Abstract:
:We have examined the regulation of neuronal nitric oxide synthase (NOS) by phosphorylation with cyclic-GMP (PKG) and cyclic-AMP-dependent (PKA) protein kinases. In vitro phosphorylation studies indicate that both PKG and PKA phosphorylate NOS on a single site. Phosphoamino-acid analysis and peptide mapping demonstrate that phosphorylation by either cyclic-nucleotide kinase occurs on a similar serine residue. Phosphorylation of purified NOS by either PKG or PKA diminishes catalytic activity. Stimulation by 8-Br-cGMP of HEK-293 cells stably transfected with the cDNA for neuronal NOS (293.NOS cells) results in phosphorylation of immunoprecipitated NOS. Incubation of 293-NOS cells with 8-bromo-cGMP or dibutyryl-cAMP reduces nitrite release in response to stimulation with calcium ionophore A23187. Phosphorylation-induced decreases in NOS activity may counterbalance and modulate NOS activating signals.
journal_name
Neuropharmacologyjournal_title
Neuropharmacologyauthors
Dinerman JL,Steiner JP,Dawson TM,Dawson V,Snyder SHdoi
10.1016/0028-3908(94)90023-xsubject
Has Abstractpub_date
1994-11-01 00:00:00pages
1245-51issue
11eissn
0028-3908issn
1873-7064journal_volume
33pub_type
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