| pubmed-article:2521661 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2521661 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:2521661 | lifeskim:mentions | umls-concept:C0028778 | lld:lifeskim |
| pubmed-article:2521661 | lifeskim:mentions | umls-concept:C0033607 | lld:lifeskim |
| pubmed-article:2521661 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:2521661 | lifeskim:mentions | umls-concept:C1819447 | lld:lifeskim |
| pubmed-article:2521661 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:2521661 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:2521661 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2521661 | pubmed:dateCreated | 1989-3-13 | lld:pubmed |
| pubmed-article:2521661 | pubmed:abstractText | Several chymotryptic-type protease inhibitors were found to inhibit both anti-CD3 mAb- and PHA-induced rise in Ca2+ and IL-2 production in Jurkat T cells. The magnitude of inhibition was a function of the effectors used to stimulate Ca2+ entry and depended on the concentration of the inhibitors. Neither tryptic-type protease inhibitors nor an elastase substrate prevented anti-CD3 mAb- or PHA-induced Ca2+ rise in Jurkat cells. The inhibitory effect of N-alpha-p-tosyl-L-phenylalanine chloromethyl-ketone on anti-CD3 mAb- and PHA-induced rise in Ca2+ resulted from a rapid increase in Ca2+ efflux. The inhibitors which were effective on Ca2+ mobilization also inhibited IL-2 production initiated by an anti-CD3 mAb in the presence of 12-O-tetradecanoylphorbol-13-acetate, and to a lesser extent by PHA or the calcium ionophore A23187. No inhibition of IL-2 production was observed when tryptic-type protease inhibitors or the elastase inhibitor were used. In addition, membrane preparations from Jurkat cells were found to hydrolyze the chymotryptic substrate Suc-Ala-Ala-Phe-paranitroaniline, an effect markedly inhibited by N-alpha-p-tosyl-L-phenylalanine chloromethylketone. Moreover, this inhibitor protected one potential endogenous substrate (Mr 38 kDa) from proteolysis. Taken together, these observations show that chymotryptic-type protease inhibitors block the responses generated by the binding of anti-CD3 mAb to Jurkat cells, and suggest that a chymotryptic-like membrane protease contributes to T cell activation. | lld:pubmed |
| pubmed-article:2521661 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2521661 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:2521661 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2521661 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2521661 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:2521661 | pubmed:author | pubmed-author:AusselCC | lld:pubmed |
| pubmed-article:2521661 | pubmed:author | pubmed-author:MarxEE | lld:pubmed |
| pubmed-article:2521661 | pubmed:author | pubmed-author:FehlmannMM | lld:pubmed |
| pubmed-article:2521661 | pubmed:author | pubmed-author:BreittmayerJ... | lld:pubmed |
| pubmed-article:2521661 | pubmed:author | pubmed-author:AubergerPP | lld:pubmed |
| pubmed-article:2521661 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2521661 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2521661 | pubmed:volume | 142 | lld:pubmed |
| pubmed-article:2521661 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2521661 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2521661 | pubmed:pagination | 1253-9 | lld:pubmed |
| pubmed-article:2521661 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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| pubmed-article:2521661 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2521661 | pubmed:articleTitle | Chymotryptic-type protease inhibitors block the increase in Ca2+ and Il-2 production in activated Jurkat T cells. | lld:pubmed |
| pubmed-article:2521661 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale U210, Nice, France. | lld:pubmed |
| pubmed-article:2521661 | pubmed:publicationType | Journal Article | lld:pubmed |
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