pubmed-article:12556365 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12556365 | lifeskim:mentions | umls-concept:C1705079 | lld:lifeskim |
pubmed-article:12556365 | lifeskim:mentions | umls-concept:C1337092 | lld:lifeskim |
pubmed-article:12556365 | lifeskim:mentions | umls-concept:C1522558 | lld:lifeskim |
pubmed-article:12556365 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
pubmed-article:12556365 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:12556365 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:12556365 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:12556365 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12556365 | pubmed:dateCreated | 2003-1-30 | lld:pubmed |
pubmed-article:12556365 | pubmed:abstractText | This study examined the effect of hemin on the expression of heme oxygenase-1 (HO-1) and monocyte chemoattractant protein-1 (MCP-1) in immortalized rat proximal tubular epithelial cells (IRPTCs). Hemin elicited a dose- and time-dependent induction of HO-1 and MCP-1 mRNA. HO activity contributed to MCP-1 mRNA expression at early time points (4-6 h) because inhibition of HO activity by zinc protoporphyrin (ZnPP) prevented hemin-induced expression of MCP-1 mRNA. Catalytically active intracellular iron was markedly increased in hemin-treated IRPTCs and contributed to the induction of HO-1 and MCP-1 mRNA because an iron chelator blocked hemin-induced upregulation of both genes, whereas a cell-permeant form of iron directly induced these genes. N-acetylcysteine completely blocked hemin-induced expression of HO-1 and MCP-1 mRNA, thereby providing added evidence for redox regulation of expression of these genes. The redox-sensitive transcription factor NF-kappaB was recruited in hemin-induced upregulation of MCP-1 because two different compounds that abrogate the activation of NF-kappaB (TPCK and BAY 11-7082) completely blocked hemin-induced upregulation of MCP-1 mRNA. In contrast to this HO-mediated induction of MCP-1 through redox-sensitive, iron-dependent, and NF-kappaB-involved pathways observed after 4-6 h, hemin also elicited a delayed induction of MCP-1 at 18 h through HO-independent pathways. We conclude that hemin is a potent inducer of MCP-1 in IRPTCs: HO-dependent, heme-degrading pathways lead to an early, robust, and self-remitting induction of MCP-1, whereas HO-independent mechanisms lead to a delayed expression of MCP-1. | lld:pubmed |
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pubmed-article:12556365 | pubmed:language | eng | lld:pubmed |
pubmed-article:12556365 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12556365 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12556365 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12556365 | pubmed:month | Mar | lld:pubmed |
pubmed-article:12556365 | pubmed:issn | 1931-857X | lld:pubmed |
pubmed-article:12556365 | pubmed:author | pubmed-author:IngelfingerJu... | lld:pubmed |
pubmed-article:12556365 | pubmed:author | pubmed-author:TangShiow-Shi... | lld:pubmed |
pubmed-article:12556365 | pubmed:author | pubmed-author:NathKarl AKA | lld:pubmed |
pubmed-article:12556365 | pubmed:author | pubmed-author:AlamJawedJ | lld:pubmed |
pubmed-article:12556365 | pubmed:author | pubmed-author:KanakiriyaSha... | lld:pubmed |
pubmed-article:12556365 | pubmed:author | pubmed-author:CroattAnthony... | lld:pubmed |
pubmed-article:12556365 | pubmed:author | pubmed-author:HaggardJill... | lld:pubmed |
pubmed-article:12556365 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12556365 | pubmed:volume | 284 | lld:pubmed |
pubmed-article:12556365 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12556365 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12556365 | pubmed:pagination | F546-54 | lld:pubmed |
pubmed-article:12556365 | pubmed:dateRevised | 2011-4-28 | lld:pubmed |
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pubmed-article:12556365 | pubmed:meshHeading | pubmed-meshheading:12556365... | lld:pubmed |
pubmed-article:12556365 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12556365 | pubmed:articleTitle | Heme: a novel inducer of MCP-1 through HO-dependent and HO-independent mechanisms. | lld:pubmed |
pubmed-article:12556365 | pubmed:affiliation | Division of Nephrology, Mayo Clinic/Foundation, Rochester, Minnesota 55905, USA. | lld:pubmed |
pubmed-article:12556365 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12556365 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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