Calmodulin- and Ca2+-Dependent Facilitation and Inactivation of the CaV1.2 Ca2+ Channels in Guinea-Pig Ventricular Myocytes

Han, Dong-Yun; Minobe, Etsuko; Wang, Wuyang; Guo, Feng; Xu, Jianjun; Liang, Hao; Kameyama, Masaki

doi:10.1254/jphs.09282fp

Cited by 30 publications

(47 citation statements)

References 49 publications

(45 reference statements)

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“…Since short preIQ and IQ peptides can bind with one molecule each of CaM, it is reasonable to state that the longer preIQ-IQ peptide binds with two molecules of CaM at the same time. This idea is consistent with our hypothesis that CaM binding to one site plays a role in CDF and the binding of the second CaM to the other site triggers CDI (24).…”

Section: Two Molecules Of Cam Bind To the C-terminus Of Cav12 Channelsupporting

confidence: 92%

Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels

et al. 2010

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Abstract. Although calmodulin binding to various sites of the Cav1.2 Ca 2+ channel has been reported, the mechanism of the interaction is not fully understood. In this study we examined calmodulin binding to fragment channel peptides using a semi-quantitative pull-down assay. Calmodulin bound to the peptides with decreasing affinity order: IQ > preIQ > I-II loop > N-terminal peptide. A peptide containing both preIQ and IQ regions (Leu 1599 -Leu 1668 ) bound with approximately 2 mol of calmodulin per peptide. These results support the hypothesis that two molecules of calmodulin can simultaneously bind to the C-terminus of the Cav1.2 channel and modulate its facilitatory and inhibitory activities.

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Section: Two Molecules Of Cam Bind To the C-terminus Of Cav12 Channelsupporting

confidence: 92%

Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels

et al. 2010

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“…Single ventricular myocytes of guinea-pig heart were obtained with an enzymatic dissociation protocol. 19,20) Briefly, animals were anaesthetized intraperitoneally with 100 mg/kg sodium pentoparbital. The heart was dissected out quickly and was mounted on a Langendorff apparatus for digestion.…”

Section: Animals and Cell Preparationmentioning

confidence: 99%

Effects of Astragaloside IV on Action Potentials and Ionic Currents in Guinea-Pig Ventricular Myocytes

Zhao

et al. 2013

Biological & Pharmaceutical Bulletin

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Astragaloside IV (AS-IV) is one of the main active constituents of Astragalus membranaceus, which has various actions on the cardiovascular system. However, its electrophysiological mechanisms are not clear. In the present study, we investigated the effects of AS-IV on action potentials and membrane currents using the whole-cell patch clamp technique in isolated guinea-pig ventricular myocytes. AS-IV prolonged the action potential duration (APD) at all three tested concentrations. The peak effect was achieved with 1×10 −6 m, at which concentration AS-IV significantly prolonged the APD at 95% repolarization from 313.1±38.9 to 785.3±83.7 ms. AS-IV at 1×10 −6 m also enhanced the inward rectifier K + currents (I K1 ) and inhibited the delayed rectifier K + currents (I K ). AS-IV (1×10 −6 m) strongly depressed the peak of voltage-dependent Ca 2+ channel current (I CaL ) from −607.3±37.5 to −321.1±38.3 pA. However, AS-IV was not found to affect the Na + currents. Taken together, AS-IV prolonged APD of guinea-pig ventricular myocytes, which might be explained by its inhibition of I K . AS-IV also influences Ca 2+ signaling through suppressing I CaL .

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“…-dependent regulations of the Cav1.2 channel [9][10][11]. Numerous studies have suggested that the tethering or binding sites in the C-terminal tail of Cav1.2 include an isoleucineglutamine motif (i.e., the IQ motif, a consensus CaM-binding motif in many proteins) [9] and a PreIQ motif [10] (referred to as peptides A and C [9]) (Fig.…”

Section: +mentioning

confidence: 99%

The Ca²⁺‐dependent interaction of calpastatin domain L with the C‐terminal tail of the Cav1.2 channel

Sun

Feng

et al. 2014

FEBS Letters

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Calmodulin- and Ca2+-Dependent Facilitation and Inactivation of the CaV1.2 Ca2+ Channels in Guinea-Pig Ventricular Myocytes

Abstract: Abstract. The L-type Ca 2+ channel (Ca V 1.2) shows clear Ca 2+

Cited by 30 publications

References 49 publications

Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels

Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels

Effects of Astragaloside IV on Action Potentials and Ionic Currents in Guinea-Pig Ventricular Myocytes

The Ca²⁺‐dependent interaction of calpastatin domain L with the C‐terminal tail of the Cav1.2 channel

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Calmodulin- and Ca2+-Dependent Facilitation and Inactivation of the CaV1.2 Ca2+ Channels in Guinea-Pig Ventricular Myocytes

Abstract: Abstract. The L-type Ca 2+ channel (Ca V 1.2) shows clear Ca 2+

Cited by 30 publications

References 49 publications

Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels

Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels

Effects of Astragaloside IV on Action Potentials and Ionic Currents in Guinea-Pig Ventricular Myocytes

The Ca2+‐dependent interaction of calpastatin domain L with the C‐terminal tail of the Cav1.2 channel

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The Ca²⁺‐dependent interaction of calpastatin domain L with the C‐terminal tail of the Cav1.2 channel