Definition
Ion channels are used as biosensors in order to visualize the spatiotemporal changes that occur in cyclic nucleotides in living cells.
Introduction
Ion channels are pore-forming proteins that allow the flow of ions down their electrochemical gradient thus helping to establish and control the small voltage gradient across the plasma membrane of cells. They are present in the membranes that surround all biological cells and can be distinguished based upon their ion selectivity, gating mechanism, and sequence similarity. Ion channels can be voltage gated, ligand gated, pH gated, or mechanically gated. These gating criteria along with a combination of sequence similarity and ion selectivity further subdivide ion channels into several subtypes:
Voltage-gated ion channels which open and close in response to membrane potential such as the voltage-gated sodium channels,...
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Abi-Gerges A, Richter W, Lefebvre F, Matéo P, Varin A, Heymes C, Samuel J-L, Lugnier C, Conti M, Fischmeister R, Vandecasteele G. Decreased expression and activity of cAMP phosphodiesterases in cardiac hypertrophy and its impact on ß-adrenergic cAMP signals. Circ Res. 2009;105:784–92.
Baruscotti M, Bucchi A, DiFrancesco D. Physiology and pharmacology of the cardiac pacemaker (“funny”) current. Pharmacol Ther. 2005;107:59–79.
Bers DM. Cardiac excitation-contraction coupling. Nature. 2002;415:198–205.
Biel M, Schneider A, Wahl C. Cardiac HCN channels: structure, function, and modulation. Trends Cardiovasc Med. 2002;12:206–12.
Bos JL. Epac: a new cAMP target and new avenues in cAMP research. Nat Rev Mol Cell Biol. 2003;4:733–8.
Brady JD, Rich TC, Le X, Stafford K, Fowler CJ, Lynch L, Karpen JW, Brown RL, Martens JR. Functional role of lipid raft microdomains in cyclic nucleotide-gated channel activation. Mol Pharmacol. 2004;65:503–11.
Castro LRV, Verde I, Cooper DMF, Fischmeister R. Cyclic guanosine monophosphate compartmentation in rat cardiac myocytes. Circulation. 2006;113:2221–8.
Castro LRV, Schittl J, Fischmeister R. Feedback control through cGMP-dependent protein kinase contributes to differential regulation and compartmentation of cGMP in rat cardiac myocytes. Circ Res. 2010;107:1232–40.
Dhein S, Van Koppen CJ, Brodde OE. Muscarinic receptors in the mammalian heart. Pharmacol Res. 2001;44:161–82.
Dubois J-M. Physiologie et pharmacologie des canaux Na et K des membranes axonales. J Physiol Paris. 1985;80:120–8.
Fagan KA, Schaack J, Zweifach A, Cooper DMF. Adenovirus encoded cyclic nucleotide-gated channels: a new methodology for monitoring cAMP in living cells. FEBS Lett. 2001;500:85–90.
Fischmeister R, Castro L, Abi-Gerges A, Rochais F, Vandecasteele G. Species- and tissue-dependent effects of NO and cyclic GMP on cardiac ion channels. Comp Biochem Physiol A Mol Integr Physiol. 2005;142:136–43.
Fischmeister R, Castro LRV, Abi-Gerges A, Rochais F, Jurevičius J, Leroy J, Vandecasteele G. Compartmentation of cyclic nucleotide signaling in the heart: the role of cyclic nucleotide phosphodiesterases. Circ Res. 2006;99:816–28.
Honda A, Adams SR, Sawyer CL, Lev-Ram V, Tsien RY, Dostmann WR. Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator. Proc Natl Acad Sci USA. 2001;98:2437–42.
Kaupp UB, Seifert R. Cyclic nucleotide-gated ion channels. Physiol Rev. 2002;82:769–824.
Layland J, Li JM, Shah AM. Role of cyclic GMP-denendent protein kinase in the contractile response to exogenous nitric oxide in rat cardiac myocytes. J Physiol. 2002;540:457–67.
Leroy J, Abi-Gerges A, Nikolaev VO, Richter W, Lechęne P, Mazet J-L, Conti M, Fischmeister R, Vandecasteele G. Spatiotemporal dynamics of ß-adrenergic cAMP signals and L-type Ca2+ channel regulation in adult rat ventricular myocytes: role of phosphodiesterases. Circ Res. 2008;102:1091–100.
Mangoni ME, Nargeot J. Genesis and regulation of the heart automaticity. Physiol Rev. 2008;88:919–82.
Méry P-F, Lohmann SM, Walter U, Fischmeister R. Ca2+ current is regulated by cyclic GMP-dependent protein kinase in mammalian cardiac myocytes. Proc Natl Acad Sci USA. 1991;88:1197–201.
Morel E, Marcantoni A, Gastineau M, Birkedal R, Rochais F, Garnier A, Lompré A-M, Vandecasteele G, Lezoualc’h F. The cAMP-binding protein Epac induces cardiomyocyte hypertrophy. Circ Res. 2005;97:1296–304.
Nikolaev VO, Bunemann M, Hein L, Hannawacker A, Lohse MJ. Novel single chain cAMP sensors for receptor-induced signal propagation. J Biol Chem. 2004;279:37215–8.
Nikolaev VO, Gambaryan S, Engelhardt S, Walter U, Lohse MJ. Real-time monitoring of live cell’s PDE2 activity: hormone-stimulated cAMP hydrolysis is faster than hormone-stimulated cAMP synthesis. J Biol Chem. 2005;280:1716–9.
Nikolaev VO, Bunemann M, Schmitteckert E, Lohse MJ, Engelhardt S. Cyclic AMP imaging in adult cardiac myocytes reveals far-reaching ß1-adrenergic but locally confined ß2 -adrenergic receptor-mediated signaling. Circ Res. 2006;99:1084–91.
Ponsioen B, Zhao J, Riedl J, Zwartkruis F, van der Krogt G, Zaccolo M, Moolenaar WH, Bos JL, Jalink K. Detecting cAMP-induced Epac activation by fluorescence resonance energy transfer: Epac as a novel cAMP indicator. EMBO Rep. 2004;5:1176–80.
Rich TC, Karpen JW. Review article: cyclic AMP sensors in living cells: what signals can they actually measure? Ann Biomed Eng. 2002;30:1088–99.
Rich TC, Fagan KA, Nakata H, Schaack J, Cooper DMF, Karpen JW. Cyclic nucleotide-gated channels colocalize with adenylyl cyclase in regions of restricted cAMP diffusion. J Gen Physiol. 2000;116:147–61.
Rich TC, Fagan KA, Tse TE, Schaack J, Cooper DM, Karpen JW. A uniform extracellular stimulus triggers distinct cAMP signals in different compartments of a simple cell. Proc Natl Acad Sci USA. 2001a;98:13049–54.
Rich TC, Tse TE, Rohan JG, Schaack J, Karpen JW. In vivo assessment of local phosphodiesterase activity using tailored cyclic nucleotide-gated channels as cAMP sensors. J Gen Physiol. 2001b;118:63–77.
Rochais F, Vandecasteele G, Lefebvre F, Lugnier C, Lum H, Mazet J-L, Cooper DMF, Fischmeister R. Negative feedback exerted by PKA and cAMP phosphodiesterase on subsarcolemmal cAMP signals in intact cardiac myocytes. An in vivo study using adenovirus-mediated expression of CNG channels. J Biol Chem. 2004;279:52095–105.
Rochais F, Abi-Gerges A, Horner K, Lefebvre F, Cooper DMF, Conti M, Fischmeister R, Vandecasteele G. A specific pattern of phosphodiesterases controls the cAMP signals generated by different Gs-coupled receptors in adult rat ventricular myocytes. Circ Res. 2006;98:1081–8.
Schroder F, Klein G, Fiedler B, Bastein M, Schnasse N, Hillmer A, Ames S, Gambaryan S, Drexler H, Walter U, Lohmann SM, Wollert KC. Single L-type Ca2+ channel regulation by cGMP-dependent protein kinase type I in adult cardiomyocytes from PKG I transgenic mice. Cardiovasc Res. 2003;60:268–77.
Vandecasteele G, Rochais F, Abi-Gerges A, Fischmeister R. Functional localization of cAMP signalling in cardiac myocytes. Biochem Soc Trans. 2006;34:484–8.
Willoughby D, Cooper DM. Organization and Ca2+ regulation of adenylyl cyclases in cAMP microdomains. Physiol Rev. 2007;87:965–1010.
Willoughby D, Cooper DM. Live-cell imaging of cAMP dynamics. Nat Methods. 2008;5:29–36.
Zaccolo M. Use of chimeric fluorescent proteins and fluorescence resonance energy transfer to monitor cellular responses. Circ Res. 2004;94:866–73.
Zaccolo M, De Giorgi F, Cho CY, Feng L, Knapp T, Negulescu PA, Taylor SS, Tsien RY, Pozzan T. A genetically encoded, fluorescent indicator for cyclic AMP in living cells. Nat Cell Biol. 2000;2:25–9.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 European Biophysical Societies' Association (EBSA)
About this entry
Cite this entry
Abi-Gerges, A., Fischmeister, R. (2013). Ion Channels: New Tools to Track Cyclic Nucleotide Changes in Living Cells. In: Roberts, G.C.K. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16712-6_377
Download citation
DOI: https://doi.org/10.1007/978-3-642-16712-6_377
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-16711-9
Online ISBN: 978-3-642-16712-6
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences