Control of K+ channels by G proteins

Brown, Arthur M.; Yatani, Atsuko; Kirsch, Glenn E.; Okabe, Kouji; VanDongen, Antonius M.J.; Birnbaumer, Lutz

doi:10.1007/bf00785808

Cited by 6 publications

(4 citation statements)

References 58 publications

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“…While it appears that G. is involved with a neuronal voltage-dependent Ca2+ channel (6,8,9,22,23) and that both Go and Gi are involved with K+ channels (75) there are also reports that G. and Gi are involved with Ca2+ channels in neuronal ganglion cells (13), adrenal cortex cells (76), and pituitary cells (77). We believe that Go and Gi are involved with the Ca2+ channels, based on our findings (Fig.…”

Section: Discussionsupporting

confidence: 55%

Occurrence of the alpha subunits of G proteins in cerebral cortex synaptic membrane and postsynaptic density fractions: modulation of ADP-ribosylation by Ca2+/calmodulin.

Nigám

Ledoux

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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We have examined the isolated postsynaptic density (PSD) Pertussis Toxin-Activated ADP-Ribosylation. Pertussis toxin-activated ADP-ribosylation of SM and PSD proteins was performed as described using [32P]NADP (35). The samples were processed by SDS/PAGE and autoradiography (36), with the polyacrylamide gel being a 7.5-15% linear gradient in all cases. MATERIALS AND METHODS Materials. Guanosine 5'-[-[35S]thio]triphosphate (GTP[-35S]) (1400Immunochemical Characterization of the G Proteins. To identify the G proteins in the SM and PSD fractions, the subcellular fractions (60 ,ug each) were subjected to SDS/ PAGE and the resolved proteins in the gel were transferred electrophoretically to Immobilon (Millipore) paper as described (37). The Western blot blots were probed with anti-Ga antibodies followed by 125I-labeled protein A (38). 8686The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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Section: Discussionsupporting

confidence: 55%

Occurrence of the alpha subunits of G proteins in cerebral cortex synaptic membrane and postsynaptic density fractions: modulation of ADP-ribosylation by Ca2+/calmodulin.

Nigám

Ledoux

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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“…Neuroendocrine control of cardiac function, notably by vagal innervation or by circulating catecholamines, is an important mechanism for control of the rate and force of contraction of the heart. Acetylcholine binds to M 2 muscarinic cholinergic receptors to activate an inwardly rectifying K ϩ channel (IK.ACh), through a pertussis toxin-sensitive mechanism (65). Hyperpolarization contributes to a slowing of the rate of contraction of the heart.…”

Section: Ion Channelsmentioning

confidence: 99%

Physiological Regulation of G Protein-Linked Signaling

Morris

Malbon

1999

Physiological Reviews

403

294

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Heterotrimeric G proteins in vertebrates constitute a family molecular switches that transduce the activation of a populous group of cell-surface receptors to a group of diverse effector units. The receptors include the photopigments such as rhodopsin and prominent families such as the adrenergic, muscarinic acetylcholine, and chemokine receptors involved in regulating a broad spectrum of responses in humans. Signals from receptors are sensed by heterotrimeric G proteins and transduced to effectors such as adenylyl cyclases, phospholipases, and various ion channels. Physiological regulation of G protein-linked receptors allows for integration of signals that directly or indirectly effect the signaling from receptor-->G protein-->effector(s). Steroid hormones can regulate signaling via transcriptional control of the activities of the genes encoding members of G protein-linked pathways. Posttranscriptional mechanisms are under physiological control, altering the stability of preexisting mRNA and affording an additional level for regulation. Protein phosphorylation, protein prenylation, and proteolysis constitute major posttranslational mechanisms employed in the physiological regulation of G protein-linked signaling. Drawing upon mechanisms at all three levels, physiological regulation permits integration of demands placed on G protein-linked signaling.

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“…Taken together, these data suggest the involvement of cGMP in the signaling pathway for GN, UGN, and STa causing depolarizations of IHKE-1 cells. Activation of PT-sensitive G proteins open K ϩ channels in the plasma membrane which can cause hyperpolarizations (33,34). Therefore, we incubated cells with 1 g/ml PT for 24 h. Basal V m in these cells was Ϫ35.1 Ϯ 0.7 mV (n ϭ 14).…”

Section: Effects Of Gn Ugn Sta and 8-br-cgmp On Membranementioning

confidence: 99%

“…As shown before, activation of cAMP and increases in cellular Ca 2ϩ in IHKE-1 cells do not induce hyperpolarizations excluding an involvement of PKA and PKC (23). In muscle, neuron and kidney PT-sensitive G protein stimulation activates K ϩ channels (33,34). Crane et al (41) failed to demonstrate an effect of PT on GC-C-mediated effect of STa in the intestine excluding the involvement of G proteins in this signaling cascade.…”

Section: Effects Of Guanylin Peptides In Ihke-1 Cellsmentioning

confidence: 99%

Guanylin, Uroguanylin, and Heat-stable Euterotoxin Activate Guanylate Cyclase C and/or a Pertussis Toxin-sensitive G Protein in Human Proximal Tubule Cells

Sindiće¹,

Basoglu²,

Çerçi³

et al. 2002

Journal of Biological Chemistry

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Membrane guanylate cyclase C (GC-C) is the receptor for guanylin, uroguanylin, and heat-stable enterotoxin (STa) in the intestine. GC-C-deficient mice show resistance to STa in intestine but saluretic and diuretic effects of uroguanylin and STa are not disturbed. Here we describe the cellular effects of these peptides using immortalized human kidney epithelial (IHKE-1) cells with properties of the proximal tubule, analyzed with the slow-whole-cell patch clamp technique. Uroguanylin (10 or 100 nM) either hyperpolarized or depolarized membrane voltages (V m ). Guanylin and STa (both 10 or 100 nM), as well as 8-Br-cGMP (100 M), depolarized V m . All peptide effects were absent in the presence of 1 mM Ba 2؉ . Uroguanylin and guanylin changed V m pH dependently. Pertussis toxin (1 g/ml, 24 h) inhibited hyperpolarizations caused by uroguanylin. Depolarizations caused by guanylin and uroguanylin were blocked by the tyrosine kinase inhibitor, genistein (10 M). All three peptides increased cellular cGMP. mRNA for GC-C was detected in IHKE-1 cells and in isolated human proximal tubules. In IHKE-1 cells GC-C was also detected by immunostaining. These findings suggest that GC-C is probably the receptor for guanylin and STa. For uroguanylin two distinct signaling pathways exist in IHKE-1 cells, one involves GC-C and cGMP as second messenger, the other is cGMP-independent and connected to a pertussis toxin-sensitive G protein.

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Control of K+ channels by G proteins

Cited by 6 publications

References 58 publications

Occurrence of the alpha subunits of G proteins in cerebral cortex synaptic membrane and postsynaptic density fractions: modulation of ADP-ribosylation by Ca2+/calmodulin.

Occurrence of the alpha subunits of G proteins in cerebral cortex synaptic membrane and postsynaptic density fractions: modulation of ADP-ribosylation by Ca2+/calmodulin.

Physiological Regulation of G Protein-Linked Signaling

Guanylin, Uroguanylin, and Heat-stable Euterotoxin Activate Guanylate Cyclase C and/or a Pertussis Toxin-sensitive G Protein in Human Proximal Tubule Cells

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