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