| pubmed-article:10739672 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C0021701 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C2936824 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C0009085 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C1554184 | lld:lifeskim |
| pubmed-article:10739672 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10739672 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10739672 | pubmed:dateCreated | 2000-5-12 | lld:pubmed |
| pubmed-article:10739672 | pubmed:abstractText | The beta(2)-integrins on leukocytes can serve as a signaling unit during cell adhesion and locomotion, and to further clarify this important property we investigated the possible mechanisms of beta(2)-integrin-induced activation of PtdIns 3-kinase. It has previously been demonstrated that clustering of beta(2)-integrins activates p21(ras) by a tyrosine kinase-dependent pathway, and here we show that active p21(ras) interacts with its downstream target, PtdIns 3-kinase. Engagement of beta(2)-integrins also activates the tyrosine kinases p58(c-fgr) and p59/61(hck) and causes them to associate with the p85 subunit of PtdIns 3-kinase. These findings suggest a mechanism whereby p58(c-fgr) and p59/61(hck) are directly involved in the activation of PtdIns 3-kinase. No coupling between p58(c-fgr) and p59/61(hck) could be detected; hence these kinases probably trigger independent but parallel signals to PtdIns 3-kinase. The effect of beta(2)-integrin clustering on PtdIns 3-kinase activity was monitored as the activation of protein kinase B (PKB). Stimulation of PKB by beta(2)-integrins was abolished by genistein and wortmannin but not by using methyl transferase inhibitors to abrogate the influence of p21(ras)-related proteins. Thus, even if PtdIns 3-kinase is not activated by p21(ras), it can maintain full enzyme activity due to the mentioned interaction with p58(c-fgr) or p59/61(hck). These tyrosine kinases apparently activate similar pathways that operate in parallel and therefore have the potential to substitute for each other in mediating adhesion and regulating cell locomotion. | lld:pubmed |
| pubmed-article:10739672 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10739672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10739672 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10739672 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10739672 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:10739672 | pubmed:author | pubmed-author:SmithDD | lld:pubmed |
| pubmed-article:10739672 | pubmed:author | pubmed-author:AnderssonTT | lld:pubmed |
| pubmed-article:10739672 | pubmed:author | pubmed-author:ZhengLL | lld:pubmed |
| pubmed-article:10739672 | pubmed:author | pubmed-author:AxelssonLL | lld:pubmed |
| pubmed-article:10739672 | pubmed:author | pubmed-author:HellbergCC | lld:pubmed |
| pubmed-article:10739672 | pubmed:author | pubmed-author:MelanderFF | lld:pubmed |
| pubmed-article:10739672 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:10739672 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10739672 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:10739672 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:10739672 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10739672 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10739672 | pubmed:pagination | 257-63 | lld:pubmed |
| pubmed-article:10739672 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
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| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:meshHeading | pubmed-meshheading:10739672... | lld:pubmed |
| pubmed-article:10739672 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10739672 | pubmed:articleTitle | Clustering of beta(2)-integrins on human neutrophils activates dual signaling pathways to PtdIns 3-kinase. | lld:pubmed |
| pubmed-article:10739672 | pubmed:affiliation | Division of Experimental Pathology, Lund University, Malmö, Sweden. | lld:pubmed |
| pubmed-article:10739672 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10739672 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:10739672 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:2268 | entrezgene:pubmed | pubmed-article:10739672 | lld:entrezgene |
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