東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Alteration of histone modifications ...

Ke, Qingdong.

FindBook

Google Book

Amazon

博客來

Alteration of histone modifications by nickel compounds: Epigenetic mechanisms.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Alteration of histone modifications by nickel compounds: Epigenetic mechanisms./
作者:	Ke, Qingdong.
面頁冊數:	158 p.
附註:	Adviser: Max Costa.
Contained By:	Dissertation Abstracts International68-01B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3247368

Alteration of histone modifications by nickel compounds: Epigenetic mechanisms.
Ke, Qingdong.

Alteration of histone modifications by nickel compounds: Epigenetic mechanisms. - 158 p.

Adviser: Max Costa.

Thesis (Ph.D.)--New York University, 2007.

Nickel (Ni) compounds are known carcinogens and the carcinogenicity of different forms of Ni compounds varies with their water solubility. Due to their weak mutagenecity, epigenetic mechanisms likely play an important role in Ni carcinogenesis. This project investigated epigenetic effects of Ni compounds in cells. The results demonstrated that both water soluble and insoluble Ni compounds were taken up by cells, resulting in Ni ion accumulation in the cytoplasm and nucleus. When the exposure was ceased, Ni ions persisted in both sites in the insoluble Ni-exposed cells longer than in the soluble Ni-exposed ones. It was found that Ni exposure caused alterations in histone modifications at the global level in cells. Among these were: loss of acetylation of all four core histones, and increases of H3K9 dimethylation. These changes in histone modification were implicated in Ni-induced transgene silencing. In addition, Ni exposure also resulted in an increase in H3S10 phosphorylation and ubiquitination of H2A and H2B. Exploration of the mechanisms by which Ni induced these increases in histone modifications revealed that Ni activated JNK-MAPK pathway which induced H3S10 phosphorylation. In vitro studies of histone ubiquitination and deubiquitination suggested that Ni elevated histone ubiquitination by inhibition the deubiquitinating enzyme activity. These studies have demonstrated strong epigenetic effects of Ni in cells which are important in its toxicity and carcinogenicity. In addition, the results present a likely explanation for the difference in carcinogenicity between water soluble and insoluble Ni compounds in experimental animals, as well as suggesting a possible mechanism for why insoluble Ni compounds are more potent carcinogens than the soluble species.Subjects--Topical Terms:

1017719
Biology, Molecular.

Alteration of histone modifications by nickel compounds: Epigenetic mechanisms.
LDR:02650nam 2200277 a 45 001 941707
005 20110519
008 110519s2007 ||||||||||||||||| ||eng d
035 $a (UMI)AAI3247368
035 $a AAI3247368
040 $a UMI $c UMI
100 1 $a Ke, Qingdong. $3 1265801
245 1 0 $a Alteration of histone modifications by nickel compounds: Epigenetic mechanisms.
300 $a 158 p.
500 $a Adviser: Max Costa.
500 $a Source: Dissertation Abstracts International, Volume: 68-01, Section: B, page: 0254.
502 $a Thesis (Ph.D.)--New York University, 2007.
520 $a Nickel (Ni) compounds are known carcinogens and the carcinogenicity of different forms of Ni compounds varies with their water solubility. Due to their weak mutagenecity, epigenetic mechanisms likely play an important role in Ni carcinogenesis. This project investigated epigenetic effects of Ni compounds in cells. The results demonstrated that both water soluble and insoluble Ni compounds were taken up by cells, resulting in Ni ion accumulation in the cytoplasm and nucleus. When the exposure was ceased, Ni ions persisted in both sites in the insoluble Ni-exposed cells longer than in the soluble Ni-exposed ones. It was found that Ni exposure caused alterations in histone modifications at the global level in cells. Among these were: loss of acetylation of all four core histones, and increases of H3K9 dimethylation. These changes in histone modification were implicated in Ni-induced transgene silencing. In addition, Ni exposure also resulted in an increase in H3S10 phosphorylation and ubiquitination of H2A and H2B. Exploration of the mechanisms by which Ni induced these increases in histone modifications revealed that Ni activated JNK-MAPK pathway which induced H3S10 phosphorylation. In vitro studies of histone ubiquitination and deubiquitination suggested that Ni elevated histone ubiquitination by inhibition the deubiquitinating enzyme activity. These studies have demonstrated strong epigenetic effects of Ni in cells which are important in its toxicity and carcinogenicity. In addition, the results present a likely explanation for the difference in carcinogenicity between water soluble and insoluble Ni compounds in experimental animals, as well as suggesting a possible mechanism for why insoluble Ni compounds are more potent carcinogens than the soluble species.
590 $a School code: 0146.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Engineering, Environmental. $3 783782
650 4 $a Health Sciences, Toxicology. $3 1017752
690 $a 0307
690 $a 0383
690 $a 0775
710 2 $a New York University. $3 515735
773 0 $t Dissertation Abstracts International $g 68-01B.
790 $a 0146
790 1 0 $a Costa, Max, $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3247368