Cited 0 times in Scipus Cited Count

Overexpression of Par-4 sensitizes TRAIL-induced apoptosis via inactivation of NF-kappaB and Akt signaling pathways in renal cancer cells.

DC Field Value Language
dc.contributor.authorLee, TJ-
dc.contributor.authorJang, JH-
dc.contributor.authorNoh, HJ-
dc.contributor.authorPark, EJ-
dc.contributor.authorChoi, KS-
dc.contributor.authorKwon, TK-
dc.date.accessioned2011-05-31T01:59:08Z-
dc.date.available2011-05-31T01:59:08Z-
dc.date.issued2010-
dc.identifier.issn0730-2312-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/2732-
dc.description.abstractThe prostate-apoptosis-response-gene-4 (Par-4) is up-regulated in prostate cells undergoing programmed cell death. Furthermore, Par-4 protein has been shown to function as an effector of cell death in response to various apoptotic stimuli that trigger mitochondria and membrane receptor-mediated cell death pathways. In this study, we investigated how Par-4 modulates TRAIL-mediated apoptosis in TRAIL-resistant Caki cells. Par-4 overexpressing cells were strikingly sensitive to apoptosis induced by TRAIL compared with control cells. Par-4 overexpressing Caki cells treated with TRAIL showed an increased activation of the initiator caspase-8 and the effector caspase-3, together with an enforced cleavage of XIAP and c-FLIP. TRAIL-induced reduction of XIAP and c-FLIP protein levels in Par-4 overexpressing cells was prevented by z-VAD pretreatment. In addition, the surface DR5 protein level was increased in TRAIL-treated Par-4 overexpressing cells. Interestingly, even though a deletion of leucine zipper domain in Par-4 recovered Bcl-2 level to basal level induced by wild type Par-4, it partly decreased sensitivity to TRAIL in Caki cells. In addition, exposure of Caki/Par-4 cells to TRAIL led to reduction of phosphorylated Akt levels, but deletion of leucine zipper domain of Par-4 did not affect these phosphorylated Akt levels. In conclusion, we here provide evidence that ectopic expression of Par-4 sensitizes Caki cells to TRAIL via modulation of multiple targets, including DR5, Bcl-2, Akt, and NF-kappaB.-
dc.language.isoen-
dc.subject.MESHAntigens, CD95-
dc.subject.MESHApoptosis-
dc.subject.MESHApoptosis Regulatory Proteins-
dc.subject.MESHCASP8 and FADD-Like Apoptosis Regulating Protein-
dc.subject.MESHCaspase 8-
dc.subject.MESHCell Line, Tumor-
dc.subject.MESHCycloheximide-
dc.subject.MESHEnzyme Activation-
dc.subject.MESHHumans-
dc.subject.MESHKidney Neoplasms-
dc.subject.MESHLeucine Zippers-
dc.subject.MESHNF-kappa B-
dc.subject.MESHPhosphorylation-
dc.subject.MESHProtein Structure, Tertiary-
dc.subject.MESHProto-Oncogene Proteins c-akt-
dc.subject.MESHReceptors, Death Domain-
dc.subject.MESHSequence Deletion-
dc.subject.MESHSignal Transduction-
dc.subject.MESHTNF-Related Apoptosis-Inducing Ligand-
dc.subject.MESHTumor Necrosis Factor-alpha-
dc.subject.MESHX-Linked Inhibitor of Apoptosis Protein-
dc.titleOverexpression of Par-4 sensitizes TRAIL-induced apoptosis via inactivation of NF-kappaB and Akt signaling pathways in renal cancer cells.-
dc.typeArticle-
dc.identifier.pmid20127709-
dc.contributor.affiliatedAuthor최, 경숙-
dc.type.localJournal Papers-
dc.identifier.doi10.1002/jcb.22504-
dc.citation.titleJournal of cellular biochemistry-
dc.citation.volume109-
dc.citation.number5-
dc.citation.date2010-
dc.citation.startPage885-
dc.citation.endPage895-
dc.identifier.bibliographicCitationJournal of cellular biochemistry, 109(5). : 885-895, 2010-
dc.identifier.eissn1097-4644-
dc.relation.journalidJ007302312-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
Files in This Item:
There are no files associated with this item.

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse