Excitation of Limulus Photoreceptors by Hydrolysis-Resistant Analogs of cGMP and cAMP

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Abstract

cGMP was proposed to be the agent which directly opens the light-sensitive channel in Limulus ventral photoreceptors. However, the light-sensitive rhabdomeral-lobe (R-lobe) is not uniformly responsive to cGMP injection; that is, there are ‘hot spots’ of sensitivity. A potent phosphodiesterase which rapidly hydrolyses cGMP was suggested to explain the existence of these ‘hot spots’. To test this idea we injected ventral photoreceptors with hydrolysis-resistant cyclic nucleotide analogues. Whereas there can be a lack of a response to cGMP injection into the R-lobe, we find a reproducible depolarization upon R-lobe injection of hydrolysis-resistant cGMP analogues. Furthermore, the depolarization resulting from the injection of cGMP analogues does not require a rise in intracellular Ca 2+ , as it is not blocked by the Ca 2+ buffer, BAPTA. Surprisingly, R-lobe injection of a hydrolysis-resistant cAMP analogue also depolarized ventral photoreceptors. Further work will be needed to resolve the role of cGMP in Limulus visual transduction.

Original languageAmerican English
Pages (from-to)291-294
JournalBrain Research
Volume552
Issue number2
DOIs
StatePublished - Jun 28 1991
Externally publishedYes

Keywords

  • Cyclic adenosine 5′-phosphate
  • Cyclic guanosine 5′-phosphate
  • Limulus polyphemus
  • Photoreceptor

Disciplines

  • Marine Biology
  • Oceanography and Atmospheric Sciences and Meteorology

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