全球基因素修饰模式预测前列腺癌复发风险
David B Seligson1, Steve Horvath, Tao Shi
1Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, University of California, Los Angeles, California 90095, USA.
Nature
|July 1, 2005
概括
全球基因组修饰,如乙化和甲基化,与癌症有关,并预测患者的结果. 这些广泛的变化揭示了前列腺癌的分子差异,影响了临床行为.
科学领域:
- 表观遗传学 在表观遗传学中,表观遗传学是指表观遗传学.
- 癌症生物学 癌症生物学
- 分子病理学分子病理学
背景情况:
- 在癌症中,翻译后的基因组修饰会发生变化,但通常发生在特定的基因促进器中.
- 影响大染色体区域的全球基因组修饰没有与临床结果有广泛的联系.
- 前列腺癌表现出不同的临床行为,表明潜在的分子异质性.
研究的目的:
- 调查全球基因素修饰水平与前列腺癌的临床结果之间的关联.
- 为了确定全球质子修饰模式是否可以预测瘤复发风险.
- 探索作为前列腺癌分子异质性指标的基因组修饰的潜力.
主要方法:
- 在初级前列腺切除组织样本上进行了免疫组织化学染色.
- 量化了对基因素乙化和二甲基化 (H3和H4) 阳性细胞的百分比.
- 使用统计分析将修改模式与临床数据和复发风险相关联.
主要成果:
- 在前列腺癌组织中发现了全球基因组修饰的明显模式.
- 这些模式与两个不同的疾病亚型有关.
- 在低度前列腺癌患者中,特定的组素修饰模式独立预测瘤复发风险,超出已确定的临床因素.
结论:
- 广泛的变化在特定的组素修饰与前列腺癌有关.
- 全球基因组修饰模式可以作为临床结果的预测生物标志物.
- 这些发现表明前列腺癌的新型分子异质性,可能解释不同的临床轨迹.
相关概念视频
02:32Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:25Spreading of Chromatin Modifications
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer is an enzyme that can...
Writers
The writer is an enzyme that can...
02:30Histone Variants at the Centromere
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
02:32Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...