Study of the cellular mechanism induced by nanogold particles
| Autor: | Tsai, Yenyin, 蔡雁尹 |
|---|---|
| Jazyk: | zh-TW |
| Rok vydání: | 2011 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 99 In previous study, we observed a growth inhibition and apoptotic/necrotic phenotype in the AuNPs treated human chronic myelogenous leukemia K562 cells. To dissect the cellular mechanisms elicited by AuNPs, proteomic techniques, 2-DE/MS, were utilized to analyze the identities of differentially expressed and heat shock protein. When analyzing the proteomic data by systems biology software, endoplasmic reticulum (ER) stress response was suggested as the major elicited event. This study first assessed the toxicity associated with the size of AuNPs, and discovered that the smaller particle size of AuNPs had higher cytotoxicity. For the 3-5 nm of AuNPs, most cells about their semi-lethal dose were approximately 5ppm. The cytotoxicity of two different chemical chemical AuNPs and AuNRs were simultaneously analysed, and discovered that chemical AuNPs caused more severe cytotoxicity. AuNPs could enter the cells, and increased with incubation time, while TEM showed that AuNPs could enter the endoplasmic reticulum. Moreover, the AuNP treated K562 cells demonstrated a similar expression profile of ER stress marker proteins as that elicited by the standard ER stress inducer, thapsigargin. When AuNPs and TG-induced endoplasmic reticulum stress, intracellular ROS and mitochondrial damage will be increased, and then induced apoptosis or necrosis. But AuNPs-induced endoplasmic reticulum stress was independent of intracellular calcium concentration, and different with TG. In addition, this study used mRNA microarray technology combining with systems biology analysis to investigate meaning of AuNPs-induced gene expression, and also related to endoplasmic reticulum stress. However, this study developed a AuNPs affinity chromatography method to understand the mechanism of AuNPs into the cell. AuNPs and variety of proteins in blood could closed link by ionic and hydrophobic interaction. This data hinted that aforementioned proteins played some function when AuNPs were into animal cells by oral and injection modes. These protein identity were identified by mass spectrometry, and discovered that AuNPs could combine with most of the blood proteins. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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