Vasoactive intestinal peptide is a neuroprotective factor that has a stimulatory effect on the growth of some tumor cells and an inhibitory effect on others. This gene encodes a protein that is upregulated by vasoactive intestinal peptide and may be involved in its stimulatory effect on certain tumor cells. The encoded protein contains one homeobox and nine zinc finger domains, suggesting that it functions as a transcription factor. This gene is also upregulated in normal proliferative tissues. Finally, the encoded protein may increase the viability of certain cell types through modulation of p53 activity. Alternatively spliced transcript variants encoding the same protein have been described.
Human thiol dioxygenases include cysteine dioxygenase (CDO, MIM 603943) and cysteamine (2-aminoethanethiol) dioxygenase (ADO, EC 1.13.11.19). CDO adds 2 oxygen atoms to free cysteine, whereas ADO adds 2 oxygen atoms to free cysteamine to form hypotaurine. Mouse Ado has strong and specific dioxygenase activity in vitro towards cysteamine but not cysteine. Recombinant Ado was shown to bind iron. Overexpression of Ado in HepG2/C3A cells increased the production of hypotaurine from cysteamine. Similar results were found with human ADO. When endogenous expression of ADO was reduced by RNA-mediated interference, hypotaurine production decreased. The demonstration of high levels of ADO in brain challenges the previous assumption that most of the taurine in the brain is a consequence of CDO activity.
A synthesized peptide derived from human ADORA1, corresponding to a region within C-terminal amino acids.
A synthesized peptide derived from human ADORA2A, corresponding to a region within the internal amino acids.
A synthetic peptide from human ADORA2A
A synthesized peptide derived from human ADORA2B, corresponding to a region within the internal amino acids.
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