Abstract
The initial and only light-activated step in vision is the photoisomerization of the ligand of the visual pigment,11-cis retinal to all-trans retinal, which occurs while being covalently bound to a lysine deep in the membrane region of the visual pigment. This event leads to the activation of the g-protein, transducin, which in turn activates c-gmp phosphodiesterase causing the destruction of c-gmp, the closure of cation channels in the plasma membrane of the photoreceptor, and eventually to the reduction in release of synaptic transmitter to other retinal neurons in the visual pathway. However, the visual pigment containing retinal in its all-trans form is now incapable of absorbing photons in the visual region of the spectrum and can no longer activate the transduction cascade. In order to do so, it must be regenerated into a form that contains 1 1-cis retinal. The biochemical reactions by which this occurs are collectively called the visual cycle. This complex series of reactions is initiated in the photoreceptors themselves, by the reduction of all-trans retinal to all-trans retinol by all-trans retinol dehydrogenase (rdh) and the cofactor nadph. All the subsequent steps in the regeneration of 11-cis retinal take place in the retinal pigment epithelium. Regenerated 11-cis retinal is then transported from the retinal pigment epithelium through the extracellular matrix back to the photoreceptor cells where it condenses with opsin to reform visual pigment.
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References
Alpern, M., Rushton, W. A. and Torii, S., 1970, The attenuation of rod signals by bleachings. J. Physiol. 207(2):449-61.
Blaner, W. S. and Churchich, J. E., 1980, The membrane bound retinol dehydrogenase from bovine rod outer segments. Biochem. Biophys. Res. Commun. 94(3):820-6.
Boll, F., 1877, Zur anatomie und physiologie der retina. Arch. Anat. Physiol 4-36. [Translation: 1977, On the anatomy and physiology of the retina. Vis. Res. 17(11-12):1249-65].
Cohen, G. B., Oprian, D. D., and Robinson, P. R., 1992, Mechanism of activation and inactivation of opsin: Role of GIul l3 and Lys296. Biochemistry. 31(50):12592-601.
Denton, E. J., 1959, The contributions of the oriented photosensitive and other molecules to the absorption of the whole retina. Proc. R. Soc. (Lond.) Series B. 150:78-94.
Fain, G. L., Matthews, H. R., and Cornwall, M. C., 1996, Dark adaptation in vertebrate photoreceptors. Trends Neurosci. 19(11):502-7.
Fukada Y., and Yoshizawa, T., 1981, Activation of phosphodiesterase in frog rod outer segment by an intermediate of rhodopsin photolysis. II. Biochim. Biophys. Acta. 675(2):195-200.
Futterman, S., 1963, Metabolism of the retina. J. Biol. Chem. 238:1145-50.
Futterman, S., Hendrickson, A., Bishop, P. E., Rollins, M. H., and Vacano, E., 1970, Metabolism of glucose and reduction of retinaldehyde in retinal photoreceptors. J. Neurochem. 17(2):149-56.
Haeseleer, F., Huang, J., Lebioda, L., Saari, J. C., and Palczewski, K., 1998, Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal. J. Biol. Chem. 273(34):21790-9.
Harosi, F. I., and MacNichol Jr. E. F., 1974, Dichroic microspectrophotometer: A computer-assisted, rapid, wavelength-scanning photometer for measuring linear dichroism in single cells. J. Opt. Soc. Am. 64(7):903-18.
Hofmann, K. P., Pulvermuller, A., Buczylko, J., Van Hooser, P., and Paczewski, K., 1992, The role of arrestin and retinoids in the regeneration pathway of rhodopsin. J. Biol. Chem. 267(22):15701-6.
Hsu, S. C., and Molday, R. S., 1991, Glycolytic enzymes and a GLUT-1 glucose transporter in the outer segments of rod and cone photoreceptor cells. J. Biol. Chem. 266(32):21745-52.
Hsu, S. C., and Molday, R. S., 1994, Glucose metabolism in photoreceptor outer segments. Its role in phototransduction and in NADPH-requiring reactions. J. Biol. Chem. 269(27):17954-9.
Ishiguro, S., Suzuki, Y., Tamai, M., and Mizuno, K., 1991, Purification of retinol dehydrogenase from bovine retinal rod outer segments. J. Biol. Chem. 266(23):15520-4.
Jager, S., Palczewski, K., and Hofmann, K. P., 1996, Opsin/all-trans-retinal complex activates transducin by different mechanisms than photolyzed rhodopsin. Biochemistry. 35(9):2901-8.
Jin, J., Crouch, R. K., Corson, D. W., Katz, B. M., MacNichol, E. F., and Cornwall, M. C., 1993, Noncovalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones. Neuron. 11(3):513-22.
Kaplan, M. W., Liebman, P. A., 1977, Slow bleach-induced birefringence changes in rod outer segments. J. Physiol. 265(3):657-72.
Kaplan, M. W., 1985, Distribution and axial diffusion of retinol in bleached rod outer segments of frogs (Rana pipiens). Exp. Eye Res. 40(5):721.9.
Kefalov, V. J., Crouch, R. K., and Cornwall, M. C., 2001, Role of nncovalent binding of 11-cis-retinal to opsin in dark adaptation of rod and cone photoreceptors. Neuron. 29(3):749-55.
Kemp, C. M., 1973, Dichroism in rods during bleaching, In: Langer, H., editor, Biochemistry and Physiology of Visual Pigments. Berlin: Springer-Verlag. p. 307-12.
Kuhne W., 1879, Chemische vorgange in der netzhaut, (ed. Hermann, L.) Vol. 3 [Translation: Hubbard, R., Wald, G., 1977, Chemical processes in the retina. Vis. Res. 17(11-12):1269-316].
Lamb, T. D., 1980, Spontaneous quantal events induced in toad rods by pigment bleaching. Nature. 287(5780):349-51.
Li, X. B., Szerencsei, R. T., and Schnetkamp, P. P., 1994, The glucose transporter in the plasma membrane of the outer segments of bovine retinal rods. Exp. Eye Res. 59(3):351-8.
Liebman, P. A., 1969, Microspectrophotometry of retinal cells. Ann. N. Y. Acad. Sci. 157:250-64.
Lopez-Escalera, R., Li, X. B., and Szerencsei, P. P., 1991, Glycolysis and glucose uptake in intact outer segments isolated from bovine retinal rods. Biochemistry. 30(37):8970-6.
McConnell, D. G., Ozga, G. W., and Solze, D. A., 1969, Evidence for glycolysis in bovine retinal microsomes and photoreceptor outer segments. Biochim. Biophys. Acta. 184(1):11-28.
Melia Jr., T. J., Cowan, C. W., Angleson, J. K., and Wensel, T. G., 1997, A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. Biophys. J. 73(6): 3182-91.
Nicotra, C., and Livrea, M. A., 1982, Retinol dehydrogenase from bovine retinal rod outer segments. Kinetic mechanism of the solubilized enzyme. J Biol. Chem. 257(19):11836-41.
Palczewski, K., Jager, S., Buczylko, J., Crouch, R. K., Bredberg, D. L., Hofmann, K. P., Asson-Batres, M. A., and Saari, J. C., 1994, Rod outer segment retinol dehydrogenase: Substrate specificity and role in phototransduction. Biochemistry. 33(46):13741-50.
Paupoo, A. A., Mahroo, O. A., Friedburg, C., and Lamb, T. D., 2000, Human cone photoreceptor responses measured by the electroretinogram a-wave during and after exposure to intense illumination. J. Physiol. 529(Pt2):469-82.
Rattner, A., Smallwood, P. M., and Nathans, J., 2000, Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol. J. Biol. Chem. 275(15):11034-43.
Saari, J. C., Garwin, G. G., Van Hooser, J. P., and Palczewski K., 1998, Reduction of all-trans-retinal limits regeneration of visual pigment in mice. Vis. Res. 38(10):1325-33.
Sakmar, T. P., Franke, R. R., and Khorana, H. G., 1989, Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc. Nat. Acad. Sci. U. S. A. 86(21):8309-13.
Schnetkamp, P. P., and Daemen, F. J., 1981, Transfer of high-energy phosphate in bovine rod outer segments. A nucleotide buffer system. Biochim. Biophys. Acta. 672(3):307-12.
Sears, R. C., and Kaplan, M. W., 1989, Axial diffusion of retinol in isolated frog rod outer segments following substantial bleaches of visual pigment. Vis. Res. 29(11):1485-92.
Surya, A., Foster, K. W., and Knox, B. E., 1995, Transducin activation by the bovine opsin apoprotein. J. Biot. Chem. 270(10): 5024-31.
Thomas, M. M., and Lamb, T. D., 1999, Light adaptation and dark adaptation of human rod photoreceptors measured from the a-wave of the electroretinogram. J. Physiol. 518(PÃ2): 479-96.
Wald, G., 1935, Carotenoids and the visual cycle. J. Gen. PhysioL 19(2):351-71.
Wallimann, T., Wegmann, G., Moser, H., Huber, R., and Eppenberger, H. M., 1986, High content of creatine kinase in chicken retina: Compartmentalized localization of creatine kinase isoenzymes in photoreceptor cells. Proc. Nat. Acad. Sci. U. S. A. 83(11):3816-9.
Zimmerman, W. F., Yost, M. T., and Daemen, F. J., 1974, Dynamics and function of vitamin A compounds in rat retina after a small bleach of rhodopsin. Nature. 250(461):66-7.
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Cornwall, M.C., Tsina, E., Crouch, R.K., Wiggert, B., Chen, C., Koutalos, Y. (2003). Regulation of the Visual Cycle: Retinol Dehydrogenase and Retinol Fluorescence Measurements In Vertebrate Retina. In: LaVail, M.M., Hollyfield, J.G., Anderson, R.E. (eds) Retinal Degenerations. Advances in Experimental Medicine and Biology, vol 533. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0067-4_45
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DOI: https://doi.org/10.1007/978-1-4615-0067-4_45
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