| pubmed-article:12954601 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0079459 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0812246 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0079460 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0543482 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0680829 | lld:lifeskim |
| pubmed-article:12954601 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:12954601 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12954601 | pubmed:dateCreated | 2003-12-8 | lld:pubmed |
| pubmed-article:12954601 | pubmed:abstractText | Stimulation of human neutrophils with tumor necrosis factor-alpha (TNF), granulocyte-macrophage colony-stimulating factor (GM-CSF), or granulocyte CSF (G-CSF) resulted in decreased fluorescence intensity of FITC-phalloidin (actin depolymerization) and morphological changes. Cytokine-induced actin depolymerization was dependent on the concentration of cytokines used as stimuli. The maximal changes were detected at 10 min after stimulation with TNF or GM-CSF and at 20 min after stimulation with G-CSF. Cytokine-induced actin depolymerization was sustained for at least 30 min after stimulation. In contrast, N-formyl-methionyl-leucyl-phenylalanine (FMLP) rapidly (within 45 s) induced an increase in the fluorescence intensity of FITC-phalloidin (actin polymerization) and morphological changes. TNF- and GM-CSF-induced actin depolymerization and morphological changes, but not FMLP-induced responses, were partially inhibited by either PD-98059, an inhibitor of mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) kinase, or SB-203580, an inhibitor of p38 MAPK, and were almost completely abolished by these inhibitors in combination. G-CSF-induced responses were almost completely abolished by PD-98059 and were unaffected by SB-203580. These findings are consistent with the ability of these cytokines to activate the distinct MAPK subtype cascade in human neutrophils. Phosphorylated ERK and p38 MAPK were not colocalized with F-actin in neutrophils stimulated by cytokines or FMLP. Furthermore, FMLP-induced polarization and actin polymerization were prevented by cytokine pretreatment. These findings suggest that TNF, GM-CSF, and G-CSF induce actin depolymerization and morphological changes through activation of ERK and/or p38 MAPK and that cytokine-induced actin reorganization may be partly responsible for the inhibitory effect of these cytokines on neutrophil chemotaxis. | lld:pubmed |
| pubmed-article:12954601 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12954601 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12954601 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12954601 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:12954601 | pubmed:issn | 0363-6143 | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:MizunoKensaku... | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:KobayashiHiro... | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:SuzukiKenichi... | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:KitagawaSeiic... | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:IshiiMasamits... | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:KatoTakayukiT | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:HatoFumihikoF | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:KamataNorikoN | lld:pubmed |
| pubmed-article:12954601 | pubmed:author | pubmed-author:KutsunaHaruoH | lld:pubmed |
| pubmed-article:12954601 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12954601 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:12954601 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12954601 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12954601 | pubmed:pagination | C55-64 | lld:pubmed |
| pubmed-article:12954601 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12954601 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:12954601 | pubmed:articleTitle | Actin reorganization and morphological changes in human neutrophils stimulated by TNF, GM-CSF, and G-CSF: the role of MAP kinases. | lld:pubmed |
| pubmed-article:12954601 | pubmed:affiliation | Department of Physiology, Osaka City University Medical School, Asahi-machi, Abeno-ku, Osaka 545-8585, Japan. | lld:pubmed |
| pubmed-article:12954601 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12954601 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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