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Article: Akt Is Activated in Response to an Apoptotic Signal

TitleAkt Is Activated in Response to an Apoptotic Signal
Authors
Issue Date2001
Citation
Journal of Biological Chemistry, 2001, v. 276, n. 32, p. 30461-30466 How to Cite?
AbstractAkt is a serine-threonine kinase known to exert anti-apoptotic effects through several downstream targets. Akt is cleaved during mitochondrial-mediated apoptosis in a caspase-dependent manner. The reason for this is not clear, however, because Akt has not been demonstrated to be activated in response to mitochondrial apoptotic stimuli. Accordingly, we explored whether the well described mitochondrial apoptotic stimuli staurosporine (STS) and etoposide activate Akt and whether such activation impacts apoptosis. Both STS and etoposide activated Akt in NIH 3T3 cells, maximally at 8 and 2 h, respectively, preceding the onset of apoptosis and poly(ADP-ribose) polymerase cleavage. The overexpression of Akt delayed STS-induced apoptosis with an even more pronounced delay observed with overexpression of constitutively active Akt. Akt activation by proapoptotic stimuli lay upstream of mitochondria, because neither caspase inhibitors nor overexpression of Bcl-2 or Bcl-xL could prevent it. Activation depended on phosphatidylinositol 3-kinase activity, however. Conversely, inhibition of phosphatidylinositol 3-kinase with wort-mannin sensitized cells to apoptosis initiated by STS. These data demonstrate that mitochondrial apoptotic stimuli also activate Akt and such activation modulates apoptosis in this setting.
Persistent Identifierhttp://hdl.handle.net/10722/291581
ISSN
2020 Impact Factor: 5.157
2023 SCImago Journal Rankings: 1.766
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTang, Damu-
dc.contributor.authorOkada, Hitoshi-
dc.contributor.authorRuland, Jurgen-
dc.contributor.authorLiu, Lieqi-
dc.contributor.authorStambolic, Vuk-
dc.contributor.authorMak, Tak W.-
dc.contributor.authorIngram, Alistair J.-
dc.date.accessioned2020-11-17T14:54:41Z-
dc.date.available2020-11-17T14:54:41Z-
dc.date.issued2001-
dc.identifier.citationJournal of Biological Chemistry, 2001, v. 276, n. 32, p. 30461-30466-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/291581-
dc.description.abstractAkt is a serine-threonine kinase known to exert anti-apoptotic effects through several downstream targets. Akt is cleaved during mitochondrial-mediated apoptosis in a caspase-dependent manner. The reason for this is not clear, however, because Akt has not been demonstrated to be activated in response to mitochondrial apoptotic stimuli. Accordingly, we explored whether the well described mitochondrial apoptotic stimuli staurosporine (STS) and etoposide activate Akt and whether such activation impacts apoptosis. Both STS and etoposide activated Akt in NIH 3T3 cells, maximally at 8 and 2 h, respectively, preceding the onset of apoptosis and poly(ADP-ribose) polymerase cleavage. The overexpression of Akt delayed STS-induced apoptosis with an even more pronounced delay observed with overexpression of constitutively active Akt. Akt activation by proapoptotic stimuli lay upstream of mitochondria, because neither caspase inhibitors nor overexpression of Bcl-2 or Bcl-xL could prevent it. Activation depended on phosphatidylinositol 3-kinase activity, however. Conversely, inhibition of phosphatidylinositol 3-kinase with wort-mannin sensitized cells to apoptosis initiated by STS. These data demonstrate that mitochondrial apoptotic stimuli also activate Akt and such activation modulates apoptosis in this setting.-
dc.languageeng-
dc.relation.ispartofJournal of Biological Chemistry-
dc.titleAkt Is Activated in Response to an Apoptotic Signal-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M102045200-
dc.identifier.pmid11399756-
dc.identifier.scopuseid_2-s2.0-0035839614-
dc.identifier.volume276-
dc.identifier.issue32-
dc.identifier.spage30461-
dc.identifier.epage30466-
dc.identifier.isiWOS:000170558000112-
dc.identifier.issnl0021-9258-

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