| pubmed-article:12946945 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0600251 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0128897 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0296346 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C1539477 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:12946945 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:12946945 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:12946945 | pubmed:dateCreated | 2003-9-22 | lld:pubmed |
| pubmed-article:12946945 | pubmed:abstractText | We previously reported that treatment of human vascular smooth muscle cells (SMCs) with proapoptotic stimuli, including Fas ligand plus cycloheximide (FasL/Chx), or overexpression of Fas-associated death domain protein (FADD) result in increased expression of monocyte chemoattractant protein-1 (MCP-1) and other proinflammatory genes. In this study, we demonstrate that Fas/FADD-induced MCP-1 upregulation is driven by an autocrine/paracrine signaling loop in which interleukin (IL)-1alpha synthesis and release are activated through caspase- and calpain-dependent processes. Untreated SMCs contain very little IL-1alpha protein or transcript. Both were increased greatly in response to Fas/FADD activation, primarily through an autocrine/paracrine pathway in which secreted IL-1alpha stimulated additional IL-1alpha synthesis and release. Caspase 8 (Csp8) activity increased in response to FasL/Chx treatment, and Csp8 inhibitors markedly reduced IL-1alpha release and MCP-1 upregulation. In contrast, Csp8 activity was not significantly increased in response to FADD overexpression and caspase inhibitors did not effect FADD-induced MCP-1 upregulation. Both FasL/Chx treatment and FADD overexpression increased the activity of calpains. Calpain inhibitors reduced IL-1alpha release and MCP-1 upregulation in both FADD-overexpressing SMCs and FasL/Chx-treated SMCs without blocking Csp8 activity. This indicates that calpains are not required for activation of caspases and that caspase activation is not sufficient for IL-1alpha release and MCP-1 upregulation. These data suggest that calpains play a dominant role in Fas/FADD-induced IL-1alpha release and MCP-1 upregulation and that caspase activation may function to amplify the effects of calpain activation. | lld:pubmed |
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| pubmed-article:12946945 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12946945 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12946945 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12946945 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12946945 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12946945 | pubmed:issn | 1524-4571 | lld:pubmed |
| pubmed-article:12946945 | pubmed:author | pubmed-author:LilesW... | lld:pubmed |
| pubmed-article:12946945 | pubmed:author | pubmed-author:FerriNicolaN | lld:pubmed |
| pubmed-article:12946945 | pubmed:author | pubmed-author:SeifertRonald... | lld:pubmed |
| pubmed-article:12946945 | pubmed:author | pubmed-author:Bowen-PopeDan... | lld:pubmed |
| pubmed-article:12946945 | pubmed:author | pubmed-author:SchaubFriedem... | lld:pubmed |
| pubmed-article:12946945 | pubmed:author | pubmed-author:SaysonKirsten... | lld:pubmed |
| pubmed-article:12946945 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:12946945 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:12946945 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:12946945 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12946945 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12946945 | pubmed:pagination | 515-22 | lld:pubmed |
| pubmed-article:12946945 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12946945 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12946945 | pubmed:articleTitle | Fas and Fas-associated death domain protein regulate monocyte chemoattractant protein-1 expression by human smooth muscle cells through caspase- and calpain-dependent release of interleukin-1alpha. | lld:pubmed |
| pubmed-article:12946945 | pubmed:affiliation | Department of Pathology, University of Washington, Box 357470, Seattle, Wash 98195-7470, USA. | lld:pubmed |
| pubmed-article:12946945 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12946945 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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