Amplitude, kinetics, and reversibility of a light-induced decrease in guanosine 3',5'-cyclic monophosphate in frog photoreceptor membranes
نویسندگان
چکیده
The concentration of guanosine 3',5'-cyclic monophosphate (cyclic GMP) has been examined in suspensions of freshly isolated frog rod outer segments using conditions which previously have been shown to maintain the ability of outer segments to perform a light-induced permeability change (presence of calf serum, anti-oxidant, and low calcium concentration). Illumination causes a rapid decrease in cyclic GMP levels which has a half-time approximately 125 ms. With light exposures that bleach less than 100 rhodopsin molecules in each rod outer segment, at least 10(4)-10(5) molecules of cyclic GMP are hydrolyzed for each rhodopsin molecule bleached. Half of the total cyclic GMP in each outer segment, approximately 2 X 10(7) molecules, is contained in the light-sensitive pool. If outer segments are exposed to continuous illumination, using intensities which bleach between 5.0 X 10(1) and 5.0 X 10(4) rhodopsin molecules/outer segment per second, cyclic GMP levels fall to a value characteristic for the intensity used. This suggests that a balance between synthesis and degradation of cyclic GMP is established. This constant level appears to be regulated by the rate of bleaching rhodopsin molecules (by the intensity of illumination), not the absolute number of rhodopsin molecules bleached...
منابع مشابه
Amplitude, Kinetics, and Reversibility of a Light-Induced Decrease in Guanosine 3',5'-Cyclic Monophosphate in Frog Photoreceptor Membranes
I N T R O D U C T I O N I n v e r t e b r a t e r o d p h o t o r e c e p t o r s b i o c h e m i c a l m a c h i n e r y f o r exc i t a t i on a n d a d a p t a t i o n is c o n t a i n e d w i th in t he o u t e r s e g m e n t , a c y l i n d r i c a l o r g a n e l l e w h i c h J. GEN. PHYSIOL. ~) The Rockefeller University Press 00"22-1295/79/05/062912551.00 629 Volume 73 May 1979 629-65...
متن کاملControl of the cyclic GMP phosphodiesterase of frog photoreceptor membranes
The light-activated cyclic GMP phosphodiesterase (PDE) of frog photoreceptor membranes has been assayed in isolated outer segments suspended in a low-calcium Ringer's solution. Activation occurs over a range of light intensity that also causes a decrease in the permeability, cyclic GMP levels, and GTP levels of isolated outer segments. At intermediate intensities, PDE activity assumes constant ...
متن کاملLight adaption of the cyclic GMP phosphodiesterase of frog photoreceptor membranes mediated by ATP and calcium ions
The light-activated guanosine 3',5'-cyclic monophosphate (cyclic GMP) phosphodiesterase (PDE) of frog photoreceptor membranes has been assayed by measuring the evolution of protons that accompanies cyclic GMP hydrolysis. The validity of this assay has been confirmed by comparison with an isotope assay used in previous studies (Robinson et al. 1980. J. Gen. Physiol. 76: 631-645). The PDE activit...
متن کاملBiochemical correlates of adaptation processes in isolated frog photoreceptor membranes
Frog rod outer segments isolated in suspension can maintain much of their in vivo activity. This observation provides us with a simpler system than the intact retina for correlating biochemical and physiological changes. The relevant physiological process, a decrease of sodium permeability by illumination, is assayed as light suppression of outer segment swelling in a modified Ringer's solution...
متن کاملGuanosine 3',5'-cyclic monophosphate and the in vitro physiology of frog photoreceptor membranes
Frog rod outer segments freshly detached from dark-adapted retinas contain approximately 1-2 molecules of guanosine 3',5'-cyclic monophosphate (cyclic GMP) for every 100 molecules of visual pigment present. This cyclic GMP decays to 5'-GMP, and the conversion is accelerated upon illumination of the outer segments. Bleaching one rhodopsin molecule can lead to the hydrolysis of 1,000-2,000 molecu...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Journal of General Physiology
دوره 73 شماره
صفحات -
تاریخ انتشار 1979