Single‐channel properties of BK‐type calcium‐activated potassium channels at a cholinergic presynaptic nerve terminal

Sun, Xiaoping; Schlichter, Lyanne C.; Stanley, Elise F.

doi:10.1111/j.1469-7793.1999.0639p.x

Cited by 41 publications

(33 citation statements)

References 49 publications

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“…1, 2). This resembles the arrangement in frog neuromuscular junction (Robitaille et al, 1993), whereas in chick ciliary ganglion BK channels were found on both the release face and non-release face of the presynaptic calyx (Sun et al, 1999). Being near the release sites, the BK channels may be colocalized with, and functionally coupled to, the voltage-gated Ca 2ϩ channels that trigger transmitter release, which in these synapses are of the N and P/Q types (Wheeler et al, 1994;Malenka and Nicoll, 1999).…”

Section: The Immunogold Datamentioning

confidence: 58%

“…Although presynaptic Ca 2ϩ -activated K ϩ channels have been described in some peripheral synapses (Gho and Ganetzky, 1992;Meir et al, 1999;Sun et al, 1999;Yazejian et al, 2000) and have often been assumed to control synaptic transmission, to our knowledge this has actually been demonstrated under normal conditions only in frog and lizard neuromuscular junction (Robitaille and Charlton, 1992;Robitaille et al, 1993;Blundon et al, 1995). Thus, the enigmatic silence of presynaptic BK channels may be a widespread phenomenon and could be caused by several factors.…”

Section: Bk Channels and Regulation Of Transmitter Releasementioning

confidence: 94%

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Presynaptic Ca²⁺-Activated K⁺Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Shao

Chavoshy³

et al. 2001

J. Neurosci.

307

303

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Large-conductance Ca 2ϩ -activated K ϩ channels (BK, also called Maxi-K or Slo channels) are widespread in the vertebrate nervous system, but their functional roles in synaptic transmission in the mammalian brain are largely unknown. By combining electrophysiology and immunogold cytochemistry, we demonstrate the existence of functional BK channels in presynaptic terminals in the hippocampus and compare their functional roles in somata and terminals of CA3 pyramidal cells. Doublelabeling immunogold analysis with BK channel and glutamate receptor antibodies indicated that BK channels are targeted to the presynaptic membrane facing the synaptic cleft in terminals of Schaffer collaterals in stratum radiatum. Whole-cell, intracellular, and field-potential recordings from CA1 pyramidal cells showed that the presynaptic BK channels are activated by calcium influx and can contribute to repolarization of the presynaptic action potential (AP) and negative feedback control of Ca 2ϩ influx and transmitter release. This was observed in the presence of 4-aminopyridine (4-AP, 40-100 M), which broadened the presynaptic compound action potential. In contrast, the presynaptic BK channels did not contribute significantly to regulation of action potentials or transmitter release under basal experimental conditions, i.e., without 4-AP, even at high stimulation frequencies. This is unlike the situation in the parent cell bodies (CA3 pyramidal cells), where BK channels contribute strongly to action potential repolarization. These results indicate that the functional role of BK channels depends on their subcellular localization.

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Section: The Immunogold Datamentioning

confidence: 58%

Section: Bk Channels and Regulation Of Transmitter Releasementioning

confidence: 94%

Presynaptic Ca²⁺-Activated K⁺Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Shao

Chavoshy³

et al. 2001

J. Neurosci.

307

303

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“…The outward current was completely blocked by perfusion with TEA 30 mM saline ( Figure 4a) and was insensitive to Cl In the presence of 100 nM ChTx and paxilline (Figure 4b), two selective blockers of BK-type Ca 2ϩ -activated voltage-dependent K ϩ channels (18,19), the total I K was decreased to 55.0 Ϯ 17.3% (ChTx, n ϭ 3) and to 48.5 Ϯ 15.4% (paxilline, n ϭ 3). Conversely, 100 M apamine, a selective blocker of SK-type Ca 2ϩ -dependent K ϩ channels (20), and 100 M nifedipine, an L-type Ca V -channel blocker, were ineffective (Figure 4b).…”

Section: Outward Currentmentioning

confidence: 99%

Nonspecific Cation Current Associated with Native Polycystin-2 in HEK-293 Cells

Pelucchi¹,

Aguiari²,

Pignatelli³

et al. 2006

Journal of the American Society of Nephrology

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Mutations in either PKD1 or PKD2 gene are associated with autosomal dominant polycystic kidney disease, the most common inherited kidney disorder. Polycystin-2 (PC2), the PKD2 gene product, and the related protein polycystin-L, function as Ca 2؉ -permeable, nonselective cation channels in different expression systems. This work describes a nonspecific cation current (I CC ) that is present in native HEK-293 cells and highly associated with a PC2-channel activity. The current is voltage dependent, activating for potentials that are positive to ؊50 mV and inactivating in a few milliseconds. It is sensitive to Cd 2؉ , Gd 3؉ , La 3؉ , SKF96365, and amiloride. After silencing of PC2 by RNA interfering, cells show a reduced current that is restored by transfection with normal but not truncated PC2. Consistently, I CC is abolished by perfusion with an anti-PC2 antibody. Furthermore, heterologous expression of the PC1 cytoplasmic tail significantly increases I CC peak amplitude compared with native cells. This is the first characterization of such a current in HEK-293 cells, a widely used expression system for ion channels. These cells, therefore, could be regarded as a suitable and readily accessible tool to study interactions between native PC2/PC1 complex and other membrane proteins, thus contributing to the understanding of autosomal dominant polycystic kidney disease pathogenesis.

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“…Then, Src tyrosine kinase and protein kinase A (PKA) catalytic subunit also are found to interact with Drosophila BK Ca channels (Wang et al, 1999). In neuronal cells, BK Ca channels control calcium influxes and regulate the neurotransmitter release (Roberts et al, 1990;Sun et al, 1999), process that may require the colocalization with calcium channels at presynaptic sites (Issa and Hudspeth, 1994;Marrion and Tavalin, 1998;Hu et al, 2001;Orio et al, 2002). Recently, it was reported that ␤2 adrenergic receptor could simultaneously interact with both BK Ca and L-type Ca 2ϩ channels in vivo (Liu et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Identification and Functional Characterization of Ankyrin-Repeat Family Protein ANKRA as a Protein Interacting with BK_CaChannel

Lim

Park

2005

MBoC

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Ankyrin-repeat family A protein (ANKRA) was originally cloned in mouse as an interacting protein to megalin, a member of low-density lipoprotein receptor superfamily. Here, we report that the isolation of rat ANKRA as a new binding partner for the ␣-subunit of rat large-conductance Ca 2؉ -activated K ؉ channel (rSlo). We mapped the binding region of each protein by using yeast two-hybrid and in vitro binding assays. ANKRA expressed together with rSlo channels were colocalized near the plasma membrane and coimmunoprecipitated in transfected cells. We also showed that BK Ca channel in rat cerebral cortex coprecipitated with rANKRA and colocalized in cultured rat hippocampal neuron. Although the coexpression of ANKRA did not affect the surface expression of rSlo, the gating kinetics of rSlo channel was significantly altered and the effects were highly dependent on the intracellular calcium. These results indicate that ANKRA could modulate the excitability of neurons by binding directly to endogenous BK Ca channel and altering its gating kinetics in a calcium-dependent manner.

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Single‐channel properties of BK‐type calcium‐activated potassium channels at a cholinergic presynaptic nerve terminal

Abstract: Art et al. 1995) which share many properties with fast-transmitting nerve terminals. It is not clear which specific types of KCa channel are present at most of these sites but, where tested by specific staining or direct recording, the high-conductance, BK-type has been repeatedly observed

Cited by 41 publications

References 49 publications

Presynaptic Ca²⁺-Activated K⁺Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Presynaptic Ca²⁺-Activated K⁺Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Nonspecific Cation Current Associated with Native Polycystin-2 in HEK-293 Cells

Identification and Functional Characterization of Ankyrin-Repeat Family Protein ANKRA as a Protein Interacting with BK_CaChannel

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Single‐channel properties of BK‐type calcium‐activated potassium channels at a cholinergic presynaptic nerve terminal

Cited by 41 publications

References 49 publications

Presynaptic Ca2+-Activated K+Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Presynaptic Ca2+-Activated K+Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Nonspecific Cation Current Associated with Native Polycystin-2 in HEK-293 Cells

Identification and Functional Characterization of Ankyrin-Repeat Family Protein ANKRA as a Protein Interacting with BKCaChannel

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Presynaptic Ca²⁺-Activated K⁺Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Presynaptic Ca²⁺-Activated K⁺Channels in Glutamatergic Hippocampal Terminals and Their Role in Spike Repolarization and Regulation of Transmitter Release

Identification and Functional Characterization of Ankyrin-Repeat Family Protein ANKRA as a Protein Interacting with BK_CaChannel