Abstract
The purpose of photoreceptors is the conversion of light into an electrical signal that controls the release of transmitter (glutamate) and thereby initiates a chain of physiological responses in other retinal neurons. The first step in the transduction cascade is the absorption of a photon by rhodopsin. Rhodopsin is mainly located in the plasma membrane of disks in the outer segment and consists of the chromophore 11-cis-retinal linked to the heptahelical protein opsin via a Schiff base to a lysin. Absorption of a photon isomerizes retinal to the all-trans-conformation and converts rhodopsin to metarhodopsin II. Metarhodopsin II activates a cGMP-cleaving phosphodiesterase (PDE) via a specific G-protein (transducin). As a result of these enzymatic reactions the intracellular cGMP concentration is lowered and cGMP dissociates from the binding sites of the cGMP-dependent channels in the plasma membrane of the outer segment. The cGMP-dependent kation channels are open when the cGMP concentration in the photoreceptor is high in darkness. The channels close when the cGMP-level is lowered upon illumination and the inward current driven by a sodium-potassium pump in the inner segment is stopped. Interruption of this inward current, which is carried by sodium and calcium ions hyperpolarizes the membrane.
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References
H. Kühn, Light-regulated binding of rhodopsin kinase and other proteins to cattle bovine photoreceptor membranes, Biochem. 17: 4389–4395 (1978).
H. Kühn, Light-and GTP-regulated interaction of GTP-ase and other proteins with bovine photoreceptor membranes, Nature 283: 587–589 (1980).
L. Lagnado and D. Baylor, Signal flow in visual transduction, Neuron 8: 995–1002 (1992).
E.N.Jr. Pugh and T.D. Lamb, Amplification and kinetics of the activation steps in phototransduction,Biochim. Biophys. Acta 1141: 111–149 (1993).
Y. Koutalos and K.W. Yau, A rich complexity emerges in phototransduction, Curr. Opin. Neurobiol. 3:513–519(1993)
K.-W. Koch and L. Stryer, Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions, Nature 334: 64–66 (1988).
Y. Horio and F. Murad, Solubilization of guanylyl cyclase from bovine rod outer segments and effects of lowering Ca2+ and nitro compounds, J. Biol. Chem. 266: 3411–3415 (1991).
H.-G. Lambrecht and K.-W. Koch, Phosphorylation of recoverin, the calcium-sensitive activator of photoreceptor guanylyl cyclase, FEBS Letters 294: 207–209 (1991).
H.-G. Lambrecht and K.-W. Koch, A 26 kD calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase. EMBO J. 10: 793–798 (1991).
L.W. Haynes, A.R. Kay, and K.W. Yau, Single cyclic GMP-activated channel activity in excised patches of rod outer segment membrane, Nature 321: 66–70 (1986).
A. Zimmerman and D.A. Baylor, Cyclic GMP-sensitive conductance of retinal rods consists of aqueous pores, Nature 321: 70–72 (1986).
Y.T. Hsu and R.S. Molday, Modulation of the cGMP-gated channel of rod photoreceptor cells by calmodulin, Nature 361: 76–79 (1993).
S. Kawamura, Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin. Nature 362: 855–857 (1993).
U.B. Kaupp and K.-W. Koch, Role of cGMP and Ca2+ in vertebrate photoreceptor excitation and adaptation, Ann. Rev. Physiol. 54: 153–175 (1992).
V.J. Coccia and R.H. Cote, Regulation of intracellular cyclic GMP concentration by light and calcium in electropermeabilized rod photoreceptors, J. Gen. Physiol. 103: 67–86 (1994).
A. Margulis, R.K. Sharma, and A. Sitaramayya, Nitroprusside-sensitive and insensitive guanylate cyclases in retinal rod outer segments, Biochem. Biophys. Res. Comm. 185: 909–914 (1992).
CM. Venturini, R.G. Knowles, R.M.J. Palmer, and S. Moncada, Synthesis of nitric oxide in the bovine retina, Biochem. Biophys. Res. Comm. 180: 920–925 (1991).
E.E. Fesenko, S.S. Kolesnikov, and A.L. Lyubarski, Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segment, Nature 313: 310–313 (1985).
K.-F. Schmidt, G.N. Noll, and C. Baumann, Effect of guanine nucleotides on the dark voltage of single frog rods, Visual Neurosci. 2: 101–108 (1989).
C.R. Bader, D. Bertrand, and E.A. Schwartz, Voltage activated and calcium-activated currents studied in solitary rod inner segments from the salamander retina, J. Physiol. 331: 253–284 (1982).
M. Pusch and E. Neher, Rates of diffusional exchange between small cells and a measuring patch pipette, Pflügers Arch., 411: 204–211 (1988).
K.-F. Schmidt, G.N. Noll, P. Jacobi, and C. Baumann, Configuration of light responses in isolated retinal rods. A patch-clamp study, Graefe’s Arch. Clin. Exp. Ophthalmol. 232: 153–161 (1994).
K.-F. Schmidt, G.N. Noll, and Y. Yamamoto, Sodium Nitroprusside alters dark voltage and light responses on isolated retinal rods during whole-cell recording, Visual Neurosci. 9: 205–209 (1992).
Y. Tsuyama, G.N. Noll, and K.-F. Schmidt, L-Arginine and nicotinamide adenine dinucleotide phosphate alter dark voltage and accelerate light response recovery in isolated retinal rods of the frog (Rana temporaria), Neurosci. Letters 149: 95–98 (1993).
A. Ames, T.F. Walseth, R.A. Heyman, M. Barad, R.M. Graeff, and N.D. Goldberg, Light-induced increases in cGMP metabolic flux correspondend with electrical responses of photoreceptors, J. Biol. Chem. 261: 13034–13042(1986).
S.M. Dawis, R.M. Graeff, R.A. Heyman, T.F. Walseth, and N.D. Goldberg, Regulation of cyclic GMP metabolism in toad photoreceptors, J. Biol. Chem. 263: 8771–8785 (1988).
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Schmidt, KF., Nöll, G.N. (1995). Nitric Oxide in Amphibian Photoreceptors. In: Weissman, B.A., Allon, N., Shapira, S. (eds) Biochemical, Pharmacological, and Clinical Aspects of Nitric Oxide. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1903-4_11
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DOI: https://doi.org/10.1007/978-1-4615-1903-4_11
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