Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Polychaeta”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 631 records · Page 35Linked to original sources

Quantitative description of the sodium conductance of the giant axon of Myxicola in terms of a generalized second-order variable.

A variety of experimental observations in Myxicola and other preparations indicate that the sodium conductance, gNa, has properties quite different from those described by the m and h variables of Hodgkin and Huxley. A new quantitative description of the gNa is presented in which the gNa is assumed to be proportional to the fifth power of a generalized second-order variable, i.e., gNa = g'Na times v to the fifth, v = -Kav + K2U = K3, U = K4U + K5v + K6. This model is shown to be able to quantitatively simulate all of the experimentally observed behavior of the gNa. A view of the sodium gate consistent with these kinetics is to imagine it to be composed of five independent subunits, each of the type A eq. B eq. C eq. A where A represents the resting state, B the conducting state, and C the inactivated state. A model in which the subunit is of the type A eq. B eq. C could not simulate the experimental observations. It was concluded that two processes are sufficient to account for all of the behavior of the gNa.

Animals↗

Dipole moment, enthalpy, and entropy changes of Hodgkin-Huxley type kinetic units.

Dipole moment, enthalpy, and entropy changes were calculated for hypothetical structural units which control the opening and closing of ionic channels in axon membranes. The changes of these thermodynamic functions were calculated both for activation (transition to intermediate complex) and for the structural transformation as a whole. The calculations are based on the experimentally determined Q10 values and the empirical formulae for the rate constants (alpha's and beta's) as functions of membrane potentials in Hodgkin-Huxley type models. From the calculated thermodynamic functions we suggest that the specific structural units of the axon membranes are probably of macromolecular (possible protein-like) dimensions with large dipole moments (hundreds of debyes). The calculated dipole moment changes of a single structural unit indicate that in many cases these dipole moments saturate at strong depolarizations or hyperpolarizations. The transitions in structural units show substantial activation enthalpies and entropies but the net enthalpy and entropy changes are practically negligible for the transition as a whole, i.e. the structural units presumably undergo displacements. While the calculated dipole moment changes associated with structural transformations in Loligo and Myxicola show similar potential dependencies, those for Rana usually show a different behavior. The relevance of the dipole moment changes to gating currents is discussed.

Animals↗

Further studies of activation-inactivation coupling in Myxicola axons. Insensitivity to changes in calcium concentration.

In Myxicola axons subjected to moderate depolarizations the sodium inactivation time constants obtained from the decay of sodium current during a maintained depolarizatin (TSh) are substantially smaller than inactivation time constants determined at the same potential from the effect of changes in the duration of conditioning prepulses (Tph). This report extends these observations to positive membrane potentials and demonstrates that for sufficiently large depolarizations TSh and Tph become comparable. The ratio of inactivation time constants, Tph/TSh, is unaffected by changes in [Ca++] provided total divalent cation concentration is maintained constant, while changes in total divalent ion concentrations produce simple voltage shifts comparable to those obtained from measurement of membrane sodium or potassium conductances. Sodium inactivation delay was quantitatively determined as a function of membrane potential, and found to be similarly unaffected by changes in [Ca++] at constant total divalent ion concentration. Inactivation delay is, however, directly proportional to the activation rate constant over a wide range of potentials.

Animals↗

Comparison of two-pulse sodium inactivation with reactivation in Myxicola giant axons.

Values for the time constant of reactivation of the sodium conductance following depolarization sufficient to completely inactivate GNa have been compared over a 15 mV range of membrane potential with the time constants of inactivation during a depolarization prepulse. Over this range the reactivation time constants were consistently 30-50% larger than the inactivation time constants determined simultaneously at the same potential in the same axon. The data suggests that inactivation and reactivation do not occur by identical mechanisms, and therefore implies that there are at least three kinds of experimental procedures necessary to fully characterize the sodium inactivation process in any particular system.

Animals↗

Slow sodium inactivation in Myxicola axons. Evidence for a second inactive state.

Sodium inactivation and reactivation have been examined in voltage-clamped Myxicola axons after long-lasting membrane depolarizations produced either directly by changes in holding potential or indirectly by elevation of external K+ concentration. The results suggest the existence of a second inactivated state of the sodium channel with associated voltage-dependent rate constants at least two orders of magnitude lower than those of the fast inactivation process commonly examined. No specific influence of external [K+] on slow Na+ inactivation could be detected.

Animals↗

Activation-inactivation coupling in Myxicola giant axons injected with tetraethylammonium.

Myxicola giant axons internally injected with tetraethylammonium chloride to block potassium currents were examined under voltage clamp. The sodium inactivation time constants obtained from the decline in INa during step depolarizations were substantially smaller than those obtained using conditioning prepulses to the same potentials and the ratios agreed with previous observations using TTX. Inactivation shifts were also measured and found to be comparable to previous results.

Animals↗

Internal cesium alters sodium inactivation in Myxicola.

When Myxicola giant axons are internally dialyzed with Cs+ as the sole cation, the time-course of prepulse inactivation is selectively accelerated compared to its rate with K+ dialysis in the same axons. This decrease in tauph occurs without any change in the magnitude or time-course of INa during step depolarizations and results in tauph/taush ratios near unity over most of the potential range in Cs+ dialyzed axons.

Animals↗

Internally perfused Myxicola giant axons showing long-term survival.

An improved method for internally perfusing the Myxicola giant axon based on removing the axoplasm by dispersing it in KCl-KF salt solutions is described. Proteolytic enzymes are not introduced. With this improved method perfused preparations show long-term stability of their electrical properties and the ability to generate action potentials for many hours. Mean initial values for resting membrane potential, action potential amplitude, and peak inward current were -68 mV, 118 mV, and 3.62 mA/cm2, respectively. Mean resting membrane resistance was 75% of that in intact axons. In one series of voltage clamp experiments, perfused preparations remained excitable for a mean period of 5 1/2 h, but this period could exceed 10 h. 4 min are needed for exchange of internal solutions. At least 50 mM KF is required both in the axoplasm liquefying solution and in the standard perfusate to obtain stable preparations.

Action Potentials↗

Modifications of sodium channel gating in Myxicola giant axons by deuterium oxide, temperature, and internal cations.

In dialyzed Myxicola axons substitution of heavy water (D2O) externally and internally slows both sodium and potassium kinetics and decreases the maximum conductances. Furthermore, this effect is strongly temperature dependent, the magnitude of the slowing produced by D2O substitution decreasing with increasing temperature over the range 3-14 degrees C with a Q10 of approximately 0.71. The relatively small magnitude of the D2O effect, combined with its strong temperature dependence, suggests that the rate limiting process producing a conducting channel involves appreciable local changes in solvent structure. Maximum conductances in the presence of D2O were decreased by approximately 30%, while the voltage dependences of both gNa and gK were not appreciably changed. In contrast to the effects of heavy water substitution on the ionic currents, membrane asymmetry currents were not altered by D2O, suggesting that gating charge movement may preceed by several steps the final transformation of the Na+ channel to a conducting state. In Myxicola axons the effect of temperature alone on asymmetry current kinetics can be well described via a simple temporal expansion equivalent to a Q10 of 2.2, which is somewhat less than the Q10 of GNa activation. The integral of membrane asymmetry current, representing maximum charge movement, is however not appreciably altered by temperature.

Animals↗

Inhibition of potassium conductance with external tetraethylammonium ion in Myxicola giant axons.

In voltage clamp experiments, externally applied tetraethylammonium ion (TEA) was found to have minimal effects on transient sodium currents and to suppress steady-state potassium currents of Myxicola giant axons by causing a specific decrease in the maximum potassium conductance gK. The dose-response curve suggests a one-to-one stoichiometry for TEA-receptor binding with an apparent dissociation constant on 24 mM. The suppression of IK is essentially reversible. Experiments performed on high external potassium ion concentrations indicate that both outward and inward IK were blocked by external TEA. The results thus suggest the presence of TEA receptors on the outer surface of Myxicola axonal membrane similar to those reported in the frog node.

Animals↗

Solvent substitution as a probe of channel gating in Myxicola. Differential effects of D2O on some components of membrane conductance.

Careful examination of effects of solvent substitution on excitable membranes offers the theoretical possibility of identifying those aspects of the gating and translocation processes which are associated with significant changes in solvent order. Such information can then be used to develop or modify moire detailed models. We have examined the effects of heavy water substitution in Cs+-and K+-dialyzed Myxicola giant axons. At temperatures of 4-6 degrees C, the rates of Na+, K+, and Na+ inactivation during a maintained depolarization were all showed by approximately 50% in the presence of D2O. In contrast, the effects of solvent substitution on the time-course of prepulse inactivation and reactivation were much larger, with slowing averaging 160%. Studies at higher temperatures yielded Q10's for Na+ activation and K+ activation which were essentially comparable (0.72) and slightly but significantly smaller than that for inactivation during a maintained depolarization (0.84). In contrast, the Q10 for the D2O effect on prepulse inactivation was approximately 0.48. Heavy water substitution decrease Gk to a significantly greater extent than G(Na), while the decrease in the conductance of the Na+ channel caused by D2O was independent of whether the current-carrying species was Na+ or Li+. Sodium channel selectivity to the alkali metal cations and NH4+ was not changed by D2O substitution.

Animals↗

Experimental evidence consistent with aggregation kinetics in the sodium current of Myxicola giant axons.

Aggregation kinetics, in contrast to the Hodgkin-Huxley equations, predict that if an axon is subjected to a brief perturbing depolarization of large amplitude, the resulting perturbed current will cross over the response to a conventional maintained depolarization, and then remain smaller for the remainder of the depolarizing step. This has been experimentally tested using voltage-clamped Myxicola giant axons, compensated for series resistance and bathed in 10% Na+ sea water to minimize possible artifacts. Under such conditions perturbed and unperturbed currents are observed to cross over in a manner qualitatively consistent with the behavior predicted by an aggregation model. We suggest, therefore, that the aggregation concept may warrant further experimental and theoretical investigation.

Animals↗

Solvent substitution as a probe of channel gating in Myxicola. Effects of D2O on kinetic properties of drugs that occlude channels.

The effects of solvent substitution on the steady-state and kinetic properties of drugs (gallamine triethiodide) and ions (nonyltriethylammonium and Ba++) known to occlude Na+ and K+ channels have been examined and compared with the effects of D2O on unmodified channels. In general, we observed large isotope effects on the kinetics of occlusion at temperatures of 5 degrees C, but only minor effects at 15 degrees C, consistent with processes involving significant solvent interaction. Steady-state behavior was not affected. In the case of gallamine, where a dual effect on INa is evident, although both processes were D2O sensitive, only the occlusion phase had a significant temperature dependence.

Animals↗

Evidence for negative gating charges in Myxicola axons.

In Myxicola giant axons, the total amount of intramembrane charge available to move over the range -80 to + 120 mV decreases by 23% when the external pH is reduced from 7.3 to 5.5. The remaining charge moves more slowly at the onset of depolarizing pulse, but the rate of charge movement at the end of the pulse is unchanged. In contrast to acidic external pH, intramembrane charge movements are insensitive to alkaline external pH or any change in the internal pH. The results are consistent with a hypothesis in which a portion of the initial outward gating current consists of titratable negative charges moving inward.

Animals↗

Tetramethylammonium ions alter sodium-channel gating in Myxicola.

In Myxicola axons, substitution of tetramethylammonium (TMA+) for Cs+ alters intramembrane charge movements (gating currents). Although the total charge moved during and following a depolarizing step remains constant, with TMA+ the ON response has additional slower component(s), and the OFF response is retarded. Concommitantly, TMA+ produces the same voltage-dependent block of Na+ inactivation in Myxicola as has been observed in other preparations. At large positive potentials as many as 70% of the Na+ channels fail to inactivate in the steady state. In addition, TMA+ slows Na+ activation, retards the inactivation of those Na+ channels that remain able to inactivate, and decreases the maximum Na+ conductance. The steady-state Na+ conductance induced by internal TMA+ or Na+ is consistent with a scheme in which these internal cations simply modify Na+ channels in an all-or-none fashion so that a fraction become incapable of inactivating.

Animals↗

Steady state current noise from the intrinsic gating of inward rectifier channels.

Steady-state current noise from the intrinsic gating of inward rectifier channels in the eggs of the marine polychaete Neanthes arenaceodentata was recorded under voltage clamp conditions. Lorentzian-shaped power spectra with corner frequencies near 1 Hz and zero-frequency asymptotes of 1 - 5 X 10(-23) A2/Hz were obtained for test potentials 15-45 mV positive to EK in solutions containing 10-40 mM Ko. The spectra are compatible with the predictions of a three-state kinetic model for inward rectification in which the single channel rectification is independent of voltage. The single channel conductance derived from this interpretation is 8 pS with 40 mM Ko.

Animals↗

Internal cesium and the sodium inactivation gate in Myxicola giant axons.

Internal cesium (CSi), relative to internal potassium (Ki), alters Na current (INa) time course in internally perfused Myxicola giant axons. CSi slows the time to peak INa, slows its decline from peak and increases the steady state to peak current ratio, INainfinity/INapeak. Neither activation nor deactivation kinetics are appreciably affected by CSi. Na current rising phases, times to half maximum and tail current time courses are similar in CSi and Ki. Inactivation time constants determined by both one (tau h) and two (tau c) pulses are also little changed by CSi. The CSi effects are due largely or entirely to an increased INainfinity/INapeak. CSi decreases the steady level of inactivation reached during a step in potential, preventing some fraction of inactivation gates from closing at all, the rest apparently closing normally. Inactivation block in CSi decreases with increasing inward current magnitude and in Ki inactivation block is appreciable only for outward Na channel current, suggesting the site of action is located somewhere in the current pathway. If this site mediates the normal operation of the inactivation gate, then a possible mechanism for gate closure could involve a positively charged structure moving to associate with a negative site near or into the inner channel mouth.

Animals↗

Geographical distribution and inactivation kinetics in internally perfused Myxicola giant axons.

In some preparations the time constant of Na current inactivation determined with two pulses (tau c) is larger over some range of potentials than that determined from the current decay during a single pulse (tau h), while in others tau c(V) and tau h(V) are the same. Myxicola giant axons obtained from specimens collected from coastal waters of northeastern North America display a tau c - tau h difference under all conditions we have tested. In these axons tau c(V) and tau h(V) are unchanged by reduction of Na current density, addition of K-channel blockers, or internal perfusion. Specimens of the same species, Myxicola infundibulum, collected from a different geographical location, the south coast of England, have been studied under internal perfusion with K as the major cation internally, with reduced external Na concentration and in the presence of K-channel blockers. In these axons tau c(V) and tau h(V) approximately superpose, raising the possibility that dramatic differences in Na current kinetics may not necessarily reflect basic differences in the organization of the Na channel gating machinery.

Animals↗