Premium
Histone Deacetylase Inhibitor Activates the p21/WAF1/Cip1 Gene Promoter through the Sp1 Sites
Author(s) -
SOWA Y.,
ORITA T.,
HIRANABEMINAMIKAWA S.,
NAKANO K.,
MIZUNO T.,
NOMURA H.,
SAKAI T.
Publication year - 1999
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1999.tb09415.x
Subject(s) - trichostatin a , hdac11 , acetylation , histone deacetylase , histone deacetylase inhibitor , histone deacetylase 5 , microbiology and biotechnology , hdac4 , sap30 , histone deacetylase 2 , histone , chemistry , histone h2a , hdac10 , cancer research , biology , gene , genetics
Trichostatin A (TSA), a specific histone deacetylase inhibitor, induces histone hyperacetylation and modulates the expression of some genes. We examined the effects of TSA on MG63 cells. TSA induced growth arrest and expression of the p21/WAF1/Cip1 protein. A close correlation between the level of histone acetylation and induction of the p21/WAF1/Cip1 protein was detected. Using several mutant p21/WAF1/Cip1 promoter fragments, mutation of either of two Sp1 sites at -82 or -69 of the p21/WAF1/Cip1 promoter reduced the responsiveness to TSA. This finding indicates that TSA activates the p21/WAF1/Cip1 promoter through the Sp1 sites in a p53-independent manner.