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PubMed1981

Specific photoisomerization of retinal in squid rhodopsin and metarhodopsin.

The composition of retinal isomers in the photosteady-state mixtures formed from squid rhodopsin and metarhodopsin was determined by high-pressure liquid chromatography. A large amount of 9-cis-retinal was obtained at liquid N2 temperature when rhodopsin was irradiated with orange light, but only small quantities of 9-cis-retinal were obtained at 15 degrees C. Scarcely any 9-cis-retinal was produced from metarhodopsin by irradiation at liquid N2 temperature. A large quantity of 7-cis-retinal was found in the photoproduct of rhodopsin irradiated at solid carbon dioxide temperature, but not at 15 degrees C and liquid N2 temperature. 7-cis-Retinal was not produced from metarhodopsin at any temperatures. These results indicate that the photoisomerization of retinal is regulated by the structure of the retinal-binding site of this protein. The formation of 9-cis- and 7-cis-retinals is forbidden in the metarhodopsin protein.

Animals↗
PubMed1984

Formation of hypsorhodopsin at room temperature by picosecond green pulse.

Excitation of squid rhodopsin with a single laser pulse (532 nm, 25 ps) at 18 degrees C yielded photorhodopsin, a precursor of bathorhodopsin. In the linear region, no relation between amount of photorhodopsin and excitation-energy hypsorhodopsin was detected, while in a photon saturation region this was observed. The time constant of hypsorhodopsin to bathorhodopsin decay was about 125 ps. Dependencies of formation of photorhodopsin and hypsorhodopsin on the excitation energy suggest that hypsorhodopsins of squid and octopus are formed by a two-photon reaction. No cattle hypsorhodopsin was detected in our experimental conditions.

Animals↗
PubMed1975

Light scattering spectroscopy of the squid axon membrane.

Light scattering studies on the giant squid axon were done using the technique of optical mixing spectroscopy. This experimental approach is based on the use of laser light to detect the fluctuations of membrane macromolecules which are associated with conductance fluctuations. The light scattering spectra were similar to the Lorentzian-like behavior of conductance fluctuations, possibly reflecting an underlying conformational change in the specific membrane sites responsible for the potassium ion conductance. The amplitude of the spectra measured, increased when the membrane was depolarized and decreased on hyperpolarization. The spectra were fit to the sum of two terms, a (1/f component and a simple Lorentzian term. Spectra from deteriorating axons did not show sensitivity to membrane potential changes. It is shown theoretically that fluctuations due to the voltage-dependent variable, n, of the Hodgkin-Huxley formalism are identical to the voltage fluctuations. The derived power spectrum is that of a second order system, capable of showing resonance peaking only if the voltage dependence of the potassium rate of constants is included in the analysis. The lack of resonance peaking in the observed light scattering spectra, indicates that the data are best described by a damped second order system.

Animals↗
PubMed1975

Electrical properties of squid axon membrane. II. Effect of partial degradation by phospholipase A and pronase on electrical characteristics.

Passive electrical characteristics of perfused squid axon membrane are investigated. In a previous publication, we reported that the capacitance of intact squid axon membrane is partly frequency dependent. We extended the same measurement to perfused axons. We found that the electrical characteristics of perfused axon membrane are essentially the same as those of intact axons. In this work, we investigated the effects of phospholipase A and pronase on the membrane capacitance. Phospholipase A is known to block the sodium activation and pronase to eliminate the sodium inactivation. Phospholipase A is found to increase the frequency dependent as well as the frequency independent capacitances. Our tentative conclusion is that this enzyme perturbs the lipid structure and decreases its thickness. Pronase is found to increase the frequency dependent capacitance slightly while the capacitance of the lipid layer remains unaltered. Although voltage clamp data indicate that the pronase disrupts the excitatory mechanism extensively, this enzyme has relatively little effect on the overall membrane capacitance.

Animals↗
PubMed1976

Alteration of birefringence signals from squid giant axons by intracellular perfusion with protease solution.

The optical signal, arising from a transient birefringence change associated with excitation, was recorded from a squid giant axon together with the membrane potential change, and the effect of removal of the axoplasm on the optical signal was examined. In an unperfused axon, repetitive stimulation at a frequency of about 100 Hz produced two kinds of optical response. The initial response had a brief, spike-like time course and was elicited by each stimulating pulse. The delayed response had a slow time course and the sign of decreased light intensity, and summated with repetitive stimulation. Most of the axoplasm was removed from interior of the axon by intracellular perfusion with solutions containing pronase at a concentration of 0.1 mg/ml. The delayed response could selectively be eliminated by perfusion with a pronase-containing solution for 2-8 min. The result was interpreted as showing that the delayed birefringence signal originates from axoplasm when its gel structure was transiently disturbed by an increased Ca2+ influx associated with excitation. When perfusion was further continued the duration of the action potential started increasing and often a prominent after-depolarization appeared. At this stage the initial optical response was again followed by a large slow signal with the sign of increased light intensity. This reversed delayed response was tentatively assumed to originate from the membrane with some remaining axoplasm, but its cause is still not understood.

Animals↗
PubMed1977

Dipole moment changes and voltage dependent membrane capacity of squid axon.

Changes in the membrane capacity of squid axons during hyper- and depolarizations are measured between --160 and +40 mV. After corrections for the series resistance and fringe effect, we found that the membrane capacity increased from 0.68 to 1.2 muF/cm2 with depolarization. It was further observed that tetrodotoxin the external medium eliminated the change in membrane capacity without affecting the conductivity. The voltage-dependent membrane conductivity is, in turn, greatley reduced by the internal cesium ion. These observations clearly indicate that the voltage-dependent membrane capacity and conductivity are closely related to ionic channels. Particularly, the increase in membrane capacity with depolarizations may be due to sodium channels. The change in the dipole moment associated with sodium sites was determined using values of alpham and betam at various depolarizations. We found, based on voltage clamp measurements, that the increase in the dipole moment of the sodium site between --40 and --5 mV is 1230 Debye units (D.U.) and 930 D.U. between --5 and +60mV, indicating that the depolarization of sodium channels may consist of two different steps.

Animals↗
PubMed1978

Chemistry of photoreceptor membrane preparations from squid retinas.

Photoreceptor membrane preparations were made from retinas of the squid Loligo (Doryteuthis) plei for protein and lipid analysis. Lipid analysis was also completed on a single membrane preparation from Loligo pealei. (1) The membranes contain 75 wt. % protein and 25 wt. % lipid. Neutral lipids make up 26 mol % of the total lipid, the remaining 74% being phospholipid. No glycolipids were observed. (2) Free fatty acids and cholesterol comprise 8.6 and 17 mol %, respectively of the total lipid. No other neutral lipids were found. (3) Phosphatidylethanolamine and phosphatidylcholine are the major phospholipids. Lysophosphatidylcholine, lysophosphatidylethanolamine, sphingomyelin, and phosphatidylserine are present in small quantities. Phosphatidylinositol was not detected in the membranes. (4) The levels of polyunsaturated fatty acids, principally 20:4 omega 6, 20:5 omega 3, and 22:6 omega 3 are higher in the squid membranes than in any othr vertebrate or invertebrate retina that has been examined thus far. These acids account for 58 mol % of the fatty acids in phosphatidylcholine and phosphatidylserine, 75 mol % of the free fatty acids, and nearly 90% of the fatty acids of lyso- and phosphatidylethanolamine. The results from L. plei and L. pealei were indistinguishable. (5) Rhodopsin is the major protein of the membrane preparations and has a molecular weight of 50 500 +/- 850 determined by sodium dodecyl sulfate polyacrylamide gel disc electrophoresis.

Animals↗
PubMed1978

Effect of magnesium on calcium efflux in dialyzed squid axon.

The Ca efflux mechanism located in the axolemma of the tropical squid Doritheutis plei is shown to be affected by the concentration of intracellular Mg (Mgi). The removal of all of the Mg from the experimental preparation causes an increase in Ca efflux. This effect seems to be more pronounced at low levels of internal ionized calcium and high levels of internal Na.

Adenosine Triphosphate↗
PubMed1979

Sidedness of the ATP-Na+-K+ interactions with the Na+ pump in squid axons.

Using dialysed squid axons we have been able to control internal and external ionic compositions under conditions in which most of the Na+ efflux goes through the Na+ pump. We found that (i) internal K+ had a strong inhibitory effect on Na+ efflux; this effect was antagonized by ATP, with low affinity, and by internal Na+, (ii) a reduction in ATP levels from 3 mM to 50 microM greatly increased the apparent affinity for external K+, but reduced its effectiveness compared with other monovalent cations, as an activator of Na+ efflux, and (iii) the relative effectiveness of different K+ congeners as external activator of the Na+ efflux, though affected by the ATP concentration, was not affected by the Na+/K+ ratio inside the cells. These results are consistent with the idea that the same conformation of the (Na+ + K+)-ATPase can be reached by interaction with external K+ after phosphorylation and with internal K+ before rephosphorylation. They also stress a nonphosphorylating regulatory role of ATP.

Adenosine Triphosphate↗
PubMed1979

Vanadate selectively inhibits the Ko+-activated Na+ efflux in squid axons.

The effects of internally applied 1 mM vanadate on the Na+ efflux in dialysed squid axons were found to depend on the presence of external K+. In K+-free artificial sea water, vanadate did not produce any change in the rate of Na+ efflux, whereas in the presence of 10 mM K+ the Na+ efflux was reduced to values even lower than those observed in the absence of K+ (inversion of the K+-free effect). In vanadate-poisoned axons, K+ and NH+4 at low concentrations activated Na+ efflux, but at high concentrations both cations were inhibitory. However, NH+4 was always a better activator and a poorer inhibitor than K+.

Ammonia↗
PubMed1980

A new internal perfusion method for transport studies in squid giant axons.

A new internal perfusion method has been developed which allows control of the internal solute composition in squid axons. The superiority of this technique compared to the old perfusion methods is shown by the experiments performed which have reproduced, both qualitatively and quantitatively, the Na+ and Ca2+ fluxes observed in intact and dialyzed axons. Compared with the internal dialysis, the perfusion method has the advantage that the permeability barrier give by the porous capillary has been eliminated. This allows the introduction into the axon of solutes with very high molecular weight, at the same time that a fast and reliable internal control can be achieved.

Adenosine Triphosphate↗
PubMed1981

A (Ca2+, Mg2+)-ATPase activity in plasma membrane fragments isolated from squid nerves.

A (Ca2+, Mg2+)-ATPase activity and a (Ca2+, Mg2+)-dependent phosphorylation from ATP have been found in plasma membrane fragments from squid optical nerves under conditions where contamination by intracellular organelles is unlikely. The properties of this (Ca2+, Mg2+)-ATPase activity are almost identical to those of the ATP-dependent uncoupled Ca2+ efflux observed in dialyzed squid giant axons. This gives further support to the notion that the mechanism responsible for maintaining the low levels of ionized Ca concentration in nerves at rest is not a Na+-Ca2+ exchange system but an ATP-driven uncoupled Ca2+ pump.

Adenosine Triphosphatases↗
PubMed1981

Permeability of axon membranes to local anesthetics.

The permeability of the neutral form of tertiary amine local anesthetics across squid axon membranes was studied by utilizing three different experimental methods: (1) narcotic action of axon excitability was measured by monitoring the time derivative of action potential and the results were analyzed in terms of a diffusion reaction equation of local anesthetics to obtain their permeabilities; (2) the influx of local anesthetic into the axon was measured by use of the radioisotope tracer technique; and (3) the desorption rates of the neutral form of local anesthetics from lipid monolayers were measured and the desorption rate was correlated with permeability. The relative permeabilities obtained for procaine, lidocaine and tetracaine by the above three methods were comparable. The order of relative permeabilities was procaine greater than lidocaine greater than tetracaine, and had an inverse correlation with the partition coefficients of anesthetics at oil/water phases. Some discussion concerning the concept of permeability is made when the partition coefficient of a permeant molecule is high.

Action Potentials↗
PubMed1981

The effects of vanadate on calcium transport in dialyzed squid axons. Sidedness of vanadate-cation interactions.

(1) Vanadate (VO3-) fully inhibits the ATP-dependent uncoupled Ca efflux (Ca pump) in dialyzed squid axons. (2) Vanadate inhibits with high affinity. The mean apparent affinity (K 1/2) obtained was 7 microM. (3) Inhibition by vanadate is dependent on Cao. External Ca lead to a release of the inhibitory effect. (K 1/2 congruent to 3 mM). This antagonistic effect can be reverted by increasing the vanadate concentration. Internal K+ increases the affinity of the intracellular vanadate binding site. External K+ has no effect on the inhibition. (4) Vanadate has no effect on the Nao-dependent Ca efflux component (forward Na-Ca exchange) in the absence of ATP. In axons containing ATP vanadate modified this component.

Adenosine Triphosphate↗