N. Tsuboyama-kasaoka et al., Human cysteine dioxygenase gene: Structural organization, tissue-specific expression and downregulation by phorbol 12-myristate 13-acetate, BIOS BIOT B, 63(6), 1999, pp. 1017-1024
The organization of the human cysteine dioxygenase (CDO) gene was found to
be similar to its rat counterpart, and the location of the introns in the p
rotein structure was identical to the rat CDO gene. The major transcription
start site, identified by primer extension, was located 260 bp upstream fr
om the ATG codon. The sequence of the 5'-immediate upstream region was high
ly conserved between the human and rat CDO genes. The putative promoter reg
ion contained a TATA-box-like sequence, and many putative cis-acting elemen
ts including HNF5, GRE, TRE, CRE, CArG box, ARE, MBS, and NF-kB. A Northern
blot analysis revealed that CDO mRNA was strongly expressed in the liver a
nd placenta, and weakly in the heart, brain and pancreas. CDO mRNA was also
detected in human hepatoblastoma HepG2 cells. The CDO mRNA level in HepG2
cells was decreased after 2 h and reached a minimum 6 h-8 h after a phorbol
12-myristate 13-acetate (PMA) treatment, and then gradually returned to th
e basal level.