Functional role of post-translational modifications of Sp1 in tumorigenesis

被引:84
作者
Chang, Wen-Chang [1 ,2 ,3 ,4 ,5 ]
Hung, Jan-Jong [1 ,2 ,3 ,4 ]
机构
[1] Natl Cheng Kung Univ, Coll Med, Inst Basic Med Sci, Tainan 701, Taiwan
[2] Natl Cheng Kung Univ, Coll Med, Dept Pharmacol, Tainan 701, Taiwan
[3] Natl Cheng Kung Univ, Coll Biosci & Biotechnol, Inst Bioinformat & Biosignal Transduct, Tainan 701, Taiwan
[4] Natl Cheng Kung Univ, Ctr Infect Dis & Signal Transduct Res, Tainan 701, Taiwan
[5] Taipei Med Univ, Coll Med, Grad Inst Med Sci, Taipei, Taiwan
关键词
HISTONE DEACETYLASE INHIBITOR; BREAST-CANCER CELLS; TRANSCRIPTION FACTOR SP1; ESTROGEN-RECEPTOR-ALPHA; O-GLYCOSYLATION; GENE-TRANSCRIPTION; PANCREATIC-CANCER; CYCLE ARREST; DNA-BINDING; PHOSPHORYLATION;
D O I
10.1186/1423-0127-19-94
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Specific protein 1 (Sp1), the first transcription factor to be isolated, regulates the expression of numerous genes involved in cell proliferation, apoptosis, and differentiation. Recent studies found that an increase in Sp1 transcriptional activity is associated with the tumorigenesis. Moreover, post-translational modifications of Sp1, including glycosylation, phosphorylation, acetylation, sumoylation, ubiquitination, and methylation, regulate Sp1 transcriptional activity and modulate target gene expression by affecting its DNA binding activity, transactivation activity, or protein level. In addition, recent studies have investigated several compounds with anti-cancer activity that could inhibit Sp1 transcriptional activity. In this review, we describe the effect of various post-translational modifications on Sp1 transcriptional activity and discuss compounds that inhibit the activity of Sp1.
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页数:7
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共 73 条
[1]   Tolfenamic acid and pancreatic cancer growth, angiogenesis, and Sp protein degradation [J].
Abdelrahim, Maen ;
Baker, Cheryl H. ;
Abbruzzese, James L. ;
Safe, Stephen .
JOURNAL OF THE NATIONAL CANCER INSTITUTE, 2006, 98 (12) :855-868
[2]   Casein kinase II-mediated phosphorylation of the C terminus of spl decreases its DNA binding activity [J].
Armstrong, SA ;
Barry, DA ;
Leggett, RW ;
Mueller, CR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (21) :13489-13495
[3]   Principles of ubiquitin and SUMO modifications in DNA repair [J].
Bergink, Steven ;
Jentsch, Stefan .
NATURE, 2009, 458 (7237) :461-467
[4]  
Bevilacqua A, 2000, DEVELOPMENT, V127, P1541
[5]   Induction of cPLA2 in lung epithelial cells and non-small cell lung cancer is mediated by Sp1 and c-jun [J].
Blaine, SA ;
Wick, M ;
Dessev, C ;
Nemenoff, RA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (46) :42737-42743
[6]   MITHRAMYCIN INHIBITS SP1 BINDING AND SELECTIVELY INHIBITS TRANSCRIPTIONAL ACTIVITY OF THE DIHYDROFOLATE-REDUCTASE GENE INVITRO AND INVIVO [J].
BLUME, SW ;
SNYDER, RC ;
RAY, R ;
THOMAS, S ;
KOLLER, CA ;
MILLER, DM .
JOURNAL OF CLINICAL INVESTIGATION, 1991, 88 (05) :1613-1621
[7]   Fibroblast growth factor-2 represses platelet-derived growth factor receptor-α (PDGFR-α) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-α promoter [J].
Bonello, MR ;
Khachigian, LM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (04) :2377-2382
[8]   Glutamine stimulates argininosuccinate synthetase gene expression through cytosolic O-glycosylation of Sp1 in Caco-2 cells [J].
Brasse-Lagnel, C ;
Fairand, A ;
Lavoinne, A ;
Husson, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (52) :52504-52510
[9]   Curcumin decreases specificity protein expression in bladder cancer cells [J].
Chadalapaka, Gayathri ;
Jutooru, Indira ;
Chintharlapani, Sudhakar ;
Papineni, Sabitha ;
Smith, Roger, III ;
Li, Xiangrong ;
Safe, Stephen .
CANCER RESEARCH, 2008, 68 (13) :5345-5354
[10]   Betulinic acid inhibits prostate cancer growth through inhibition of specificity protein transcription factors [J].
Chintharlapalli, Sudhakar ;
Papineni, Sabitha ;
Ramaiah, Shashi K. ;
Safe, Stephen .
CANCER RESEARCH, 2007, 67 (06) :2816-2823