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  4. Proteomics analysis of A375 human malignant melanoma cells in response to arbutin treatment
 
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Proteomics analysis of A375 human malignant melanoma cells in response to arbutin treatment

Resource
Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1794 (2): 159-167
Journal
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics
Pages
159-167
Date Issued
2009
Date
2009
Author(s)
Nawarak, Jiraporn
Huang-Liu, Rosa
Kao, Shao-Hsuan
Liao, Hsien-Hua
Sinchaikul, Supachok
Chen, Shui-Tein
Cheng, Sun-Long
DOI
10.1016/j.bbapap.2008.09.023
URI
http://ntur.lib.ntu.edu.tw//handle/246246/163164
Abstract
Although the toxicogenomics of A375 human malignant melanoma cells treated with arbutin have been elucidated using DNA microarray, the proteomics of the cellular response to this compound are still poorly understood. In this study, we performed proteomic analyses to investigate the anticancer effect of arbutin on the protein expression profile in A375 cells. After treatment with arbutin (8?μg/ml) for 24, 48 and 72?h, the proteomic profiles of control and arbutin-treated A375 cells were compared, and 26 differentially expressed proteins (7 upregulated and 19 downregulated proteins) were identified by MALDI-Q-TOF MS and MS/MS. Among these proteins, 13 isoforms of six identical proteins were observed. Bioinformatic tools were used to search for protein function and to predict protein interactions. The interaction network of 14 differentially expressed proteins was found to be correlated with the downstream regulation of p53 tumor suppressor and cell apoptosis. In addition, three upregulated proteins (14-3-3G, VDAC-1 and p53) and five downregulated proteins (ENPL, ENOA, IMDH2, PRDX1 and VIME) in arbutin-treated A375 cells were validated by RT-PCR analysis. These proteins were found to play important roles in the suppression of cancer development. ? 2008 Elsevier B.V. All rights reserved.
Subjects
A375 cells; Arbutin; Cancer; Malignant melanoma; Proteomics
SDGs

[SDGs]SDG3

Other Subjects
alpha enolase; arbutin; cell protein; endoplasmin precursor; inosinate dehydrogenase; peroxiredoxin 1; protein 14 3 3; protein 14 3 3 gamma; protein enpl; protein p53; tumor suppressor protein; unclassified drug; vimentin; voltage dependent anion channel 1; amino acid sequence; antineoplastic activity; apoptosis; article; carcinogenesis; concentration response; controlled study; human; human cell; matrix assisted laser desorption ionization time of flight mass spectrometry; melanoma cell; nucleotide sequence; priority journal; protein analysis; protein expression; protein function; protein protein interaction; proteomics; reverse transcription polymerase chain reaction; Antineoplastic Agents; Arbutin; Cell Line, Tumor; Down-Regulation; Humans; Melanoma; Metabolic Networks and Pathways; Protein Binding; Proteomics; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tandem Mass Spectrometry; Up-Regulation
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