Cyclic GMP stimulation of a light-activated ATPase in rod outer segments
- 1 August 1983
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 304 (5928), 733-735
- https://doi.org/10.1038/304733a0
Abstract
Rod outer segments (ROSs) of vertebrate photoreceptor cells have been reported to contain several enzyme systems including a dark, Ca2+-stimulated ATPase1, a rhodopsin kinase2,3, a phosphodiesterase4,5 and a GTPase6,7, all of which are light-stimulated. Recently, Thacher has found a light-stimulated Mg2+-ATPase in frog ROSs8,9 while our own laboratory has identified a dark, Ca2+-inhibited Mg2+-ATPase in bovine ROSs10–12. Here we extend our observations on the Mg2+-ATPase and demonstrate that flash illumination following the dark ATPase process stimulated ATPase activity at a rate considerably faster than the dark process. In addition, we find that both the dark and light stimulated ATPase activities are markedly enhanced by cyclic GMP and inhibited by Ca2+.Keywords
This publication has 11 references indexed in Scilit:
- Evidence for structural changes in the photoreceptor disk membrane, enabled by magnesium ATPase activity and triggered by lightFEBS Letters, 1979
- Guanylate cyclase of isolated bovine retinal rod axonemesBiochemistry, 1979
- EVIDENCE FOR A MAGNESIUM DEPENDENT ATPase IN BOVINE ROD OUTER SEGMENT DISK MEMBRANES*†Photochemistry and Photobiology, 1979
- A light-activated GTPase in vertebrate photoreceptors: Regulation of light-activated cyclic GMP phosphodiesteraseProceedings of the National Academy of Sciences, 1977
- Ca2+-dependent ATPase activity of bovine receptor cell outer segmentNature, 1977
- The rate of rhodopsin phosphorylation in isolated retinas of frog and cattleBiochimica et Biophysica Acta (BBA) - General Subjects, 1976
- Link between rhodopsin and disk membrane cyclic nucleotide phosphodiesterase. Action spectrum and sensitivity to illuminationBiochemistry, 1975
- Phosphorylation of Frog Photoreceptor Membranes induced by LightNature New Biology, 1972
- Light dependent phosphorylation of rhodopsin by ATPFEBS Letters, 1972
- Adenylyl imidiodiphosphate, an adenosine triphosphate analog containing a P-N-P linkageBiochemistry, 1971