent natural killer (A-NK) cells produce proteolytic activities (including a chymase and a tryptase) which appear to be components of the proteasome/multicatalytic proteinase complex and appear to represent the mouse homologues of the rat A-NK cell A-NKP 2 and A-NKP 1 protease components. The chymase is readily inhibited by Z-Gly-Gly-Phe chloromethylketone (Z-GGF) and to a lesser extent by N-tosyl-L-phenylalanyl-chloromethylketone (TPCK). In addition, this activity is inhibited by 3,4-dichloroisocoumarin (DCI), a suicide inhibitor for both chymotryptic and tryptic proteolytic enzymes. Protease inhibitors reduced A-NK cell-mediated cytotoxicity against P815 target cells, most prominently with inhibitors of chymotryptic and tryptic enzymes, including TPCK, DCI and Z-GGF. A polyclonal rabbit antibody raised against rat liver proteasome immunofluorescently labeled the cytoplasm of 4-day-cultured murine A-NK cells, multiple granules in 5 to 6-day cultures and large intracytoplasmic pools in cells cultured longer. Ultrastructurally this shift in labeling over time corresponded to an immunogold redistribution to non-membrane delineated mucoid masses. A minor nuclear labeling was noted at all time points, whereas the cisternae of the endoplasmic reticulum or Golgi region were negative. It is concluded that murine A-NK cells synthesize and accumulate proteasome in large intracytoplasmic pools, non-delineated by membranes which can occupy up to 80% of the A-NK cellular volume. The potential function of the proteasome produced by A-NK cells including cell-mediated cytotoxicity against tumor target cells remains to be elucidated.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0171-9335
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
71
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
402-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8980912-Animals,
pubmed-meshheading:8980912-Cell Line,
pubmed-meshheading:8980912-Cells, Cultured,
pubmed-meshheading:8980912-Cysteine Endopeptidases,
pubmed-meshheading:8980912-Cytoplasm,
pubmed-meshheading:8980912-Cytoplasmic Granules,
pubmed-meshheading:8980912-Cytotoxicity, Immunologic,
pubmed-meshheading:8980912-Immunohistochemistry,
pubmed-meshheading:8980912-Interleukin-2,
pubmed-meshheading:8980912-Killer Cells, Natural,
pubmed-meshheading:8980912-Lymphocyte Activation,
pubmed-meshheading:8980912-Male,
pubmed-meshheading:8980912-Mice,
pubmed-meshheading:8980912-Mice, Inbred C57BL,
pubmed-meshheading:8980912-Microscopy, Electron,
pubmed-meshheading:8980912-Microscopy, Fluorescence,
pubmed-meshheading:8980912-Multienzyme Complexes,
pubmed-meshheading:8980912-Organelles,
pubmed-meshheading:8980912-Protease Inhibitors,
pubmed-meshheading:8980912-Proteasome Endopeptidase Complex
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Immunocytochemical localization of multicatalytic protease complex (proteasome) during generation of murine IL-2-activated natural killer (A-NK) cells.
|
| pubmed:affiliation |
Department of Anatomy and Cell Biology, University of Göteborg, Sweden.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|