Acetylcholine (ACh)-activated channel properties were examined on an aneural culture of chick embryo myotubes by using patch-clamp techniques. Changes in conductance, open time and closed time were induced by the selective activator of the calcium- and phospholipid-dependent C-kinase (PKc), 12-O-tetradecanoylphorbol-13-acetate (TPA). The action of TPA was mimicked by exogenous phospholipase C and was blocked by the PKc inhibitor, 1-(5-isoquinolinylsulphonyl)-2-methyl-piperazine. In addition to its gating action, ACh was shown to stimulate phosphoinositide turnover and to translocate PKc from the cytosol to the cell membrane. Both these ACh-induced effects were inhibited by curare and not substantially affected by atropine. Bath-applied ACh outside the patch-pipette in the cell-attached patch-clamp mode, had a strong effect on the ACh-activated channels in the patch membrane, in a way that resembled the action of TPA. These findings raise the possibility that ACh regulates its own nicotinic receptors through the C-kinase system.
ACETYLCHOLINE MAY REGULATE ITS OWN NICOTINIC RECEPTOR-CHANNEL THROUGH THE C-KINASE SYSTEM / Eusebi, Fabrizio; Grassi, Francesca; Nervi, Clara; C., Caporale; Adamo, Sergio; B. M., Zani; Molinaro, Mario. - In: PROCEEDINGS OF THE ROYAL SOCIETY OF LONDON. SERIES B, BIOLOGICAL SCIENCES. - ISSN 0080-4649. - STAMPA. - 230:1260(1987), pp. 355-365. [10.1098/rspb.1987.0024]
ACETYLCHOLINE MAY REGULATE ITS OWN NICOTINIC RECEPTOR-CHANNEL THROUGH THE C-KINASE SYSTEM
EUSEBI, Fabrizio;GRASSI, Francesca;NERVI, Clara;ADAMO, Sergio;MOLINARO, Mario
1987
Abstract
Acetylcholine (ACh)-activated channel properties were examined on an aneural culture of chick embryo myotubes by using patch-clamp techniques. Changes in conductance, open time and closed time were induced by the selective activator of the calcium- and phospholipid-dependent C-kinase (PKc), 12-O-tetradecanoylphorbol-13-acetate (TPA). The action of TPA was mimicked by exogenous phospholipase C and was blocked by the PKc inhibitor, 1-(5-isoquinolinylsulphonyl)-2-methyl-piperazine. In addition to its gating action, ACh was shown to stimulate phosphoinositide turnover and to translocate PKc from the cytosol to the cell membrane. Both these ACh-induced effects were inhibited by curare and not substantially affected by atropine. Bath-applied ACh outside the patch-pipette in the cell-attached patch-clamp mode, had a strong effect on the ACh-activated channels in the patch membrane, in a way that resembled the action of TPA. These findings raise the possibility that ACh regulates its own nicotinic receptors through the C-kinase system.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.