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Article: Proteomic approach to study the cytotoxicity of dioscin (saponin)

TitleProteomic approach to study the cytotoxicity of dioscin (saponin)
Authors
KeywordsCytotoxicity
Dioscin
Drug mechanism
HL-60 cells
Mitochondria
Saponin
Issue Date2006
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics
Citation
Proteomics, 2006, v. 6 n. 8, p. 2422-2432 How to Cite?
AbstractDioscin, extracted from the root of Polygonatum zanlanscianense pamp, exhibits cytotoxicity towards human myeloblast leukemia HL-60 cells. Proteomic analysis revealed that the expression of mitochondrial associated proteins was substantially altered in HL-60 cells corresponding to the dioscin treatment, suggesting that mitochondria are the major cellular target of dioscin. Mitochondrial functional studies validated that mitochondrial apoptotic pathway was initiated by dioscin treatment. Changes in proteome other than mitochondrial related proteins implicate that other mechanisms were also involved in dioscin-induced apoptosis in HL-60 cells, including the activity impairment in protein synthesis, alterations of phosphatases in cell signaling, and deregulation of oxidative stress and cell proliferation. Current study of protein alterations in dioscin-treated HL-60 cells suggested that dioscin exerts cytotoxicity through multiple apoptosis-inducing pathways. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
Persistent Identifierhttp://hdl.handle.net/10722/48497
ISSN
2023 Impact Factor: 3.4
2023 SCImago Journal Rankings: 1.011
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_HK
dc.contributor.authorYim, HCen_HK
dc.contributor.authorYang, Zen_HK
dc.contributor.authorChiu, JFen_HK
dc.contributor.authorChe, CMen_HK
dc.contributor.authorHe, QYen_HK
dc.date.accessioned2008-05-22T04:15:18Z-
dc.date.available2008-05-22T04:15:18Z-
dc.date.issued2006en_HK
dc.identifier.citationProteomics, 2006, v. 6 n. 8, p. 2422-2432en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48497-
dc.description.abstractDioscin, extracted from the root of Polygonatum zanlanscianense pamp, exhibits cytotoxicity towards human myeloblast leukemia HL-60 cells. Proteomic analysis revealed that the expression of mitochondrial associated proteins was substantially altered in HL-60 cells corresponding to the dioscin treatment, suggesting that mitochondria are the major cellular target of dioscin. Mitochondrial functional studies validated that mitochondrial apoptotic pathway was initiated by dioscin treatment. Changes in proteome other than mitochondrial related proteins implicate that other mechanisms were also involved in dioscin-induced apoptosis in HL-60 cells, including the activity impairment in protein synthesis, alterations of phosphatases in cell signaling, and deregulation of oxidative stress and cell proliferation. Current study of protein alterations in dioscin-treated HL-60 cells suggested that dioscin exerts cytotoxicity through multiple apoptosis-inducing pathways. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.en_HK
dc.format.extent1192721 bytes-
dc.format.extent254114 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypeapplication/pdf-
dc.languageengen_HK
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomicsen_HK
dc.relation.ispartofProteomicsen_HK
dc.rightsPublished in Proteomics, 2006, v. 6 n. 8, p. 2422-2432en_HK
dc.subjectCytotoxicityen_HK
dc.subjectDioscinen_HK
dc.subjectDrug mechanismen_HK
dc.subjectHL-60 cellsen_HK
dc.subjectMitochondriaen_HK
dc.subjectSaponinen_HK
dc.titleProteomic approach to study the cytotoxicity of dioscin (saponin)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1615-9853&volume=6&issue=8&spage=2422&epage=2432&date=2006&atitle=Proteomic+approach+to+study+the+cytotoxicity+of+dioscin+(saponin)en_HK
dc.identifier.emailChe, CM:cmche@hku.hken_HK
dc.identifier.authorityChe, CM=rp00670en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1002/pmic.200500595en_HK
dc.identifier.pmid16548062-
dc.identifier.scopuseid_2-s2.0-33646251378en_HK
dc.identifier.hkuros120628-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33646251378&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume6en_HK
dc.identifier.issue8en_HK
dc.identifier.spage2422en_HK
dc.identifier.epage2432en_HK
dc.identifier.isiWOS:000237398700011-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridWang, Y=7601510411en_HK
dc.identifier.scopusauthoridYim, HC=13205446900en_HK
dc.identifier.scopusauthoridYang, Z=13205034800en_HK
dc.identifier.scopusauthoridChiu, JF=7201501692en_HK
dc.identifier.scopusauthoridChe, CM=7102442791en_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK
dc.identifier.issnl1615-9853-

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