Investigation protein arginine methylation in oral cancer cell lines

碩士 === 中山醫學大學 === 生物醫學科學學系碩士班 === 103 === Protein arginine methylation is a posttranslational modification implicated in signal transduction, gene transcription, DNA repair and RNA processing. Overexpression or deregulation of protein arginine methyltransferases (PRMTs) have been reported to be asso...

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Main Authors: Chien-Ping Chang, 張建評
Other Authors: Chuan-Li
Format: Others
Language:zh-TW
Published: 2015
Online Access:http://ndltd.ncl.edu.tw/handle/98594626288439986698
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spelling ndltd-TW-103CSMU51140142016-11-06T04:19:42Z http://ndltd.ncl.edu.tw/handle/98594626288439986698 Investigation protein arginine methylation in oral cancer cell lines 口腔癌細胞株的蛋白質精胺酸甲基化研究 Chien-Ping Chang 張建評 碩士 中山醫學大學 生物醫學科學學系碩士班 103 Protein arginine methylation is a posttranslational modification implicated in signal transduction, gene transcription, DNA repair and RNA processing. Overexpression or deregulation of protein arginine methyltransferases (PRMTs) have been reported to be associated with various cancers. However, there have been no reports studying protein arginine methylation in head and neck cancer (HNC). Oral cancer accounts for the largest group in head and neck cancers. In this study we thus investigate the involvement of the modification in HNC using oral (S-G) and oral cancer cell lines(SAS, OECM-1, HSC-3, SCC-9). Other human cancer cell lines such as MCF7 (breast cancer cell line) and HeLa (breast cancer cell line) are included for comparison. The level of asymmetric dimethylarginine (ADMA) are high in HeLa, MCF-7, S-G, SAS, OECM-1, and low in HSC-3 and SCC-9 as detected by an ADMA-specific antibody. The predominant PRMT1 is expressed in all cancer cell lines, and the protein levels of PRMT1 in HSC-3 and SCC-9 are lower than that in other cell lines, generally consistent with the levels of ADMA signals. Interestingly, growth rate of SAS and OECM-1 is higher than that of HSC-3, similar to the level of PRMT1 and ADMA. We then treated the cells with an indirect methyltransferase inhibitor AdOx. AdOx treatment decrease ADMA level, cell proliferation and cell migration. Knockdown PRMT1 expression by siRNA to about 50%, however, did not decrease ADMA level, cell proliferation and cell migration of the oral cancer cells. Further investigation to knockout specific PRMTs in the oral cancer cell lines should provide more valuable information for protein arginine methylation in HNC. Chuan-Li 李娟 2015 學位論文 ; thesis 74 zh-TW
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description 碩士 === 中山醫學大學 === 生物醫學科學學系碩士班 === 103 === Protein arginine methylation is a posttranslational modification implicated in signal transduction, gene transcription, DNA repair and RNA processing. Overexpression or deregulation of protein arginine methyltransferases (PRMTs) have been reported to be associated with various cancers. However, there have been no reports studying protein arginine methylation in head and neck cancer (HNC). Oral cancer accounts for the largest group in head and neck cancers. In this study we thus investigate the involvement of the modification in HNC using oral (S-G) and oral cancer cell lines(SAS, OECM-1, HSC-3, SCC-9). Other human cancer cell lines such as MCF7 (breast cancer cell line) and HeLa (breast cancer cell line) are included for comparison. The level of asymmetric dimethylarginine (ADMA) are high in HeLa, MCF-7, S-G, SAS, OECM-1, and low in HSC-3 and SCC-9 as detected by an ADMA-specific antibody. The predominant PRMT1 is expressed in all cancer cell lines, and the protein levels of PRMT1 in HSC-3 and SCC-9 are lower than that in other cell lines, generally consistent with the levels of ADMA signals. Interestingly, growth rate of SAS and OECM-1 is higher than that of HSC-3, similar to the level of PRMT1 and ADMA. We then treated the cells with an indirect methyltransferase inhibitor AdOx. AdOx treatment decrease ADMA level, cell proliferation and cell migration. Knockdown PRMT1 expression by siRNA to about 50%, however, did not decrease ADMA level, cell proliferation and cell migration of the oral cancer cells. Further investigation to knockout specific PRMTs in the oral cancer cell lines should provide more valuable information for protein arginine methylation in HNC.
author2 Chuan-Li
author_facet Chuan-Li
Chien-Ping Chang
張建評
author Chien-Ping Chang
張建評
spellingShingle Chien-Ping Chang
張建評
Investigation protein arginine methylation in oral cancer cell lines
author_sort Chien-Ping Chang
title Investigation protein arginine methylation in oral cancer cell lines
title_short Investigation protein arginine methylation in oral cancer cell lines
title_full Investigation protein arginine methylation in oral cancer cell lines
title_fullStr Investigation protein arginine methylation in oral cancer cell lines
title_full_unstemmed Investigation protein arginine methylation in oral cancer cell lines
title_sort investigation protein arginine methylation in oral cancer cell lines
publishDate 2015
url http://ndltd.ncl.edu.tw/handle/98594626288439986698
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