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Titolo:
BRADYKININ INHIBITS CYCLIC-AMP ACCUMULATION IN D384-HUMAN ASTROCYTOMA-CELLS VIA A CALCIUM-DEPENDENT INHIBITION OF ADENYLYL CYCLASE
Autore:
ALTIOK N; FREDHOLM BB;
Indirizzi:
KAROLINSKA INST,DEPT PHARMACOL,BOX 60400 S-10401 STOCKHOLM 60 SWEDEN KAROLINSKA INST,DEPT PHARMACOL,BOX 60400 S-10401 STOCKHOLM 60 SWEDEN
Titolo Testata:
Cellular signalling
fascicolo: 3, volume: 5, anno: 1993,
pagine: 279 - 288
SICI:
0898-6568(1993)5:3<279:BICAID>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUSCARINIC CHOLINERGIC RECEPTORS; CALMODULIN PLAYS; CEREBRAL-CORTEX; CA-2+; RAT; PHOSPHODIESTERASE; IDENTIFICATION; GENERATION; MEMBRANES; PROTEIN;
Keywords:
CALCIUM ENTRY; CALMODULIN; CALCIUM STORES; PHOSPHODIESTERASE; ASTROCYTE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
N. Altiok e B.B. Fredholm, "BRADYKININ INHIBITS CYCLIC-AMP ACCUMULATION IN D384-HUMAN ASTROCYTOMA-CELLS VIA A CALCIUM-DEPENDENT INHIBITION OF ADENYLYL CYCLASE", Cellular signalling, 5(3), 1993, pp. 279-288

Abstract

Bradykinin causes a concentration-dependent, transient rise in intracellular Ca2+ and a sustained inhibition of forskolin-, dopamine- and 5'-N-ethyl-carboxamidoadenosine (NECA)-stimulated cAMP accumulation in D384 astrocytoma cells. Chelation of intracellular calcium abolished bradykinin's inhibitory effect on cAMP accumulation. Chelating extracellular Ca2+ did not block the initial, but eliminated the sustained inhibition of cAMP accumulation. Increasing Ca2+ influx by calcium ionophore A23187 caused a concentration-dependent inhibition of stimulated cAMP accumulation. A hydroquinone derivative 2,5-di(tert-butyl)-1,4-benzohydroquinone tBuBHQ), which inhibits microsomal C2+ sequestration, did not mimic the effect of bradykinin, although it increased [Ca2+]i even more than A23187 did. The inhibitory effect of bradykinin was not mediated by Ca2+/CaM-dependent stimulation of phosphodiesterase (PDE). Forskolin-stimulated adenylyl cyclase activity was inhibited by Ca2+ (10(-7) to 10(-3) M), both in ethyleneglycol-bis-(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) washed and native D384 plasma membranes. This effect was not altered by calmodulin (CaM) or CaM-antagonists. Bradykinin treatment, which attenuates cAMP accumulation in intact cells, did not do so in plasma membranes. These findings suggest that bradykinin-induced inhibition of cAMP formation in D384 cells requires mobilization of [Ca2+]i and subsequent entry of Ca2+ which directly interacts with a component of the adenylyl cyclase system.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 06:45:41