Abstract：
:Pituitary adenylate cyclase-activating polypeptide (PACAP-27) was incubated in a tyrosine hydroxylase (TyrOH) assay with a homogenate preparation of the nucleus accumbens of the rat. TyrOH activity was determined in vitro by measuring the production of L-dopa with HPLC-ECD. Only in the presence of adenosine nucleotides (ATP, App(NH)p) PACAP-27 increased TyrOH activity with a EC(50)of 100 nM. Since the PACAP-27 effect on TyrOH was abolished when homogenate or pellet of the nucleus accumbens were coincubated with CHAPS, the peptide effect appears to be receptor mediated. TyrOH activation produced by PACAP-27 increased in the presence of the phosphodiesterase inhibitor papaverine indicating the involvement of cAMP. The marked effect of the non-hydrolysable adenosine nucleotide App(NH)p also supports a cAMP-dependent TyrOH activation not related to ADP or an ADP-dependent mechanism. This report's data suggest that PACAP-27 activates TyrOH in the rat nucleus accumbens through receptor-mediated cAMP formation. The exact receptor type present in the nucleus accumbens has yet not been specified.
journal_name
Neuropeptidesjournal_title
Neuropeptidesauthors
Moser A,Scholz J,Gänsle Adoi
10.1054/npep.1999.0768keywords:
subject
Has Abstractpub_date
1999-12-01 00:00:00pages
492-7issue
6eissn
0143-4179issn
1532-2785pii
S0143-4179(99)90768-0journal_volume
33pub_type
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