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Sequential cleavage of poly(ADP-ribose)polymerase and appearance of a small Bax-immunoreactive protein are blocked by Bcl-X(L) and caspase inhibitors during staurosporine-induced dopaminergic neuronal apoptosis.

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dc.contributor.authorKim, JE-
dc.contributor.authorOh, JH-
dc.contributor.authorChoi, WS-
dc.contributor.authorChang, II-
dc.contributor.authorSohn, S-
dc.contributor.authorKrajewski, S-
dc.contributor.authorReed, JC-
dc.contributor.authorO'Malley, KL-
dc.contributor.authorOh, YJ-
dc.date.accessioned2011-09-16T05:26:01Z-
dc.date.available2011-09-16T05:26:01Z-
dc.date.issued1999-
dc.identifier.issn0022-3042-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/4195-
dc.description.abstractTo assess the role of Bcl-X(L) and its splice derivative, Bcl-X(S), in staurosporine-induced cell death, we used a dopaminergic cell line, MN9D, transfected with bcl-xL (MN9D/Bcl-X(L)), bcl-xS (MN9D/Bcl-X(S)), or control vector (MN9D/Neo). Only 8.6% of MN9D/Neo cells survived after 24 h of 1 microM staurosporine treatment. Caspase activity was implicated because a caspase inhibitor, N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone (Z-VAD-fmk), attenuated staurosporine-induced cell death. Bcl-X(L) rescued MN9D cells from death (89.4% viable cells), whereas Bcl-X(S) had little or no effect. Bcl-X(L) prevented morphologically apoptotic changes as well as cleavage of poly(ADP-ribose)polymerase (PARP) induced by staurosporine. It is interesting that a small Bax-immunoreactive protein appeared 4-8 h after PARP cleavage in MN9D/Neo cells. The appearance of the small Bax-immunoreactive protein, however, may be cell type-specific as it was not observed in PC12 cells after staurosporine treatment. The sequential cleavage of PARP and the appearance of the small Bax-immunoreactive protein in MN9D cells were blocked either by Z-VAD-fmk or by Bcl-X(L). Thus, our present study suggests that Bcl-X(L) but not Bcl-X(S) prevents staurosporine-induced apoptosis by inhibiting the caspase activation that may be directly or indirectly responsible for the appearance of the small Bax-immunoreactive protein in some types of neurons.-
dc.language.isoen-
dc.subject.MESHAnimals-
dc.subject.MESHApoptosis-
dc.subject.MESHCaspases-
dc.subject.MESHCell Line-
dc.subject.MESHCycloheximide-
dc.subject.MESHDopamine-
dc.subject.MESHKinetics-
dc.subject.MESHMice-
dc.subject.MESHNeurons-
dc.subject.MESHPoly(ADP-ribose) Polymerases-
dc.subject.MESHProto-Oncogene Proteins-
dc.subject.MESHProto-Oncogene Proteins c-bcl-2-
dc.subject.MESHRecombinant Proteins-
dc.subject.MESHStaurosporine-
dc.subject.MESHTransfection-
dc.subject.MESHbcl-2-Associated X Protein-
dc.subject.MESHbcl-X Protein-
dc.titleSequential cleavage of poly(ADP-ribose)polymerase and appearance of a small Bax-immunoreactive protein are blocked by Bcl-X(L) and caspase inhibitors during staurosporine-induced dopaminergic neuronal apoptosis.-
dc.typeArticle-
dc.identifier.pmid10349855-
dc.identifier.urlhttp://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0022-3042&date=1999&volume=72&issue=6&spage=2456-
dc.contributor.affiliatedAuthor손, 성향-
dc.type.localJournal Papers-
dc.citation.titleJournal of neurochemistry-
dc.citation.volume72-
dc.citation.number6-
dc.citation.date1999-
dc.citation.startPage2456-
dc.citation.endPage2463-
dc.identifier.bibliographicCitationJournal of neurochemistry, 72(6). : 2456-2463, 1999-
dc.identifier.eissn1471-4159-
dc.relation.journalidJ000223042-
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Journal Papers > School of Medicine / Graduate School of Medicine > Microbiology
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