monensin and pyranine

monensin has been researched along with pyranine* in 3 studies

Other Studies

3 other study(ies) available for monensin and pyranine

ArticleYear
The mechanism of monensin-mediated cation exchange based on real time measurements.
    Biochimica et biophysica acta, 1996, Dec-04, Volume: 1285, Issue:2

    Monensin is an ionophore that supports an electroneutral ion exchange across the lipid bilayer. Because of this, under steady-state conditions, no electric signals accompany its reactions. Using the Laser Induced Proton Pulse as a synchronizing event we selectively acidify one face of a black lipid membrane impregnated by monensin. The short perturbation temporarily upsets the acid-base equilibrium on one face of the membrane, causing a transient cycle of ion exchange. Under such conditions the molecular events could be discerned as a transient electric polarization of the membrane lasting approx. 200 microseconds. The proton-driven chemical reactions that lead to the electric signals had been reconstructed by numeric integration of differential rate equations which constitute a maximalistic description of the multi equilibria nature of the system (Gutman, M. and Nachliel, E. (1989) Electrochim. Acta 34, 1801-1806). The analysis of the reactions reveals that the ionic selectivity of the monensin (H+ > Na+ > K+) is due to more than one term. Besides the well established different affinity for the various cations, the selectivity is also derived from a large difference in the rates of cross membranal diffusivities (MoH > MoNa > MoK), which have never been detected before. (v) Quantitative analysis of the membrane's crossing rates of the three neutral complexes reveals a major role of the membranal dipolar field in regulating ion transport. The diffusion of MoH, which has no dipole moment, is hindered only by the viscose drag. On the other hand, the dipolar complexes (MoNa and MoK) are delayed by dipole-dipole interaction with the membrane. (vi) Comparison of the calculated dipoles with those estimated for the crystalline conformation of the [MoNa(H2O)2] and [MoK(H2O)2] complexes reveals that the MoNa may exist in the membrane at its crystal configuration, while the MoK definitely attains a structure having a dipole moment larger than in the crystal.

    Topics: Arylsulfonates; Cations; Electrochemistry; Fluorescent Dyes; Ion Exchange; Ionophores; Kinetics; Lasers; Lipid Bilayers; Molecular Structure; Monensin; Phospholipids; Potassium; Protons; Sodium; Thermodynamics

1996
Utilization of monensin for detection of microdomains in cholesterol containing membrane.
    Biochimica et biophysica acta, 1996, Dec-04, Volume: 1285, Issue:2

    The effect of cholesterol on the monensin mediated proton-cation exchange reaction was measured in the time-resolved domain. The experimental system consisted of a black lipid membrane equilibrated with monensin (Nachliel, E., Finkelstein, Y. and Gutman, M. (1996) Biochim. Biophys. Acta 1285, 131-145). The membrane separated two compartments containing electrolyte solutions and pyranine (8-hydroxypyrene 1,3,6-trisulfonate) was added on to one side of the membrane. A short laser pulse was used to cause a brief transient acidification of the pyranine-containing solution and the resulting electric signal, derived from proton-cation exchange, was measured in the microsecond time domain. Incorporation of cholesterol had a clear effect on the electric transients as measured with Na+ or K+ as transportable cations. The measured transients were subjected to rigorous analysis based on numeric integration of coupled, non-linear, differential rate equations which correspond with the perturbed multi-equilibria state between all reactants present in the system. The various kinetic parameters of the reaction and their dependence on the cholesterol content had been determined. On the basis of these observations we can draw the following conclusions: (1) Cholesterol perturbed the homogeneity of the membrane and microdomains were formed, having a composition that differed from the average value. The ionophore was found in domains which were practically depleted of phosphatidylserine. (2) The diffusivity of the protonated monensin (MoH) was not affected by the presence of cholesterol, indicating that the viscosity of the central layer of the membrane was unaltered. (3) The diffusivity of the monensin metal complexes (MoNa and MoK) was significantly increased upon addition of cholesterol. As the viscosity along the cross membranal diffusion route is unchanged, the enhanced motion of the MoNa and MoK is attributed to variations of the electrostatic potential within the domains.

    Topics: Arylsulfonates; Cations; Cholesterol; Diffusion; Electrochemistry; Ion Exchange; Kinetics; Lasers; Lipid Bilayers; Monensin; Phospholipids; Potassium; Protons; Sodium

1996
Monensin-mediated antiport of Na+ and H+ across liposome membrane.
    Biochimica et biophysica acta, 1991, Apr-26, Volume: 1064, Issue:1

    The mechanism of monensin-mediated transport of Na+ and H+ across large unilamellar liposome membrane was investigated. The inside negative membrane potential (delta psi) was generated by the addition of monensin to the liposomes with an outward Na+ gradient. The effects of intravesicular H+ bufferring power and medium pH on the initial rates of delta psi formation, Na+ efflux and H+ influx were examined. The results showed that (i) the initial Na+ flux (JNa) was larger than the initial H+ flux (JH) at any H+ bufferring power, (ii) the JH increased with increasing inner buffer concentration, but the effect of H+ bufferring power on the JNa was small, (iii) the initial rate of delta psi formation increased linearly with the increase in the value of (JNa-JH), and (iv) the JNa increased with increasing H+ concentration. The generation of delta psi was not due to H+ leak from the liposome, since the delta psi was generated even when H+ concentration gradient was inwardly directed. The monensin-mediated transport of Na+ and H+ in this system occurred at the ratio of Na+/H+ greater than 1.0 and the resultant net electric charge efflux is the cause of the inside negative membrane potential. Tetraphenylphosphonium retarded both the delta psi formation and the H+ influx, but did not affect the Na+ efflux, suggesting that the driving force of H+ influx is the inside negative membrane potential generated by Na+ efflux. This idea also well accounts for the observed H+ bufferring power effects on the Na+ efflux, H+ influx and delta psi formation. It was suggested that Na+ was transported in the form of 1:1 complex between protonated monensin and Na+.

    Topics: Arylsulfonates; Biological Transport; Buffers; Carrier Proteins; Hydrogen; Hydrogen-Ion Concentration; Liposomes; Membrane Potentials; Monensin; Onium Compounds; Organophosphorus Compounds; Sodium; Sodium-Hydrogen Exchangers

1991