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Fluorescence Spectroscopy to Probe the Structure and Cellular Dynamics of Ion Channels

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Ion Channels
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Abstract

Ion channels are of universal importance owing to their mediation of several physiological responses such as excitability in nerve and muscle, stimulus-secretion, and cellular motility, to mention only a few. The past several years has seen an active increase in the biochemical and molecular characterization of ion channel structure and function using combined biophysical and biochemical approaches.

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References

  • Angelides, K. J., 1981a, Application of photoactivatable fluorescence active-site directed probes to serine-containing enzymes, Biochim. Biophys. Acta 669:149–155.

    PubMed  CAS  Google Scholar 

  • Angelides, K. J., 1981b, Fluorescent and photoactivatable fluorescent derivatives of tetrodotoxin to probe the sodium channel of excitable membranes, Biochemistry 20:4107–4118.

    Article  PubMed  CAS  Google Scholar 

  • Angelides, K. J., 1986, Fluorescently Labeled Na+ channels are localized and immobilized to synapses of innervated muscle fibers, Nature 321:63–66.

    Article  PubMed  CAS  Google Scholar 

  • Angelides, K. J., and Brown, G. B., 1984, Fluorescence resonance energy transfer on the voltagedependent sodium channel: Spatial relationship and site coupling between the batrachotoxin and Leuirus quinquestriatus α-scorpion toxin receptors, J. Biol.Chem. 259:6117–6126.

    PubMed  CAS  Google Scholar 

  • Angelides, K. J., and Hammes, G. G., 1979, Fluorescence studies of the pyruvate dehydrogenase multienzyme complex from E. coli, Biochemistry 18:1223–1229.

    Article  PubMed  CAS  Google Scholar 

  • Angelides, K. J., and Nutter, T. J., 1983a, Preparation and characterization of fluorescent scorpion toxins from Leuirus quinquestriatusquinquestriatus as probes of the sodium channel of excitable cells, J. Biol. Chem. 258:11948–11957.

    PubMed  CAS  Google Scholar 

  • Angelides, K. J., and Nutter, T. J., 1983b, Mapping the molecular structure of the voltagedependent sodium channel: Distances between the tetrodotoxin and Leiurus quinquestriatus quinquestriatus scorpion toxin receptors, J. Biol. Chem. 258:11958–11967.

    PubMed  CAS  Google Scholar 

  • Angelides, K. J., and Nutter, T. J., 1984, Molecular and cellular mapping of voltage-dependent Na+ channel, Biophys. J. 45:31–34.

    Article  PubMed  CAS  Google Scholar 

  • Angelides, K. J., Elmer, L. W., Nutter, T. J., and Kempner, E. S., 1985, Functional unit size of the neurotoxin receptors on the voltage-dependent sodium channel, J. Biol. Chem. 60:3431–3439.

    Google Scholar 

  • Angelides, K. J., Elmer, L. W., Loftus, D., and Elson, E. L., 1987, Regionalization and lateral mobility of Na + channels in neuronal cells, J. Cell Biol. (in press).

    Google Scholar 

  • Axelrod, D. A., 1983, Lateral motion of membrane proteins and biological function, J. Membr. Biol. 75:1–16.

    Article  PubMed  CAS  Google Scholar 

  • Beam, K. G., Caldwell, J. H., and Campbell, J. T., 1985, Na channels in skeletal muscle concentrated near the neuromuscular junction, Nature 313:588–590.

    Article  PubMed  CAS  Google Scholar 

  • Beardsly, K., and Cantor, C. R., 1970, Studies of transfer RNA tertiary structure by singlet-singlet energy transfer, Proc. Natl. Acad. Sci. USA 65:39–46.

    Article  Google Scholar 

  • Brazil, O. V., Franceschi-Prado, M., and Laure, C. J., 1979, Repetitive muscle responses induced by crotamine, Toxicon 17:61–67.

    Article  PubMed  CAS  Google Scholar 

  • Bright, G. R., and Taylor, D. L., 1986, Imaging at low light levels in fluorescence microscopy, in: Applications of Fluorescence to the Biomedical Sciences (D. L. Taylor, A. Waggoner, D. Murphy, F. Lanni, and R. Birge, eds.), pp. 257–288, Liss, New York.

    Google Scholar 

  • Catterall, W. A., 1980, Neurotoxins that act on voltage-sensitive Na + channels in excitable membranes, Annu. Rev. Pharmacol. Toxicol. 20:15–41.

    Article  PubMed  CAS  Google Scholar 

  • Catterall, W. A., and Risk, M. A., 1981, Toxin T4(6) from Ptychodiscus brevis (formerly Gymnodinium breve) enhances activation of voltage-sensitive sodium channels by veratridine, Mol. Pharmacol. 19:345–350.

    PubMed  CAS  Google Scholar 

  • Cherry, R. J., 1979, Rotational and lateral diffusion of membrane, proteins, Biochim. Biophys. Acta 559:289–310.

    PubMed  CAS  Google Scholar 

  • Chicheportiche, R., Balerna, M., Lombet, A., Romey, G., and Lazdunski, M., 1979, Synthesis and mode of action on axonal membranes of photoactivatable derivatives of tetrodotoxin, J. Biol. Chem. 254:1552–1557.

    PubMed  CAS  Google Scholar 

  • Darbon, H., and Angelides, K. J., 1984, Structural mapping of the voltage-dependent sodium channel: Distance between the tetrodotoxin and Centruroides suffusus suffusus B-scorpion toxin receptors,J. Biol. Chem. 259:6074–6084.

    PubMed  CAS  Google Scholar 

  • Ellisman, M. H., and Porter, K. R., 1980, Microtrabecular structure of the axoplasmic matrix: Visualization of cross-linking structures and their distribution, J. Cell Biol. 87:464–479.

    Article  PubMed  CAS  Google Scholar 

  • Elmer, L. W., O’Brien, B., Nutter, T. J., and Angelides, K. J., 1985, Physico-chemical characterization of the a-peptide, Biochemistry 24:8128–8137.

    Article  PubMed  CAS  Google Scholar 

  • Elson, E. L., and Reidler, J. A., 1979, Analysis of cell surface interactions by measurements of lateral mobility, J. Supramol. Struc. 12:481–490.

    Article  CAS  Google Scholar 

  • Elson, E.L., and Schlessinger, J., 1983, Long-range motion on cell surfaces, in: The Neurosciences 4th Study Program (F. O. Schmitt, ed.), pp. 1–5, MIT Press, Cambridge, Mass.

    Google Scholar 

  • Forster, T., 1948, Intermolecular energy migration and fluorescence (R. S. Knox, trans.), Ann. Phys.(Leipzig) 2:55–75.

    CAS  Google Scholar 

  • Forster, T., 1965, Modern quantum chemistry, Lect. Istanbul Inst. Summer Sch. 3:93–103.

    Google Scholar 

  • Garland, P. B., and Moore, C. H., 1979, Phosphorescence of protein-bound eosin and erythrosin: A possible probe for measurements of slow rotational mobility, Biochem. J. 183:561–569.

    PubMed  CAS  Google Scholar 

  • Gundersen, R. W., and Barrett, J. N., 1984, Neurite growth cone-substratum adherence increases in vitro, Dev. Brain Res. 12:21–29.

    Article  Google Scholar 

  • Guy, R., and Seetharlamu, P., 1986, Molecular model of the action potential Na+ channel, Proc. Natl. Acad. Sci. USA 83:508–512.

    Article  PubMed  CAS  Google Scholar 

  • Haas, E., Katchalski-Katzir, E., and Steinberg, I. Z., 1978, Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization, Biochemistry 17:5064–5070.

    Article  PubMed  CAS  Google Scholar 

  • Hartshorne, R. P., and Catterall, W. A., 1984, The sodium channel from rat brain: Purification and subunit composition, J. Biol. Chem. 259:1667–1672.

    PubMed  CAS  Google Scholar 

  • Haugland, R. P., Yguerabide, J., and Stryer, L., 1969, Dependence of the kinetics of singlet-singlet energy transfer on spectral overlap, Proc. Natl. Acad. Sci. USA 63:23–30.

    Article  PubMed  CAS  Google Scholar 

  • Highsmith, S., 1978, Heavy meromyosin binds actin with negative cooperativity, Biochemistry 17:22–26.

    Article  PubMed  CAS  Google Scholar 

  • Huang, K. H., Fairclough, R. H., and Cantor, C. R., 1975, Surface topography of the 30 s Escherichia coli ribosomal subunit: Reactivity towards fluorescein isothiocyanate, J. Mol. Biol. 97:443–470.

    Article  PubMed  CAS  Google Scholar 

  • Hugues, M., Romey, G., Duval, D., Vincent, T. P., and Lazdunski, M., 1982, Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: Voltage-clamp and biochemical characterization of the toxin receptor, Proc. Natl. Acad. Sci. USA 79:1308–1312.

    Article  CAS  Google Scholar 

  • Koppel, D. E., 1979, Fluorescence redistribution after photobleaching: A new multipoint analysis of membrane translational dynamics, Biophys.J. 28:281–289.

    Article  PubMed  CAS  Google Scholar 

  • Lakowicz, J. R., and Weber, G., 1980, Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime-resolved fluorescence anisotropies, Biophys. J. 32:591–601.

    Article  PubMed  CAS  Google Scholar 

  • McCammon, J. A., Gelin, B. R., and Karplus, M., 1977, Dynamics of folded proteins, Nature 267:585–588.

    Article  PubMed  CAS  Google Scholar 

  • McCammon, J. A., Wolynes, P. G., and Karplus, M., 1979, Picosecond dynamics of tyrosine side chains in proteins, Biochemistry 18:927–942.

    Article  PubMed  CAS  Google Scholar 

  • Miller, C., Moczydlowski, E., Latorre, R., and Phillips, M., 1985, Charybdotoxin, a protein inhibitor of single Ca2+ -activated K+ channels from mammalian skeletal muscle, Nature 313:316–318.

    Article  PubMed  CAS  Google Scholar 

  • Nigg, E. A., and Cherry, R. J., 1980, Anchorage of a band 3 population at the erythrocyte cytoplasmic membrane surface: Protein rotational diffusion measurements, Proc. Natl. Acad. Sci.USA 77:4702–4706.

    Article  PubMed  CAS  Google Scholar 

  • Noda, M., Shimizu, S., Tanabe, T., Takai, T., Kayano, T., Ideda, T., Takahashi, H., Nakayama, H., Kanaoka, Y., Minamino, N., Kanagawa, K., Matsuo, H., Raftery, M. A., Hirsoe, T., Inayama, S., Hayshida, H., Miyata, T., and Numa, S., 1984, Primary sequence of the sodium channel, Nature 312:121–125.

    Article  PubMed  CAS  Google Scholar 

  • Olivera, B. M., Gray, W. R., Zeikus, R., Mcintosh, J. M., Varga, J., Rivier, J., de Santos, V., and Cruz, L. J., 1985, Peptide neurotoxins from fish-hunting cone snails, Science 230:1338–1343.

    Article  PubMed  CAS  Google Scholar 

  • Olivera, B. M., Cruz, L. J., de Santos, V., LeCheminant, G. W., Griffin, D., Zeikus, R., Mcintosh, J. M., Galyean, R., Varga, J., Gray, W. R., and Rivier, J., 1987, Neuronal calcium channel antagonists. Discrimination between calcium channel subtypes using ω-conotoxin from Conus magus venom, Biochemistry 26:2086–2090.

    Article  PubMed  CAS  Google Scholar 

  • Peters, R., Brunger, A., and Schulten, K., 1981, Continuous fluorescence microphotolysis: A sensitive method for study of diffusion processes in single cells, Proc. Natl. Acad. Sci. USA 78:962–965.

    Article  PubMed  CAS  Google Scholar 

  • Petersen, N. S., and Elson, E. L., 1987, Fluorescence photobleach recovery, MethodsEnzymol.

    Google Scholar 

  • Poo, M. M., and Cone, R. A., 1974, Lateral diffusion of rhodopsin in the photoreceptor membrane, Nature 247:438–441.

    Article  PubMed  CAS  Google Scholar 

  • Rochat, H., Bernard, P., and Couraud, F., 1979, Scorpion toxins: Chemistry and mode of action, Adv.Cytopharmacol. 3:325–334.

    PubMed  CAS  Google Scholar 

  • Rosenberg, R. L., Tomiko, S. A., and Agnew, W. S., 1984, Single-channel properties of the reconstituted voltage-regulated Na channel isolated from the electroplax of Electrophorus eJectricus, Proc. Natl. Acad. Sci. USA 81:5594–5560.

    Article  PubMed  CAS  Google Scholar 

  • Schalow, G., and Schmidt, H., 1979, Local development of action potentials in slow muscle fibres after complete or partial denervation, J.Physiol. (London) 203:445–465.

    CAS  Google Scholar 

  • Shinitzky, M., Dianoux, A. C., Gitler, C., and Weber, G., 1971, Microviscosity and order in the hydrocarbon region of micelles and membranes determined with fluorescent probes. I. Synthetic micelles, Biochemistry 10:2106–2113.

    Article  PubMed  CAS  Google Scholar 

  • Small, R. K., Blank, M., Ghez, R., and Pfenninger, K. H., 1984, Components of the plasma membrane of growing axons. II. Diffusion of membrane protein complex, J. Cell Biol. 98:1434–1443.

    Article  PubMed  CAS  Google Scholar 

  • Stiges, M., Possani, L. D., and Bayon, A., 1986, Noxiustoxin, a short-chain toxin from the Mexican scorpion Centruroides noxius, induces transmitter release by blocking K + permeability, J. Neurosci. 6:1570–1574.

    Google Scholar 

  • Stryer, L., 1978, Fluorescence energy transfer as a spectroscopic ruler, Annu. Rev. Biochem. 47:819–846.

    Article  PubMed  CAS  Google Scholar 

  • Stya, M., and Axelrod, D. A., 1983, Diffusely distributed acetylcholine receptors can participate in cluster formation on cultured rat myotubes, Proc. Natl. Acad. Sci. USA 80:449–453.

    Article  PubMed  CAS  Google Scholar 

  • Suddath, F. L., Quigley, G. J., McPherson, A., Kim, J., Kim, S. H., and Rich, A., 1974, Three-dimensional structure of yeast phenylalanine transfer RNA at 3.0 angstroms resolution, Nature 248:20–24.

    Article  PubMed  CAS  Google Scholar 

  • Takahashi, M., Ohizumi, Y., and Yasumoto, T., 1982, Maitotoxin, a Ca + 2 channel activator candidate, J. Biol. Chem. 257:7287–7289.

    PubMed  CAS  Google Scholar 

  • Tokuyama, T., Daly, J., and Witkop, B., 1969, The structure of batrachotoxin, a steroidal alkaloid from the Colombian arrow poison frog, Phyllobates aurotaenia, and partial synthesis of batrachotoxin and its analogs and homologs, J. Am. Chem. Soc. 91:3931–3938.

    Article  PubMed  CAS  Google Scholar 

  • Triggle, D. A., Skattebol, A., Rampe, D., Josyln, A., and Gengo, P., 1986, Chemical pharmacology of Ca2+ channel ligands, in: New Insights into Cell and Membrane Transport Processes (G. Poste and S. T. Crooke, eds.), pp. 43–71, Plenum Press, New York.

    Google Scholar 

  • Tsien, R. Y., Green, D. P., Levinson, S. R., Rudy, B., and Sanders, J. K. M., 1975, A pharmacologically active derivative of tetrodotoxin, Proc. R. Soc. London Ser. B 191:555–559.

    Article  CAS  Google Scholar 

  • Vaz, W. L. C., Criado, M., Madiera, V. M. C., Schoellmann, C., and Jovin, T. M., 1982, Size dependence of the translational diffusion of large integral membrane proteins in liquidcrystalline phase lipid bilayers: A study using fluorescence recovery after photobleaching, Biochemistry 21:5608–5613.

    Article  PubMed  CAS  Google Scholar 

  • Wallace, B. G., Godfrey, E. W., Nitkin, R., Rubin, L. L., and McMahan, U. J., 1982, An extract of extracellular matrix that organizes acetylcholine receptors, in: Muscle Development (R. Pearson, ed.), pp. 469–480, CSH Press.

    Google Scholar 

  • Weber, G., 1952, Polarization of the fluorescence of macromolecules, Biochem.J. 51:145–155.

    PubMed  CAS  Google Scholar 

  • Wu, C.-W., and Stryer, L., 1972, Proximity relationships in rhodopsin, Proc. Natl. Acad. Sci. USA 69:1104–1108.

    Article  PubMed  CAS  Google Scholar 

  • Yang, C.-H., and Soll, D., 1974, Studies of transfer RNA tertiary structure of singlet-singlet energy transfer, Proc. Natl. Acad. Sci. USA 71:2838–2842.

    Article  PubMed  CAS  Google Scholar 

  • Yguerabide, J., Epstein, H.-F., and Stryer, L., 1970, Segmental flexibility in an antibody molecule, J. Mol. Biol. 51:573–590.

    Article  PubMed  CAS  Google Scholar 

  • Zukin, R. S., Hartig, P. R., and Koshland, D. E., 1977, Use of a distant reporter group as evidence for a conformational change in a sensory receptor, Proc. Natl. Acad. Sci. USA 74:1932–1936.

    Article  CAS  Google Scholar 

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© 1988 Plenum Press, New York

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Angelides, K.J. (1988). Fluorescence Spectroscopy to Probe the Structure and Cellular Dynamics of Ion Channels. In: Narahashi, T. (eds) Ion Channels. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7302-9_1

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  • DOI: https://doi.org/10.1007/978-1-4615-7302-9_1

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