http://purl.uniprot.org/citations/16807302 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16807302 | http://www.w3.org/2000/01/rdf-schema#comment | "Maintenance of bone structural integrity depends in part on the rate of apoptosis of bone-forming osteoblasts. Because substrate adhesion is an important regulator of apoptosis, we have investigated the role of focal adhesions in regulating bone cell apoptosis. To test this, we expressed a truncated form of alpha-actinin (ROD-GFP) that competitively displaces endogenous alpha-actinin from focal adhesions, thus disrupting focal adhesions. Immunofluorescence and morphometric analysis of vinculin and tyrosine phosphorylation revealed that ROD-GFP expression dramatically disrupted focal adhesion organization and reduced tyrosine phosphorylation at focal adhesions. In addition, Bcl-2 protein levels were reduced in ROD-GFP-expressing cells, but caspase 3 cleavage, poly(ADP-ribose) polymerase cleavage, histone H2A.X phosphorylation, and cytotoxicity were not increased due to ROD-GFP expression alone. Increases in both ERK and Akt phosphorylation were also observed in ROD-GFP-expressing cells, although inhibition of either ERK or Akt individually or together failed to induce apoptosis. However, we did find that ROD-GFP expression sensitized, whereas alpha-actinin-GFP expression protected, cells from TNF-alpha-induced apoptosis. Further investigation revealed that activation of TNF-alpha-induced survival signals, specifically Akt phosphorylation and NF-kappaB activation, was inhibited in ROD-GFP-expressing cells. The reduced expression of antiapoptotic Bcl-2 and inhibited survival signaling rendered ROD-GFP-expressing cells more susceptible to TNF-alpha-induced apoptosis. Thus we conclude that alpha-actinin plays a role in regulating cell survival through stabilization of focal adhesions and regulation of TNF-alpha-induced survival signaling."xsd:string |
http://purl.uniprot.org/citations/16807302 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajpcell.00113.2006"xsd:string |
http://purl.uniprot.org/citations/16807302 | http://purl.uniprot.org/core/author | "Pavalko F.M."xsd:string |
http://purl.uniprot.org/citations/16807302 | http://purl.uniprot.org/core/author | "Triplett J.W."xsd:string |
http://purl.uniprot.org/citations/16807302 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16807302 | http://purl.uniprot.org/core/name | "Am J Physiol Cell Physiol"xsd:string |
http://purl.uniprot.org/citations/16807302 | http://purl.uniprot.org/core/pages | "C909-21"xsd:string |
http://purl.uniprot.org/citations/16807302 | http://purl.uniprot.org/core/title | "Disruption of alpha-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosis."xsd:string |
http://purl.uniprot.org/citations/16807302 | http://purl.uniprot.org/core/volume | "291"xsd:string |
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http://purl.uniprot.org/uniprot/Q08043#attribution-96FCE0B20FE87692B9C465BF6A4E7034 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/16807302 |
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