%0 Journal Article %1 Meis_1981_636 %A Meissner, G. %D 1981 %J J. Biol. Chem. %K ATPase, Active, Adenosine Adenosinetriphosphatase, Adenylate Animal, Animals, Atypical, Bilayers, Biological Calcium, Cations, Cell Chemistry, Chickens, Chlorides, Comparative Concentration, Conformation, Culture Cyclase, Diffraction, Diphenylhexatriene, Disease Diseases, Dystrophy, Electron, Female, Fluorescence Fluorescence, Fracturing, Freeze Glucose, Gov't, Guanylate Guinea Hydrogen-Ion Infections, Intracellular Kinetics, Leucyl-beta-Naphthylamidase, Lipid Lipids, Liver, Macromolecular Male, Mathematics, Media, Membrane Membrane, Membranes, Mice, Microscopy, Microsomes, Models, Molecular Molecular, Monovalent, Muscles, Muscular Mycobacteria, Mycobacterium Non-P.H.S., Non-U.S. Osmotic P.H.S., Pectoralis Permeability, Physical, Pigs, Polarization, Potassium, Potentials, Poultry Pressure, Protein Proteins, Rabbits, Rats, Relationship, Research Reticulum, Sarcolemma, Sarcoplasmic Sodium, Sp, Structure-Activity Study, Substances, Support, Thermodynamics, Transport, Triphosphate, U.S. Virulence, X-Ray avium, ectrometry, {C}a$^{2+}$ {C}a$^{2+}$-Transporting {M}g$^{2+}$-ATPase, %N 2 %P 636--643 %T Calcium transport and monovalent cation and proton fluxes in sarcoplasmic reticulum vesicles. %V 256 %X ATP-dependent Ca$^2+$ uptake by rabbit skeletal muscle sarcoplasmic reticulum vesicles has been studied in the presence and absence of artificially generated pH gradients and membrane potentials. H$^+$ and K$^+$ diffusion potentials were generated via the H$^+$ and K,Na channels of sarcoplasmic reticulum by transfer of vesicles from low to high pH, or from high to low K$^+$. Membrane potentials were measured using the voltage-sensitive fluorescent dye 3,3'-dipentyl-2,2'-oxacarbocyanine. The initial rate of Ca$^2+$ uptake was found to be increased in the presence of a pH gradient and membrane potential (negative inside). In turn, the rates of decay of K$^+$- or H$^+$-induced membrane potentials were accelerated during Ca$^2+$ transport, suggesting that active Ca$^2+$ uptake stimulated the release of K$^+$ and H$^+$ from the vesicles. The ratio of K$^+$ (or H$^+$) release to Ca$^2+$ transport was near two. Release of K$^+$ did not appear to be directly catalyzed by the Ca$^2+$-ATPase. Evidence against a directly coupled ATP-mediated 2 K$^+$-Ca$^2+$ or K$^+$-Ca$^2+$ exchange reaction was that (i) similar results were obtained when K$^+$ was substituted by Na$^+$ or by organic cations which could rapidly permeate through the channel of K$^+$,Na$^+$-permeable vesicles and (ii) Ca$^2+$ transport did not result in an equivalent release of 86Rb+ or 22Na$^+$ from K$^+$,Na$^+$-impermeable vesicles. These studies are in support of an electrogenic Ca$^2+$ transport system in sarcoplasmic reticulum. The results further suggest that during Ca$^2+$ transport development of a membrane potential (positive inside) is likely nullified by the countermovement of the permeant cations K$^+$, Na$^+$, and H$^+$.

@article{Meis_1981_636, abstract = {A{TP}-dependent {C}a$^{2+}$ uptake by rabbit skeletal muscle sarcoplasmic reticulum vesicles has been studied in the presence and absence of artificially generated pH gradients and membrane potentials. {H}$^+$ and {K}$^{+}$ diffusion potentials were generated via the {H}$^+$ and K,Na channels of sarcoplasmic reticulum by transfer of vesicles from low to high pH, or from high to low {K}$^{+}$. Membrane potentials were measured using the voltage-sensitive fluorescent dye 3,3'-dipentyl-2,2'-oxacarbocyanine. The initial rate of {C}a$^{2+}$ uptake was found to be increased in the presence of a pH gradient and membrane potential (negative inside). In turn, the rates of decay of {K}$^{+}$- or {H}$^+$-induced membrane potentials were accelerated during {C}a$^{2+}$ transport, suggesting that active {C}a$^{2+}$ uptake stimulated the release of {K}$^{+}$ and {H}$^+$ from the vesicles. The ratio of {K}$^{+}$ (or {H}$^+$) release to {C}a$^{2+}$ transport was near two. Release of {K}$^{+}$ did not appear to be directly catalyzed by the {C}a$^{2+}$-ATPase. Evidence against a directly coupled ATP-mediated 2 {K}$^{+}$-{C}a$^{2+}$ or {K}$^{+}$-{C}a$^{2+}$ exchange reaction was that (i) similar results were obtained when {K}$^{+}$ was substituted by {N}a$^{+}$ or by organic cations which could rapidly permeate through the channel of {K}$^{+}$,{N}a$^{+}$-permeable vesicles and (ii) {C}a$^{2+}$ transport did not result in an equivalent release of 86Rb+ or 22{N}a$^{+}$ from {K}$^{+}$,{N}a$^{+}$-impermeable vesicles. These studies are in support of an electrogenic {C}a$^{2+}$ transport system in sarcoplasmic reticulum. The results further suggest that during {C}a$^{2+}$ transport development of a membrane potential (positive inside) is likely nullified by the countermovement of the permeant cations {K}$^{+}$, {N}a$^{+}$, and {H}$^+$.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Meissner, G.}, biburl = {https://www.bibsonomy.org/bibtex/2285f616575351d51353725bbb719cb2d/hake}, description = {The whole bibliography file I use.}, file = {Meis_1981_636.pdf:Meis_1981_636.pdf:PDF}, interhash = {ee494fe8f7f03f8d6dd9e8844c4c0c9d}, intrahash = {285f616575351d51353725bbb719cb2d}, journal = {J. Biol. Chem.}, key = 222, keywords = {ATPase, Active, Adenosine Adenosinetriphosphatase, Adenylate Animal, Animals, Atypical, Bilayers, Biological Calcium, Cations, Cell Chemistry, Chickens, Chlorides, Comparative Concentration, Conformation, Culture Cyclase, Diffraction, Diphenylhexatriene, Disease Diseases, Dystrophy, Electron, Female, Fluorescence Fluorescence, Fracturing, Freeze Glucose, Gov't, Guanylate Guinea Hydrogen-Ion Infections, Intracellular Kinetics, Leucyl-beta-Naphthylamidase, Lipid Lipids, Liver, Macromolecular Male, Mathematics, Media, Membrane Membrane, Membranes, Mice, Microscopy, Microsomes, Models, Molecular Molecular, Monovalent, Muscles, Muscular Mycobacteria, Mycobacterium Non-P.H.S., Non-U.S. Osmotic P.H.S., Pectoralis Permeability, Physical, Pigs, Polarization, Potassium, Potentials, Poultry Pressure, Protein Proteins, Rabbits, Rats, Relationship, Research Reticulum, Sarcolemma, Sarcoplasmic Sodium, Sp, Structure-Activity Study, Substances, Support, Thermodynamics, Transport, Triphosphate, U.S. Virulence, X-Ray avium, ectrometry, {C}a$^{2+}$ {C}a$^{2+}$-Transporting {M}g$^{2+}$-ATPase,}, month = Jan, number = 2, pages = {636--643}, pmid = {7451464}, timestamp = {2009-06-03T11:21:22.000+0200}, title = {Calcium transport and monovalent cation and proton fluxes in sarcoplasmic reticulum vesicles.}, volume = 256, year = 1981 }