Regulation of ATP-sensitive K+ channels by caveolin-enriched microdomains in cardiac myocytes

Garg, Vivek; Jiao, Jundong; Hu, Keli

doi:10.1093/cvr/cvp039

Cited by 45 publications

(40 citation statements)

References 34 publications

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“…In vascular smooth muscle, caveolin-1 was described to interact with the K ATP channel and that this suppresses gating by reducing the sensitivity of channels to the stimulatory influence of MgADP (162). Kir6.2 was also described to associate with caveolin-3 (but not caveolin-1), and it was found that ventricular K ATP channels are negatively regulated by caveolin (256). A possible role for this interaction and the presence of K ATP channels in caveolae is to localize receptor signaling to K ATP channels in smooth muscle and the endothelium (606,687,688).…”

Section: Other Interacting Proteinsmentioning

confidence: 99%

K_ATPChannels in the Cardiovascular System

Foster

Coetzee

2016

Physiological Reviews

204

237

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KATP channels are integral to the functions of many cells and tissues. The use of electrophysiological methods has allowed for a detailed characterization of KATP channels in terms of their biophysical properties, nucleotide sensitivities, and modification by pharmacological compounds. However, even though they were first described almost 25 years ago (Noma 1983, Trube and Hescheler 1984), the physiological and pathophysiological roles of these channels, and their regulation by complex biological systems, are only now emerging for many tissues. Even in tissues where their roles have been best defined, there are still many unanswered questions. This review aims to summarize the properties, molecular composition, and pharmacology of KATP channels in various cardiovascular components (atria, specialized conduction system, ventricles, smooth muscle, endothelium, and mitochondria). We will summarize the lessons learned from available genetic mouse models and address the known roles of KATP channels in cardiovascular pathologies and how genetic variation in KATP channel genes contribute to human disease.

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Section: Other Interacting Proteinsmentioning

confidence: 99%

K_ATPChannels in the Cardiovascular System

Foster

Coetzee

2016

Physiological Reviews

204

237

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“…To test this scenario, mouse atrial myocytes were pretreated with M␤CD, which disrupts caveolae by depleting cholesterol (21,22). We confirmed that treatment with 3 mM M␤CD for 10 min did not affect I GIRK .…”

Section: Caveolar Disruption Abolishes Receptor Specificity Of Girkmentioning

confidence: 55%

“…Although the caveolae of ventricle modulate excitation-contraction coupling, ␤ 2 -adrenergic signaling, and ATP-sensitive K ϩ channel regulation (21,22,29), the role of caveolae in the atria remains unclear. The current data showed that caveolae can act as signaling platforms linking GIRK channels and GqPCRs in mouse atrial myocytes.…”

Section: Discussionmentioning

confidence: 99%

Agonist-induced Localization of Gq-coupled Receptors and G Protein-gated Inwardly Rectifying K+ (GIRK) Channels to Caveolae Determines Receptor Specificity of Phosphatidylinositol 4,5-Bisphosphate Signaling

Cui

Kim

et al. 2010

Journal of Biological Chemistry

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Several lines of evidence suggest that neurohormonal imbalance plays a role in the generation of atrial fibrillation (1). Simultaneous sympathetic and parasympathetic (sympathovagal) activation facilitates the onset of paroxysmal atrial fibrillation (2). In addition, vasoactive peptide hormones such as endothelin-1 (ET-1) 3 (3) and angiotensin II (4) have been implicated in atrial fibrillation. The cardiovascular actions of native peptides and receptors showed a wide range of variety. Unlike ET-1 and angiotensin II, myocardial bradykinin (BK) might be a mechanism to protect the heart during acute myocardial infarction (5, 6). The neurohormonal imbalances have seldom been sufficiently characterized to study their pathophysiology.One possible candidate for cross-talk for sympathovagal interaction and neurohormonal interaction in cardiac myocytes is the acetylcholine activated K ϩ (GIRK) channel. Recently, we and others found that ␣ 1 -adrenergic receptor agonist inhibits GIRK channels by depleting PIP 2 in the plasma membrane, indicating a novel pathway for sympathetic-parasympathetic interaction (7,8). ET-1 and angiotensin II can also regulate GIRK channel activity via PIP 2 signaling (8, 9). Thus, GIRK channels might act as points to integrate hormonal and neurotransmitter signals from diverse pathways. However, although GIRK channels are regulated by PIP 2 , they do not respond to PIP 2 hydrolysis from stimulation of all Gqcoupled receptors. We found that BK had no effect on GIRK channels, although being capable of hydrolyzing PIP 2 in cardiac myocytes (9). It is possible that these selective responses could discriminate the beneficial effect associated with BK from other Gq protein-coupled receptor (GqPCR) pathways. Until now, the molecular mechanisms underlying receptor specificity have been mostly unknown.Several mechanisms were suggested to explain the receptor-specific and target-specific PIP 2 signaling. One of those mechanisms is the PIP 2 microdomain (10). In this scenario, PIP 2 abundance can change independently within a restricted area, so that the activation of a given GqPCR affects only *

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“…20 Briefly, cells were pretreated with or without hypoxic preconditioning and then were spin down and resuspended in 0.5 M sodium carbonate (pH 11.0; 2 ml). Subsequently the cell homogenates were subjected to centrifugation at 4 C, and the supernatant was received.…”

Section: Purification Of Caveolin-enriched Membrane Fractionsmentioning

confidence: 99%

“…19 Immunoprecipitation experiments were performed according to the previous report. 20,21 The cardiac myocytes were isolated and then pretreated with or without hypoxic preconditioning prior to homogenization. The cells were lysed and centrifuged to get supernatant.…”

Section: Western Blot and Co-immunoprecipitationmentioning

confidence: 99%

Hypoxic preconditioning promotes the translocation of protein kinase C ε binding with caveolin-3 at cell membrane not mitochondrial in rat heart

Yang

et al. 2015

Cell Cycle

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& Wei Sun (2015) Hypoxic preconditioning promotes the translocation of protein kinase C ε binding with caveolin-3 at cell membrane not mitochondrial in rat heart, Cell Cycle, 14:22, 3557-3565, DOI: 10.1080/15384101.2015 Keywords: caveolin, FRET, mitochondria, preconditioning, PKC Protein kinase C has been shown to play a central role in the cardioprotection of ischemic preconditioning. However, the mechanism underlying PKC-mediated cardioprotection is not completely understood. Given that caveolae are critical for PKC signaling, we sought to determine whether hypoxic preconditioning promotes translocation and association of PKC isoforms with caveolin-3. A cellular model of hypoxic preconditioning from adult rat cardiac myocytes (ARCM) or H9c2 cells was employed to examine PKC isoforms by molecular, biochemical and cellular imaging analysis. Hypoxia was induced by incubating the cells in an airtight chamber in which O 2 was replaced by N 2 with glucose-free Tyrode's solution. Cells were subjected to hypoxic preconditioning with 10 minutes of hypoxia followed by 30 minutes of reoxygenation. Western blot data indicated that the band intensity for PKCe, PKCd or PKCa, but not PKCb and PKCz was enhanced significantly by hypoxic preconditioning from the caveolin-enriched plasma membrane interactions. Immunoprecipitation experiments from the caveolin-enriched membrane fractions of ARCM showed that the level of PKCe, PKCd and PKCa in the anti-caveolin-3 immunoprecipitates was also increased by hypoxic preconditioning. Further, our FRET analysis in H9c2 cells suggested that there is a minimum FRET signal for caveolin-3 and PKCe along cell peripherals, but hypoxic preconditioning enhanced the FRET signal, indicating a potential interaction between caveolin-3 and PKCe. And also treatment of the cells with hypoxic preconditioning led to a smaller amount of translocation of PKCe to the mitochondria than that to the membrane. We demonstrate that hypoxic preconditioning promotes rapid association of PKCe, PKCd and PKCa with the caveolin-enriched plasma membrane microdomain of cardiac myocytes, and PKCe via direct molecular interaction with caveolin-3. This regulatory mechanism may play an important role in cardioprotection.

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Regulation of ATP-sensitive K+ channels by caveolin-enriched microdomains in cardiac myocytes

Abstract: We demonstrate that K(ATP) channels are localized to caveolin-enriched microdomains. This microdomain association is essential for adenosine receptor-mediated regulation of K(ATP) channels in cardiac myocytes.

Cited by 45 publications

References 34 publications

K_ATPChannels in the Cardiovascular System

K_ATPChannels in the Cardiovascular System

Agonist-induced Localization of Gq-coupled Receptors and G Protein-gated Inwardly Rectifying K+ (GIRK) Channels to Caveolae Determines Receptor Specificity of Phosphatidylinositol 4,5-Bisphosphate Signaling

Hypoxic preconditioning promotes the translocation of protein kinase C ε binding with caveolin-3 at cell membrane not mitochondrial in rat heart

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Regulation of ATP-sensitive K+ channels by caveolin-enriched microdomains in cardiac myocytes

Abstract: We demonstrate that K(ATP) channels are localized to caveolin-enriched microdomains. This microdomain association is essential for adenosine receptor-mediated regulation of K(ATP) channels in cardiac myocytes.

Cited by 45 publications

References 34 publications

KATPChannels in the Cardiovascular System

KATPChannels in the Cardiovascular System

Agonist-induced Localization of Gq-coupled Receptors and G Protein-gated Inwardly Rectifying K+ (GIRK) Channels to Caveolae Determines Receptor Specificity of Phosphatidylinositol 4,5-Bisphosphate Signaling

Hypoxic preconditioning promotes the translocation of protein kinase C ε binding with caveolin-3 at cell membrane not mitochondrial in rat heart

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K_ATPChannels in the Cardiovascular System

K_ATPChannels in the Cardiovascular System