| pubmed-article:9053448 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C0079189 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1157399 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C2612728 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1516451 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1514623 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:9053448 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:9053448 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9053448 | pubmed:dateCreated | 1997-3-13 | lld:pubmed |
| pubmed-article:9053448 | pubmed:abstractText | Proteases are now firmly established as major regulators of the "execution" phase of apoptosis. Here, we examine the role of proteases and their relationship to ceramide, a proposed mediator of apoptosis, in the tumor necrosis factor-alpha (TNF-alpha)-induced pathway of cell death. Ceramide induced activation of prICE, the protease that cleaves the death substrate poly(ADP-ribose) polymerase. Bcl-2 inhibited ceramide-induced death, but not ceramide generation. In contrast, Cytokine response modifier A (CrmA), a potent inhibitor of Interleukin-1 beta converting enzyme and related proteases, inhibited ceramide generation and prevented TNF-alpha-induced death. Exogenous ceramide could overcome the CrmA block to cell death, but not the Bcl-2 block. CrmA, however, did not inhibit the activation of nuclear factor (NF)-kappa B by TNF-alpha, demonstrating that other signaling functions of TNF-alpha remain intact and that ceramide does not play a role in the activation of NF-kappa B. These studies support a distinct role for proteases in the signaling/activation phase of apoptosis acting upstream of ceramide formation. | lld:pubmed |
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| pubmed-article:9053448 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9053448 | pubmed:citationSubset | IM | lld:pubmed |
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