The potential role of O-GlcNAc modification in cancer epigenetics.
The potential role of O-GlcNAc modification in cancer epigenetics.
复制标题
DOI:
10.2478/s11658-014-0204-6
复制
发表时间:
2014-09
影响因子:
8.3
通讯作者:
Krześlak A
中科院分区:
文献类型:
--
作者:
Forma E;Jóźwiak P;Bryś M;Krześlak A
There is no doubt that cancer is not only a genetic disease but that it can also occur due to epigenetic abnormalities. Diet and environmental factors can alter the scope of epigenetic regulation. The results of recent studies suggest that O-GlcNAcylation, which involves the addition of N-acetylglucosamine on the serine or threonine residues of proteins, may play a key role in the regulation of the epigenome in response to the metabolic status of the cell. Two enzymes are responsible for cyclic O-GlcNAcylation: O-GlcNAc transferase (OGT), which catalyzes the addition of the GlcNAc moiety to target proteins; and O-GlcNAcase (OGA), which removes the sugar moiety from proteins. Aberrant expression of O-GlcNAc cycling enzymes, especially OGT, has been found in all studied human cancers. OGT can link the cellular metabolic state and the epigenetic status of cancer cells by interacting with and modifying many epigenetic factors, such as HCF-1, TET, mSin3A, HDAC, and BAP1. A growing body of evidence from animal model systems also suggests an important role for OGT in polycomb-dependent repression of genes activity. Moreover, O-GlcNAcylation may be a part of the histone code: O-GlcNAc residues are found on all core histones.
登录
查看更多内容
影响因子:
11.2
作者:
Chernikova SB;Razorenova OV;Higgins JP;Sishc BJ;Nicolau M;Dorth JA;Chernikova DA;Kwok S;Brooks JD;Bailey SM;Game JC;Brown JM
通讯作者:
Brown JM
DOI:
10.1073/pnas.1013822108
发表时间:
2011-02-15
影响因子:
11.1
作者:
Daou, Salima;Mashtalir, Nazar;Affar, El Bachir
通讯作者:
Affar, El Bachir
DOI:
10.1016/j.bbrc.2010.11.138
发表时间:
2011-01-07
影响因子:
3.1
作者:
Gao, Zhen;Xu, C. Wilson
通讯作者:
Xu, C. Wilson
影响因子:
37.3
作者:
Ducasse M;Brown MA
通讯作者:
Brown MA
影响因子:
3.4
作者:
Champattanachai, Voraratt;Netsirisawan, Pukkavadee;Svasti, Jisnuson
通讯作者:
Svasti, Jisnuson