| pubmed-article:2768336 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2768336 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2768336 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:2768336 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:2768336 | lifeskim:mentions | umls-concept:C0018321 | lld:lifeskim |
| pubmed-article:2768336 | lifeskim:mentions | umls-concept:C0314672 | lld:lifeskim |
| pubmed-article:2768336 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2768336 | pubmed:dateCreated | 1989-10-4 | lld:pubmed |
| pubmed-article:2768336 | pubmed:abstractText | The effects of exogenous guanine nucleotides on the polymerization of actin in human neutrophils were tested in an electropermeabilized cell preparation. Close to 40% permeabilization was achieved with a single electric discharge as measured by nucleic acid staining with ethidium bromide or propidium iodide with minimal (less than 2%) release of the cytoplasmic marker lactate dehydrogenase. In addition, electropermeabilized neutrophils retained their capacity to produce superoxide anions and to sustain a polymerization of actin in response to surface-receptor dependent stimuli such as chemotactic factors. Electropermeabilization produced a rapid and transient permeabilization that allowed the entry of guanine nucleotides into the cells. GTP and, to a larger extent, its nonhydrolyzable analog guanosine 5'-O-2-thiotriphosphate (GTP[S]), induced a time- and concentration-dependent polymerization of actin, as determined by increased staining with 7-nitrobenz-2-oxa-1,3-diazolylphallacidin. The effects of the aforementioned guanine nucleotides were antagonized by GDP[S], but were insensitive to pertussis toxin. Cholera toxin potentiated to a small degree the amount of actin polymerization induced by GTP[S]. These results provided direct evidence for the involvement of GTP-binding proteins in the regulation of the organization of the cytoskeleton of neutrophils, an event that is of crucial importance to the performance of the defense-oriented functions of these cells. | lld:pubmed |
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| pubmed-article:2768336 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2768336 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2768336 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2768336 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2768336 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:2768336 | pubmed:author | pubmed-author:NaccacheP HPH | lld:pubmed |
| pubmed-article:2768336 | pubmed:author | pubmed-author:TherrienSS | lld:pubmed |
| pubmed-article:2768336 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2768336 | pubmed:volume | 109 | lld:pubmed |
| pubmed-article:2768336 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2768336 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2768336 | pubmed:pagination | 1125-32 | lld:pubmed |
| pubmed-article:2768336 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2768336 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2768336 | pubmed:articleTitle | Guanine nucleotide-induced polymerization of actin in electropermeabilized human neutrophils. | lld:pubmed |
| pubmed-article:2768336 | pubmed:affiliation | Département de Médecine, Université Laval, Ste Foy, Québec, Canada. | lld:pubmed |
| pubmed-article:2768336 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2768336 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2768336 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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