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Titolo:
Protein kinase A activity may kinetically upregulate the striatal transporter for dopamine
Autore:
Batchelor, M; Schenk, JO;
Indirizzi:
Washington State Univ, Dept Chem, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 pt Chem, Pullman, WA 99164 USA Washington State Univ, Dept Biochem & Biophys, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 Biophys, Pullman, WA 99164 USA Washington State Univ, Program Pharmacol Toxicol, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 Toxicol, Pullman, WA 99164 USA Washington State Univ, Program Neurosci, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 eurosci, Pullman, WA 99164 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 24, volume: 18, anno: 1998,
pagine: 10304 - 10309
SICI:
0270-6474(199812)18:24<10304:PKAAMK>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
REPEATED COCAINE; H-3 DOPAMINE; IN-VITRO; PHOSPHORYLATION; RECEPTORS; RAT; SYNAPTOSOMES; WITHDRAWAL; MODULATE; RELEASE;
Keywords:
dopamine transporter; protein kinase A; rotating disk electrode voltammetry; striatum; 8-Br-cAMP; forskolin; quinpirole; sulpiride; H-89; H-7; H-9;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Schenk, JO Washington State Univ, Dept Chem, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 llman, WA 99164 USA
Citazione:
M. Batchelor e J.O. Schenk, "Protein kinase A activity may kinetically upregulate the striatal transporter for dopamine", J NEUROSC, 18(24), 1998, pp. 10304-10309

Abstract

The neuronal dopamine transporter (DAT) plays a key role in terminating dopaminergic chemical neurotransmission; thus, the study of the regulation ofDAT activity is important in defining parameters relevant to the control of dopaminergic neurotransmission. Interpretation of the results from previous work of this laboratory suggests that occupation of presynaptic autoreceptors increases DAT activity. Second messenger signaling related to kineticupregulation of DAT has not been examined previously. However, others haveshown that protein kinase C activity may downregulate DAT activity, whereas protein kinase A has shown variable results. Herein it is shown that protein kinase A activity mediates the kinetic upregulation of DAT. Quinpirole increased DAT activity that was blocked by sulpiride and the protein kinaseA selective inhibitor H-89. Brief incubations with forskolin and 8-bromo-cAMP (8-Br-cAMP) were found to stimulate striatal DAT activity by increasingthe V-max of transport without affecting the K-m. Exposures >15 min had noeffect. The 8-Br-cAMP-stimulated increases in DAT activity were blocked bypre-exposure to H-89. Thus, second messenger signaling via the cAMP cascade may mediate kinetic upregulation of DAT. Kinetic analyses of the results suggest that either insertion of DAT into the membrane or activation of pre-existing DAT within the membrane mediates the regulation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 07:32:09