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Proteomic approach to study the cytotoxicity of dioscin (saponin)
Author(s) -
Wang Ying,
Cheung Yim Hing,
Yang Zhiqi,
Chiu JenFu,
Che ChiMing,
He QingYu
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500595
Subject(s) - cytotoxicity , apoptosis , mitochondrion , biology , proteome , microbiology and biotechnology , cell growth , proteomics , cell , oxidative stress , signal transduction , biochemistry , in vitro , gene
Dioscin, 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.