| pubmed-article:8980912 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C2709199 | lld:lifeskim |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
| pubmed-article:8980912 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:8980912 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8980912 | pubmed:dateCreated | 1997-3-7 | lld:pubmed |
| pubmed-article:8980912 | 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. | lld:pubmed |
| pubmed-article:8980912 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8980912 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8980912 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8980912 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8980912 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8980912 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8980912 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8980912 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8980912 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8980912 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8980912 | pubmed:issn | 0171-9335 | lld:pubmed |
| pubmed-article:8980912 | pubmed:author | pubmed-author:JohanssonB... | lld:pubmed |
| pubmed-article:8980912 | pubmed:author | pubmed-author:GoldfarbR HRH | lld:pubmed |
| pubmed-article:8980912 | pubmed:author | pubmed-author:RivettA JAJ | lld:pubmed |
| pubmed-article:8980912 | pubmed:author | pubmed-author:NannmarkUU | lld:pubmed |
| pubmed-article:8980912 | pubmed:author | pubmed-author:KitsonR PRP | lld:pubmed |
| pubmed-article:8980912 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8980912 | pubmed:volume | 71 | lld:pubmed |
| pubmed-article:8980912 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8980912 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8980912 | pubmed:pagination | 402-8 | lld:pubmed |
| pubmed-article:8980912 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
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| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
| pubmed-article:8980912 | pubmed:meshHeading | pubmed-meshheading:8980912-... | lld:pubmed |
| pubmed-article:8980912 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8980912 | pubmed:articleTitle | Immunocytochemical localization of multicatalytic protease complex (proteasome) during generation of murine IL-2-activated natural killer (A-NK) cells. | lld:pubmed |
| pubmed-article:8980912 | pubmed:affiliation | Department of Anatomy and Cell Biology, University of Göteborg, Sweden. | lld:pubmed |
| pubmed-article:8980912 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8980912 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
