| pubmed-article:9017600 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9017600 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9017600 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9017600 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:9017600 | lifeskim:mentions | umls-concept:C0061187 | lld:lifeskim |
| pubmed-article:9017600 | lifeskim:mentions | umls-concept:C1155980 | lld:lifeskim |
| pubmed-article:9017600 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9017600 | pubmed:dateCreated | 1997-4-14 | lld:pubmed |
| pubmed-article:9017600 | pubmed:abstractText | Human neutrophils generally function adherent to an extracellular matrix. We have previously reported that upon adhesion to laminin- or fibronectin-coated, but not uncoated, plastic there is a depolymerization of actin in neutrophils. This phenomenon was not affected by inhibitors of the more well-studied components of the signal transduction pathway, specifically, pertussis toxin, an inhibitor of G-proteins, H-7 or staurosporine, inhibitors of protein kinase C, or herbimycin A, an inhibitor of nonreceptor tyrosine kinase. We therefore focused our attention on actin-binding proteins and measured the changes in the partitioning of gelsolin between the Triton X-100-soluble and -insoluble cellular fractions which occur upon neutrophil adhesion by means of quantitating anti-gelsolin antibody binding to aliquots of these fractions. It was found that approximately 90% of the total cellular gelsolin was found in the Triton X-100-soluble fraction in suspended cells, but that upon adherence to either fibronectin- or laminin-coated plastic about 40% of the soluble gelsolin could be detected in the insoluble fraction. This effect was not observed in cells adherent to uncoated plastic, wherein more than 90% of the gelsolin was found in the soluble fraction. Results of immunofluorescence microscopy of these cell preparations was consistent with this data. A gelsolin translocation to the insoluble cellular actin network may account for a part of the observed actin depolymerization. | lld:pubmed |
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| pubmed-article:9017600 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9017600 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9017600 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9017600 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9017600 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9017600 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:9017600 | pubmed:author | pubmed-author:ZanerK SKS | lld:pubmed |
| pubmed-article:9017600 | pubmed:author | pubmed-author:TauberA IAI | lld:pubmed |
| pubmed-article:9017600 | pubmed:author | pubmed-author:WangJ SJS | lld:pubmed |
| pubmed-article:9017600 | pubmed:author | pubmed-author:CoburnJ PJP | lld:pubmed |
| pubmed-article:9017600 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9017600 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:9017600 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9017600 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9017600 | pubmed:pagination | 121-8 | lld:pubmed |
| pubmed-article:9017600 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9017600 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9017600 | pubmed:articleTitle | Role of gelsolin in actin depolymerization of adherent human neutrophils. | lld:pubmed |
| pubmed-article:9017600 | pubmed:affiliation | Department of Medicine, Boston University School of Medicine, Massachusetts 02118, USA. | lld:pubmed |
| pubmed-article:9017600 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9017600 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9017600 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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