Transcriptional activation of the human prostatic acid phosphatase gene by NF- B via a novel hexanucleotide-binding site

摘要: Human prostatic acid phosphatase (PAcP) is a prostate epithelium-specific differentiation antigen. Cellular PAcP functions as neutral protein tyrosine and involved in regulating androgen-promoted cancer cell proliferation. Despite the fact that promoter of gene has been cloned, transcriptional factors regulate expression remain unidentified. This article describes our analyses gene. Deletion sequence up to −4893 (−4893/+87) revealed 577 bp fragment (−1356/−779) represents unique positive cis-active element human cells but not HeLa cervix carcinoma cells. Interestingly, contains non-consensus nuclear factor κB (NF-κB)-binding site required for NF-κB up-regulation cells, while failed have same effect Conversely, inhibition pathway stopped p65 activation p1356 activity. Gel shift mutation determined AGGTGT (−1254/−1249) core NF-κB-binding activation. Biologically, tumor necrosis factor-α (TNF-α) activated endogenous LNCaP The data collectively indicate up-regulates activity via its binding motif, novel located inside enhancer