The Sensitivity Shift Due to Light Adaptation Depending on the Extracellular Calcium Ion Concentration in Limulus Ventral Nerve Photoreceptor

1984 ◽  
Vol 39 (6) ◽  
pp. 662-679 ◽  
Author(s):  
H. Stieve ◽  
M. Bruns ◽  
H. Gaube

Receptor potentials of Limulus ventral photoreceptors were recorded in two defined states of moderate light- and considerable dark adaptation (LA, DA) by a repeated stimulus sequence consisting of a conditioning 2 s illumination (white light, response saturating intensity) followed by two 10 ms test flashes at fixed intervals evoking LA and DA responses (intensity varied from threshold to saturation of response amplitude). The half saturating intensity I50 was determined from response height vs log stimulus intensity curves for LA and DA, while the photoreceptor was superfused either by reference saline (physiological ion concentrations, including 10 mmol/l Ca2+) or by test salines in which the [Ca2+] was varied between 40 μmol/l and 100 mmol/l. The sensitivity of the dark-adapted receptor does not significantly depend on the [Ca2+]ex, but the sensitivity shift due to LA (measured by /50) is reduced when the [Ca2+]ex is lowered, and augmented when the [Ca2+]ex is increased. Additional reduction of the [Na2+]ex from 463 mmol/l to 46 mmol/l or increase of the [Mg2+]ex from 50 mmol/l to 100 mmol/l does not counteract the effect of lowered [Ca2+]ex on LA. The results confirm the assumption that a transient increase of the intracellular [Ca2+] supplied from extracellular sources during the light response is the main cause for LA This calcium effect on light adaptation is neither characterized by a calcium/sodium antagonism, nor mimicked by magnesium, in contrast to the calcium effect on the gating of the light-activated ion channels.

1974 ◽  
Vol 52 (11) ◽  
pp. 981-990 ◽  
Author(s):  
Gerrit Voordouw ◽  
G. Maurice Gaucher ◽  
Rodney S. Roche

The physicochemical properties of the extracellular protease of the fungus Malbranchea pulchella, for which we have adopted the name thermomycolase, were investigated. The molecular weight of diisopropylphosphorylthermomycolase was found to be 32 000–33 000 by sedimentation equilibrium and sodium dodecyl sulfate (SDS) gel electrophoresis. Its sedimentation coefficient (s020, w = 2.97 S), intrinsic viscosity ([η] = 3.0 cc/g), and frictional ratio (f/f0 = 1.09) characterize the enzyme as a typical globular protein. The circular dichroism spectrum of the protein is also consistent with its globular structure. Active thermomycolase autolyzes extensively, especially at low calcium ion concentrations, producing low molecular weight peptide material. In the presence of SDS, a different autolytic degradation is observed, resulting in much higher molecular weight polypeptide products (16 500, 12 500,11 000, 8 500). The results indicate that, in the presence of SDS, thermomycolase has three sites that are highly susceptible to autolysis. At calcium ion concentrations of 10−3 M and 10−2 M the enzyme undergoes a sharp thermal denaturation with transition temperatures at 69 °C and 75 °C, respectively, and with complete loss of enzyme activity. At 70 °C the enzyme appeared to be maximally thermostable at a calcium ion concentration of 10−2 M.


Blood ◽  
1983 ◽  
Vol 61 (1) ◽  
pp. 180-185
Author(s):  
LT Friedhoff ◽  
M Sonenberg

The membrane potential of the human platelet was investigated using the membrane potential probes 3,3′-dipropyl-2,2′-thiadicarbocyanine iodide and tritiated triphenylmethylphosphonium bromide. The membrane potential in physiologic buffer was estimated to be 52–60 mV inside negative. The membrane was depolarized when extracellular potassium or hydrogen ion concentrations were increased. Changes in extracellular sodium, chloride, or calcium ion concentration had no measurable effect on membrane potential. Elevated extracellular potassium has been shown to increase platelet sensitivity to the aggregating agent, adenosine diphosphate. Our results show that changes in extracellular ion concentrations that depolarize platelets increase platelet sensitivity to aggregating agents. These results suggest that membrane potential changes may play a role in modulating the response of platelets to aggregating agents.


Blood ◽  
1983 ◽  
Vol 61 (1) ◽  
pp. 180-185 ◽  
Author(s):  
LT Friedhoff ◽  
M Sonenberg

Abstract The membrane potential of the human platelet was investigated using the membrane potential probes 3,3′-dipropyl-2,2′-thiadicarbocyanine iodide and tritiated triphenylmethylphosphonium bromide. The membrane potential in physiologic buffer was estimated to be 52–60 mV inside negative. The membrane was depolarized when extracellular potassium or hydrogen ion concentrations were increased. Changes in extracellular sodium, chloride, or calcium ion concentration had no measurable effect on membrane potential. Elevated extracellular potassium has been shown to increase platelet sensitivity to the aggregating agent, adenosine diphosphate. Our results show that changes in extracellular ion concentrations that depolarize platelets increase platelet sensitivity to aggregating agents. These results suggest that membrane potential changes may play a role in modulating the response of platelets to aggregating agents.


1992 ◽  
Vol 12 (2) ◽  
pp. 306-310 ◽  
Author(s):  
Kenji Hashimoto ◽  
Haruhiko Kikuchi ◽  
Masatsune Ishikawa ◽  
Shuichi Kobayashi

To investigate regional changes in calcium ion concentrations, we developed a new histochemical method using aequorin, a calcium ion-sensitive photoprotein. In this method, reagent film containing aequorin was made and an unfixed slice of frozen brain 16 μm thick was placed on it. Tissue calcium ions permeated the reagent layer and the bioluminescence of aequorin-calcium ions was recorded photographically with high spatial resolution. There was a close linear relationship ( r = 0.903) between the optical density of the bioluminescent images and the logarithmic values of the tissue calcium ion concentration. Using this method, we could visualize the regional tissue calcium ion distribution in pathological states in rat brains.


SIMULATION ◽  
1979 ◽  
Vol 32 (6) ◽  
pp. 193-204 ◽  
Author(s):  
George G. Járos ◽  
Thomas G. Coleman ◽  
Arthur C. Guyton

2008 ◽  
Vol 8 (3) ◽  
pp. 178-183 ◽  
Author(s):  
Sumio Watanabe ◽  
Masahiro Tomono ◽  
Makoto Takeuchi ◽  
Tsuneo Kitamura ◽  
Miyoko Hirose ◽  
...  

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