| pubmed-article:8609175 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8609175 | lifeskim:mentions | umls-concept:C0115305 | lld:lifeskim |
| pubmed-article:8609175 | lifeskim:mentions | umls-concept:C0014261 | lld:lifeskim |
| pubmed-article:8609175 | lifeskim:mentions | umls-concept:C1166758 | lld:lifeskim |
| pubmed-article:8609175 | lifeskim:mentions | umls-concept:C0023745 | lld:lifeskim |
| pubmed-article:8609175 | lifeskim:mentions | umls-concept:C1154393 | lld:lifeskim |
| pubmed-article:8609175 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:8609175 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8609175 | pubmed:dateCreated | 1996-5-30 | lld:pubmed |
| pubmed-article:8609175 | pubmed:abstractText | We have examined functions of the cytoplasmic domain of E-selectin, an inducible endothelial transmembrane protein, especially its ability to associate with the cytoskeleton during leukocyte adhesion. Confocal microscopy of interleukin-1 beta (IL-1 beta)-activated human umbilical vein endothelial cells (HUVEC) visualized clustering of E-selectin molecules in the vicinity of leukocyte-endothelial cell attachment sites. A detergent based extraction and Western blotting procedure demonstrated an association of E-selectin with the insoluble (cytoskeletal) fraction of endothelial monolayers that correlated with adhesion of leukocytes via an E-selectin-dependent mechanism. A mutant form of E-selectin lacking the cytoplasmic domain (tailless E-selectin) was expressed in COS-7 cell and supported leukocyte attachment (in a nonstatic adhesion assay) in a fashion similar to the native E-selectin molecule, but failed to become associated with the cytoskeletal fraction. To identify the cytoskeletal components that associate with the cytoplasmic domain of E-selectin, paramagnetic beads coated with the adhesion-blocking anti-E-selectin monoclonal antibody H18/7 were incubated with IL-1 beta-activated HUVEC, and then subjected to detergent extraction and magnetic separation. Certain actin-associated proteins, including alpha-actinin, vinculin, filamin, paxillin, as well as focal adhesion kinase (FAK), were copurified by this procedure, however talin was not. When a mechanical stress was applied to H18/7-coated ferromagnetic beads bound to the surface of IL-1 beta-activated HUVEC, using a magnetical twisting cytometer, the observed resistance to the applied stress was inhibited by cytochalasin D, thus demonstrating transmembrane cytoskeletal mechanical linkage. COS-7 cells transfected with the tailless E-selectin failed to show resistance to the twisting stress. Taken together, these data indicate that leukocyte adhesion to cytokine-activated HUVEC induces transmembrane cytoskeletal linkage of E-selectin through its cytoplasmic domain, a process which may have important implications for cell-cell signaling as well as mechanical anchoring during leukocyte-endothelial adhesive interactions. | lld:pubmed |
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| pubmed-article:8609175 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8609175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8609175 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8609175 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8609175 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8609175 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:8609175 | pubmed:author | pubmed-author:YoshidaMM | lld:pubmed |
| pubmed-article:8609175 | pubmed:author | pubmed-author:WaniHH | lld:pubmed |
| pubmed-article:8609175 | pubmed:author | pubmed-author:GimbroneM... | lld:pubmed |
| pubmed-article:8609175 | pubmed:author | pubmed-author:ResnickNN | lld:pubmed |
| pubmed-article:8609175 | pubmed:author | pubmed-author:RosenzweigAA | lld:pubmed |
| pubmed-article:8609175 | pubmed:author | pubmed-author:IngberD EDE | lld:pubmed |
| pubmed-article:8609175 | pubmed:author | pubmed-author:WestlinW FWF | lld:pubmed |
| pubmed-article:8609175 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8609175 | pubmed:volume | 133 | lld:pubmed |
| pubmed-article:8609175 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8609175 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8609175 | pubmed:pagination | 445-55 | lld:pubmed |
| pubmed-article:8609175 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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