期刊文献+

SIRT家族在结直肠癌中的研究进展

Research progress of SIRT family in colorectal cancer
原文传递
导出
摘要 SIRT(Sirtuins)是一类高度保守的烟酰胺腺嘌呤二核苷酸(NAD+)依赖的Ⅲ类去乙酰化酶,包括SIRT1-7共7名家族成员,主要通过调节代谢、介导自噬和维持遗传稳定性在正常细胞内稳态中发挥重要作用。在结直肠癌的发生发展中,SIRT能够通过去乙酰化组蛋白和非组蛋白来调控基因的表达,调节细胞的代谢、增殖以及凋亡等过程,进而影响肿瘤细胞的增殖、迁移和侵袭,在CRC中发挥促癌或抑癌的作用。本文综述了SIRT家族在CRC发生发展过程中的生物学作用,旨在更好地了解其作用机制,为CRC的治疗提供新的探索途径。 Sirtuins(SIRT) is a highly conserved nicotinamide adenine dinucleotide(NAD+) dependent class Ⅲ deacetylase, including seven family members, SIRT1-7. SIRT plays an important role in normal cell homeostasis by regulating metabolism, mediating autophagy and maintaining genetic stability. In the occurrence and development of colorectal cancer, SIRT can regulate cell metabolism, proliferation and apoptosis and other processes by regulating gene expression by deacetylating histones and non-histone proteins, thereby affecting the proliferation, migration and invasion of tumor cells, playing a tumor-promoting or tumor-suppressing role in CRC. This paper reviews the biological function of SIRT family in the development of colorectal cancer in order to better understand its mechanism of action and provide a new exploration way for the treatment of colorectal cancer.
作者 李博 王佳南 崔巍 LI Bo;WANG Jia'nan;CUI Wei(The Affiliated Lihuili Hospital,Ningbo University,Ningbo 315040,China)
出处 《生命的化学》 CAS 2022年第6期1138-1144,共7页 Chemistry of Life
基金 浙江省医药卫生科技计划项目(2020KY275)。
关键词 结直肠癌 SIRT家族 组蛋白去乙酰化酶 colorectal cancer SIRT family histone deacetylase
  • 相关文献

参考文献1

二级参考文献10

  • 1lmai S. Armstrong CM, Kaeherlein M, Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature, 2000, 403:795-800.
  • 2Haigis MC. Sinclair DA. Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol. 2010, 5:253-295.
  • 3Nakagawa T, Lomb D J, Haigis MC, Guarente L. SIRT5 Deacetylales carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell. 2009, 137:560-570.
  • 4Du J, Zhou Y, Su X. Yu JJ. Khan S, Jiang It. Kim J, Woo J. Kim JH, Choi BH, He B. Chen W. Zhang S. Cerione RA. Auwerx J. Hao Q, Lin H. Sifts is a NAD-dependent protein lysine demalonylase and desuccinylase. Science. 2011,334:806-809.
  • 5Tan M, Peng C. Anderson KA. Chhoy P. Xie Z. Dai L. Park J. Chert Y. Huang H, Zhang Y, Ro J, Wagner GR, Green MF. Madsen AS. Schmiesing J, Peterson BS, Xu G, Ilkayeva OR. Muehlbauer MJ. Braulke T. Muhlhausen C. Backus DS, Olsen CA. McGuire PJ. Pletcher SD, Lombard DB, Hirschey MD, Zhao Y. Lysine glutaryla- tion is it protein posttranslational modification regulated by SIRT5. Cell Metab. 2014, 19:605-617.
  • 6Ogura M, Nakamura Y. Tanaka D, Zhuang X. Fujita Y. Obara A, Hamasaki A, Hosokawa M, Inagaki N. Overexpression of SIRT5 confirms its involvement in deacetylation and activation of car- bamoyl phosphate synthetase 1. Biochem Biophys Res Commun, 2010, 393:73-78.
  • 7Peng C, Lu Z, Xie Z, Cheng Z. Chen Y, Tan M, Luo H. Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L. Lombard D. He TC, Dai J, Verdin E, Ye Y, Zhao Y, The first identification of lysine malonyl- ation substrates and its regulatory enzyme. Mol Cell Proteomics, 2011, 10: MI 11.012658.
  • 8Park J, Chen Y, Tishkoff DX, Peng C, Tan M. Dai L. Xie Z. Zhang Y, Zwaans BM, Skinner ME. Lombard DB, Zhao Y. SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol Cell, 21113, 50:919-930.
  • 9Rardin MJ, He W, Nishida Y, Newman JC, Carrico C, Danielson SR, Guo A, Gut P. Sahu AK, Li B. Uppala R, Fitch M, Riiff T. Zhu L. Zhou J. Mulhern D, Stevens RD, Ilkayeva OR, Newgard CB, Jacob- son MP, Hellerstein M. Goetzman ES, Gibson BW. Verdin E. SIRT5 regulates the mitochondrial lysine succinylome and metabolic net- works. Cell Metab, 2013, 18:9211-933.
  • 10Lombard DB, Ah FW. Cheng HL, Bunkenborg J, Streeper RS, Mos- toslavsky R, Kim J, Yancopoulos G. Valenzuela D, Murphy A. Yang Y, Chen Y. Hirschey MD. Bronson RT, Haigis M. Guarente LP, Farese RV Jr, Weissman S, Verdin E, Schwer B. Marnmalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol Cell Biol, 2007.27:8807-8814.

共引文献4

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部