| pubmed-article:9228015 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C0291573 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C1512772 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C0043481 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
| pubmed-article:9228015 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:9228015 | pubmed:issue | 30 | lld:pubmed |
| pubmed-article:9228015 | pubmed:dateCreated | 1997-9-9 | lld:pubmed |
| pubmed-article:9228015 | pubmed:abstractText | The prevention of apoptosis by Zn2+ has generally been attributed to its inhibition of an endonuclease acting in the late phase of apoptosis. In this study we investigated the effect of Zn2+ on an earlier event in the apoptotic process, the proteolysis of the "death substrate" poly(ADP-ribose) polymerase (PARP). Pretreatment of intact Molt4 leukemia cells with micromolar concentrations of Zn2+ caused an inhibition of PARP proteolysis induced by the chemotherapeutic agent etoposide. Using a cell-free system consisting of purified bovine PARP as a substrate and an apoptotic extract or recombinant caspase-3 as the PARP protease, Zn2+ inhibited PARP proteolysis in the low micromolar range. To rule out an effect of Zn2+ on PARP, a protein with two zinc finger domains, we used recombinant caspase-3 and a chromogenic tetrapeptide substrate containing the caspase-3 cleavage site. In this system, Zn2+ inhibited caspase-3 with an IC50 of 0.1 microM. These results identify caspase-3 as a novel target of Zn2+ inhibition in apoptosis and suggest a regulatory role for Zn2+ in modulating the upstream apoptotic machinery. | lld:pubmed |
| pubmed-article:9228015 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9228015 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9228015 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9228015 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9228015 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9228015 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9228015 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9228015 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9228015 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9228015 | pubmed:author | pubmed-author:PoirierG GGG | lld:pubmed |
| pubmed-article:9228015 | pubmed:author | pubmed-author:DuriezPP | lld:pubmed |
| pubmed-article:9228015 | pubmed:author | pubmed-author:SmythM JMJ | lld:pubmed |
| pubmed-article:9228015 | pubmed:author | pubmed-author:HannunY AYA | lld:pubmed |
| pubmed-article:9228015 | pubmed:author | pubmed-author:PerryD KDK | lld:pubmed |
| pubmed-article:9228015 | pubmed:author | pubmed-author:SalvesenG SGS | lld:pubmed |
| pubmed-article:9228015 | pubmed:author | pubmed-author:StennickeH... | lld:pubmed |
| pubmed-article:9228015 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9228015 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:9228015 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9228015 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9228015 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9228015 | pubmed:pagination | 18530-3 | lld:pubmed |
| pubmed-article:9228015 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9228015 | pubmed:meshHeading | pubmed-meshheading:9228015-... | lld:pubmed |
| pubmed-article:9228015 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9228015 | pubmed:articleTitle | Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis. | lld:pubmed |
| pubmed-article:9228015 | pubmed:affiliation | Department of Medicine, Duke University Medical Center, Education and Clinical Center (GRECC) Veterans Affairs Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:9228015 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9228015 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9228015 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9228015 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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