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Physiol. Rev. 81: 117-151, 2001;
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Physiological Reviews, Vol. 81, No. 1, January 2001, pp. 117-151
Copyright ©2001 by the American Physiological Society

Adaptation in Vertebrate Photoreceptors

Gordon L. Fain, Hugh R. Matthews, M. Carter Cornwall, and Yiannis Koutalos

Departments of Physiological Science and Ophthalmology, University of California, Los Angeles, California; Physiological Laboratory, University of Cambridge, Cambridge, United Kingdom; Department of Physiology, Boston University School of Medicine, Boston, Massachusetts; and Department of Physiology and Biophysics, University of Colorado School of Medicine, Denver, Colorado

Fain, Gordon L., Hugh R. Matthews, M. Carter Cornwall, and Yiannis Koutalos. Adaptation in Vertebrate Photoreceptors. Physiol. Rev. 81: 117-151, 2001.When light is absorbed within the outer segment of a vertebrate photoreceptor, the conformation of the photopigment rhodopsin is altered to produce an activated photoproduct called metarhodopsin II or Rh*. Rh* initiates a transduction cascade similar to that for metabotropic synaptic receptors and many hormones; the Rh* activates a heterotrimeric G protein, which in turn stimulates an effector enzyme, a cyclic nucleotide phosphodiesterase. The phosphodiesterase then hydrolyzes cGMP, and the decrease in the concentration of free cGMP reduces the probability of opening of channels in the outer segment plasma membrane, producing the electrical response of the cell. Photoreceptor transduction can be modulated by changes in the mean light level. This process, called light adaptation (or background adaptation), maintains the working range of the transduction cascade within a physiologically useful region of light intensities. There is increasing evidence that the second messenger responsible for the modulation of the transduction cascade during background adaptation is primarily, if not exclusively, Ca2+, whose intracellular free concentration is decreased by illumination. The change in free Ca2+ is believed to have a variety of effects on the transduction mechanism, including modulation of the rate of the guanylyl cyclase and rhodopsin kinase, alteration of the gain of the transduction cascade, and regulation of the affinity of the outer segment channels for cGMP. The sensitivity of the photoreceptor is also reduced by previous exposure to light bright enough to bleach a substantial fraction of the photopigment in the outer segment. This form of desensitization, called bleaching adaptation (the recovery from which is known as dark adaptation), seems largely to be due to an activation of the transduction cascade by some form of bleached pigment. The bleached pigment appears to activate the G protein transducin directly, although with a gain less than Rh*. The resulting decrease in intracellular Ca2+ then modulates the transduction cascade, by a mechanism very similar to the one responsible for altering sensitivity during background adaptation.




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