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Differences in the pharmacological activation of visual opsins

Published online by Cambridge University Press:  30 January 2007

T. ISAYAMA ,
Y. CHEN ,
M. KONO ,
W.J. DEGRIP ,
J.-X. MA ,
R.K. CROUCH  and
C.L. MAKINO
T. ISAYAMA
Affiliation:
Department of Ophthalmology, Massachusetts Eye & Ear Infirmary, Harvard Medical School, Boston, Massachusetts
Y. CHEN
Affiliation:
Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma
M. KONO
Affiliation:
Department of Ophthalmology, Storm Eye Research Institute, Medical University of South Carolina, Charleston, South Carolina
W.J. DEGRIP
Affiliation:
Department of Biochemistry, NCMLS, University of Nijmegen, Nijmegen, The Netherlands
J.-X. MA
Affiliation:
Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma
R.K. CROUCH
Affiliation:
Department of Ophthalmology, Storm Eye Research Institute, Medical University of South Carolina, Charleston, South Carolina
C.L. MAKINO
Affiliation:
Department of Ophthalmology, Massachusetts Eye & Ear Infirmary, Harvard Medical School, Boston, Massachusetts
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Abstract

Opsins, like many other G-protein-coupled receptors, sustain constitutive activity in the absence of ligand. In partially bleached rods and cones, opsin's activity closes cGMP-gated channels and produces a state of “pigment adaptation” with reduced sensitivity to light and accelerated flash response kinetics. The truncated retinal analogue, β-ionone, further desensitizes partially bleached green-sensitive salamander rods, but enables partially bleached red-sensitive cones to recover dark-adapted physiology. Structural differences between rod and cone opsins were proposed to explain the effect. Rods and cones, however, also contain different transducins, raising the possibility that G-protein type determines the photoreceptor-specific effects of β-ionone. To test the two hypotheses, we applied β-ionone to partially bleached blue-sensitive rods and cones of salamander, two cells that couple the same cone-like opsin to either rod or cone transducin, respectively. Immunocytochemistry confirmed that all salamander rods contain one form of transducin, whereas all cones contain another. β-Ionone enhanced pigment adaptation in blue-sensitive rods, but it also did so in blue- and UV-sensitive cones. Furthermore, all recombinant salamander rod and cone opsins, with the exception of the red-sensitive cone opsin, activated rod transducin upon the addition of β-ionone. Thus opsin structure determines the identity of β-ionone as an agonist or an inverse agonist and in that respect distinguishes the red-sensitive cone opsin from all others.

Keywords

RodConeRhodopsinTransducinPhototransduction
Type
Research Article
Information
Visual Neuroscience , Volume 23 , Issue 6 , November 2006 , pp. 899 - 908
Copyright
© 2006 Cambridge University Press

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