title: Induction of murine H-rev107 gene expression by growth arrest and histone acetylation: involvement of an Sp1/Sp3-binding GC-box.
abstract: H-rev107 is downregulated in many carcinomas and tumor cell lines. Using postconfluent NIH3T3 cells, we demonstrated that growth arrest caused by contact inhibition, but not serum deprivation, increased H-rev107 expression. Furthermore, histone deacetylase inhibitors induced H-rev107 expression in NIH3T3 cells and allowed its reexpression in H-rev107-deficient WEHI 7.1 lymphoma cells. In contrast, no effect of the postconfluent stage or histone deacetylase inhibitors on H-rev107 levels was observed in tumorigenic H-rev107-expressing cell lines, HepG2, HeLa, and SKBR3. Transfections showed that TSA treatment increased luciferase activity 20-fold in NIH3T3 cells. We found that the GC-box at -83/-75 is a key element for H-rev107 induction by TSA and growth arrest, although there were no changes in the pattern and intensity of Sp1/Sp3-binding after induction. These data suggest that contact inhibition of growth and growth arrest caused by histone deacetylase inhibitors probably use the same mechanism to stimulate H-rev107 expression via histone acetylation in NIH3T3 cells and this might contribute to the development of drugs that can induce H-rev107 expression in certain tumors.
authors.affiliation: Department of Nutritional Sciences and Toxicology, University of California, Berkeley, CA 94720, USA.
authors.forename: Karim
authors.initials: K
authors.lastname: Roder
authors.forename: Kee-Hong
authors.initials: KH
authors.lastname: Kim
authors.forename: Hei Sook
authors.initials: HS
authors.lastname: Sul
mesh_terms: D016475:3T3 Cells; D000107:Acetylation; D000818:Animals; D002452:Cell Count; D003260:Contact Inhibition; D004268:DNA-Binding Proteins / Q000378:metabolism*; D015536:Down-Regulation; D005786:Gene Expression Regulation; D006367:HeLa Cells; D056572:Histone Deacetylase Inhibitors; D006657:Histones / Q000378:metabolism*; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D051379:Mice; D010544:Peroxidases / Q000494:pharmacology; D054464:Peroxiredoxins; D054512:Phospholipases A2, Calcium-Independent; D011401:Promoter Regions, Genetic; D014176:Protein Biosynthesis; D011506:Proteins / Q000235:genetics*; D012333:RNA, Messenger / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016329:Sp1 Transcription Factor / Q000378:metabolism*; D051705:Sp3 Transcription Factor; D014157:Transcription Factors / Q000378:metabolism*; D015533:Transcriptional Activation; D014407:Tumor Cells, Cultured; D025521:Tumor Suppressor Proteins
chemical_list: D004268:DNA-Binding Proteins; D056572:Histone Deacetylase Inhibitors; D006657:Histones; D047908:Intracellular Signaling Peptides and Proteins; D011506:Proteins; D012333:RNA, Messenger; C497121:SP3 protein, human; D016329:Sp1 Transcription Factor; C497122:Sp3 protein, mouse; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins; D051705:Sp3 Transcription Factor; D010544:Peroxidases; D054464:Peroxiredoxins; C490065:PLAAT3 protein, human; D054512:Phospholipases A2, Calcium-Independent; C490066:Plaat3 protein, mouse