HDAC8
HDAC8
히스톤 디아세틸라제 8은 인간에게 HDAC8 유전자에 의해 암호화된 효소다.[5][6][7]
함수
히스톤은 전사적 조절, 세포 주기 진행, 발달 사건에 중요한 역할을 한다.히스톤 아세틸화/탈 아세틸화는 염색체 구조를 변화시키고 DNA에 대한 전사 인자 접근에 영향을 미친다.이 유전자에 의해 인코딩된 단백질은 히스톤 디아세틸라제/아큐크/아푸카 계열의 1등급에 속한다.히스톤 디아세틸라제 활성이 있으며 프로모터에 연결되면 전사를 억제한다.[7]
히스톤 디아세틸라제 8은 ERR-알파/PGC1-알파 전사 복합체의 두개골 형태생성과[8] 대사 조절에 관여한다.[9]
임상적 유의성
HDAC8은 급성 골수성 백혈병과 특히 질환의 수와 연관되어 있으며, 원활한 근육 세포에서 액틴 시토스켈레톤과 관련이 있다. HDAC8을 대상으로 한 siRNA는 항암효과를 보였다.[10]HDAC8 유도 사멸의 억제는 T세포 림프에서 관찰되었다.[11]또한 HDAC8 효소는 신경블라스토마의 병원체 생성에 관여했다.[12]따라서 HDAC8 선택적 억제제 개발에 관심이 있었다.[13][14]이 유전자에서 적어도 20개의 질병을 유발하는 돌연변이가 발견되었다.[15]
상호작용
참고 항목
참조
- ^ a b c GRCh38: 앙상블 릴리스 89: ENSG00000147099 - 앙상블, 2017년 5월
- ^ a b c GRCm38: 앙상블 릴리스 89: ENSMUSG000067567 - 앙상블, 2017년 5월
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- ^ Patil V, Sodji QH, Kornacki JR, Mrksich M, Oyelere AK (May 2013). "3-Hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition". Journal of Medicinal Chemistry. 56 (9): 3492–506. doi:10.1021/jm301769u. PMC 3657749. PMID 23547652.
- ^ Suzuki T, Ota Y, Ri M, Bando M, Gotoh A, Itoh Y, Tsumoto H, Tatum PR, Mizukami T, Nakagawa H, Iida S, Ueda R, Shirahige K, Miyata N (November 2012). "Rapid discovery of highly potent and selective inhibitors of histone deacetylase 8 using click chemistry to generate candidate libraries". Journal of Medicinal Chemistry. 55 (22): 9562–75. doi:10.1021/jm300837y. PMID 23116147.
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추가 읽기
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- Glénisson W, Waltregny D, Tran SL, North BJ, Verdin E, Colige A, Castronovo V (June 2005). "Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility". FASEB J. 19 (8): 966–8. doi:10.1096/fj.04-2303fje. PMID 15772115. S2CID 12006005.
- Wedel T, Van Eys GJ, Waltregny D, Glénisson W, Castronovo V, Vanderwinden JM (2006). "Novel smooth muscle markers reveal abnormalities of the intestinal musculature in severe colorectal motility disorders". Neurogastroenterol. Motil. 18 (7): 526–38. doi:10.1111/j.1365-2982.2006.00781.x. PMID 16771768. S2CID 58462.
- Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators". Trends Genet. 19 (5): 286–93. CiteSeerX 10.1.1.464.415. doi:10.1016/S0168-9525(03)00073-8. PMID 12711221.
- Hu E, Chen Z, Fredrickson T, et al. (2000). "Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor". J. Biol. Chem. 275 (20): 15254–64. doi:10.1074/jbc.M908988199. PMID 10748112.
- Buggy JJ, Sideris ML, Mak P, et al. (2001). "Cloning and characterization of a novel human histone deacetylase, HDAC8". Biochem. J. 350 (1): 199–205. doi:10.1042/0264-6021:3500199. PMC 1221242. PMID 10926844.
- Amann JM, Nip J, Strom DK, et al. (2001). "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain". Mol. Cell. Biol. 21 (19): 6470–83. doi:10.1128/MCB.21.19.6470-6483.2001. PMC 99794. PMID 11533236.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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- Rodriguez M, Yu X, Chen J, Songyang Z (2004). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. doi:10.1074/jbc.C300407200. PMID 14578343.
- Johnson JM, Castle J, Garrett-Engele P, et al. (2004). "Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays". Science. 302 (5653): 2141–4. CiteSeerX 10.1.1.1017.9438. doi:10.1126/science.1090100. PMID 14684825. S2CID 10007258.
- Lee H, Rezai-Zadeh N, Seto E (2004). "Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A". Mol. Cell. Biol. 24 (2): 765–73. doi:10.1128/MCB.24.2.765-773.2004. PMC 343812. PMID 14701748.
- Vannini A, Volpari C, Filocamo G, et al. (2004). "Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor". Proc. Natl. Acad. Sci. U.S.A. 101 (42): 15064–9. Bibcode:2004PNAS..10115064V. doi:10.1073/pnas.0404603101. PMC 524051. PMID 15477595.
- Waltregny D, North B, Van Mellaert F, et al. (2005). "Screening of histone deacetylases (HDAC) expression in human prostate cancer reveals distinct class I HDAC profiles between epithelial and stromal cells". European Journal of Histochemistry. 48 (3): 273–90. PMID 15590418.
- Waltregny D, Glénisson W, Tran SL, et al. (2006). "Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility". FASEB J. 19 (8): 966–8. doi:10.1096/fj.04-2303fje. PMID 15772115. S2CID 12006005.
- Gantt SL, Gattis SG, Fierke CA (2006). "Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion". Biochemistry. 45 (19): 6170–8. doi:10.1021/bi060212u. PMID 16681389.
- Lee H, Sengupta N, Villagra A, et al. (2006). "Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation". Mol. Cell. Biol. 26 (14): 5259–69. doi:10.1128/MCB.01971-05. PMC 1592721. PMID 16809764.
- Vannini A, Volpari C, Gallinari P, et al. (2007). "Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex". EMBO Reports. 8 (9): 879–84. doi:10.1038/sj.embor.7401047. PMC 1973954. PMID 17721440.
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외부 링크
- HDAC8+단백질,+인간 미국 국립 의학 라이브러리(MesH) 제목
이 기사는 공공영역에 있는 미국 국립 의학 도서관의 텍스트를 통합하고 있다.
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