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Titolo:
Ca2+-permeable AMPA receptors induce phosphorylation of cAMP response element-binding protein through a phosphatidylinositol 3-kinase-dependent stimulation of the mitogen-activated protein kinase signaling cascade in neurons
Autore:
Perkinton, MS; Sihra, TS; Williams, RJ;
Indirizzi:
Guys Hosp, GKT Sch Biomed Sci, Div Biomed Sci, Biochem Neuropharmacol Grp,Neurosci Res Ctr, London SE1 9RT, England Guys Hosp London England SE1 9RT urosci Res Ctr, London SE1 9RT, England Univ Coll London, Dept Pharmacol, London WC1E 6BT, England Univ Coll London London England WC1E 6BT macol, London WC1E 6BT, England
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 14, volume: 19, anno: 1999,
pagine: 5861 - 5874
SICI:
0270-6474(19990715)19:14<5861:CARIPO>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
LONG-TERM POTENTIATION; CENTRAL-NERVOUS-SYSTEM; BETA-GAMMA-SUBUNITS; CULTURED HIPPOCAMPAL-NEURONS; METHYL-D-ASPARTATE; MAP KINASE; GLUTAMATE-RECEPTORS; ARACHIDONIC-ACID; STRIATAL NEURONS; GENE-EXPRESSION;
Keywords:
AMPA; mitogen-activated protein kinase; phosphatidylinositol 3-kinase; CREB; wortmannin; LY 294002; pertussis toxin; G-protein; PP2; cyclothiazide; glutamate; kainate; calcium/calmodulin-dependent kinase II; tyrosine kinase; AMPA toxicity; arachidonic acid; striatum; striatal neurons;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
82
Recensione:
Indirizzi per estratti:
Indirizzo: Williams, RJ Guys Hosp, GKT Sch Biomed Sci, Div Biomed Sci, Biochem Neuropharmacol Grp,Neurosci Res Ctr, Hodgkin Bldg, London SE1 9RT, England Guys Hosp Hodgkin Bldg London England SE1 9RT 1 9RT, England
Citazione:
M.S. Perkinton et al., "Ca2+-permeable AMPA receptors induce phosphorylation of cAMP response element-binding protein through a phosphatidylinositol 3-kinase-dependent stimulation of the mitogen-activated protein kinase signaling cascade in neurons", J NEUROSC, 19(14), 1999, pp. 5861-5874

Abstract

Ca2+-permeable AMPA receptors may play a key role during developmental neuroplasticity, learning and memory, and neuronal loss in a number of neuropathologies. However, the intracellular signaling pathways used by AMPA receptors during such processes are not fully understood. The mitogen-activated protein kinase (MAPK) cascade is an attractive target because it has been shown to be involved in gene expression, synaptic plasticity, and neuronal stress. Using primary cultures of mouse striatal neurons and a phosphospecific MAPK antibody we addressed whether AMPA receptors can activate the MAPK cascade. We found that in the presence of cyclothiazide, AMPA caused a robust and direct (no involvement of NMDA receptors or L-type voltage-sensitiveCa2+ channels) Ca2+ dependent activation of MAPK through MAPK kinase (MEK). This activation was blocked by GYKI 53655, a noncompetitive selective antagonist of AMPA receptors. Probing the mechanism of this activation revealed an essential role for phosphatidylinositol 3-kinase (PI 3-kinase) and theinvolvement of a pertussis toxin (PTX)-sensitive G-protein, a Src family protein tyrosine kinase, and Ca2+/calmodulin-dependent kinase II. Similarly,kainate activated MAPK in a PI 3-kinase-dependent manner. AMPA receptor-evoked neuronal death and arachidonic acid mobilization did not appear to involve signaling through the MAPK pathway. However, AMPA receptor stimulationled to a Ca2+-dependent phosphorylation of the nuclear transcription factor CREB, which could be prevented by inhibitors of MEK or PI 3-kinase. Our results indicate that Ca2+-permeable AMPA receptors transduce signals from the cell surface to the nucleus of neurons through a PI 3-kinase-dependent activation of MAPK. This novel pathway may play a pivotal role in regulatingsynaptic plasticity in the striatum.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:23:56