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  • Articles  (147)
  • calcium  (147)
  • Springer  (147)
  • 1985-1989  (147)
  • 1965-1969
  • 1
    Electronic Resource
    Electronic Resource
    Ca2+-activated K+ channels from cultured renal medullary thick ascending limb cells: Effects of pH (1989)
    Springer
    The journal of membrane biology 110 (1989), S. 49-55 
    Details
    ISSN: 1432-1424
    Keywords: loop of Henle ; potassium secretion ; channels ; acid/base balance ; thick ascending limb ; calcium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Ca2+-activated K+ channels were studied in cultured medullary thick ascending limb cells (MTAL) using the patch-clamp technique. The purpose was to determine the effect of acidic pH on channel properties in excised patches of apical cell membrane. At pH 7.4, increasing Ca2+ on the intracellular side or applying positive voltages increases channel open probability. Reducing pH to 5.8 on the intracellular face of the channel decreases channel open probability at each voltage and Ca2+ concentration. Channel mean open times display two distributions and mean closed times display three distributions. Increasing Ca2+ or applying depolarizing voltages lengthens each of the mean open times and shortens each of the closed times. Lowering pH to 5.8 decreases the mean open times and increases mean closed times at each Ca2+ and voltage with the greatest effect on the mean closed times. In contrast, both single-channel conductance and channel kinetics are unaffected when pH is reduced to 5.8 on the extracellular face of the membrane. We conclude that protons interfere with Ca2+ binding to the gate of Ca2+-activated K+ channels reducing the probability of channel opening.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870992
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  • 2
    Electronic Resource
    Electronic Resource
    Tight junction formation in cultured epithelial cells (MDCK) (1985)
    Springer
    The journal of membrane biology 86 (1985), S. 113-125 
    Details
    ISSN: 1432-1424
    Keywords: epithelial monolayers ; MDCK cells ; tight junctions ; calcium ; biosynthesis of junctions ; junctional assembly ; apical/basolateral polarization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Synthesis and assembly of tight junctions are studied in monolayers of MDCK cells plated at a density sufficient for confluence, allowed to attach for 1 hr, and transferred to fresh media without cells containing or not Ca2+, 20 hr later, while monolayers with Ca2+ have fully developed junctions that confer an electrical resistance across of 346±51 Ω cm2, those without Ca2+ have a negligible resistance. If at this time Ca2+ is added, junctions assemble and seal with a fast kinetics, that can be followed through the development of electrical resistance, penetration of ruthenium red, and electron microscopy. Drugs that impair synthesis, maturation and transport of proteins (cycloheximide, tunicamycin, monensin) indicate that protein components are synthesized early upon plating, do not seem to require N-glycosylation, and are stored in the Golgi compartment. Upon addition of Ca2+ they are transferred to the membrane with the participation of microfilaments but not of microtubules. These components seem to insert directly in the position they occupy in the strands, and the cell circles its perimeter with one strand as early as 15 min, even if in some segments it only consists of a row of particles. New strands develop in association with previous ones, and the pattern completes in 4 to 6 hr. Ca2+ is required for the maintenance of the assembly and also for the sealing with neighboring cells. These processes cannot occur below 25°C. Serum is not required. Polarized distribution of intramembrane particles (IMP) in apical and basolateral regions follows the same time course as junction formation, in spite of the fence constituted by those strands that are already assembled. This suggests that IMP do not redistribute by lateral displacements in the plane of the membrane, but by removal and insertion in the apical and basolateral domains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870778
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  • 3
    Electronic Resource
    Electronic Resource
    Electric pulse-induced fusion of mouse lymphoma cells: Roles of divalent cations and membrane lipid domains (1985)
    Springer
    The journal of membrane biology 85 (1985), S. 269-280 
    Details
    ISSN: 1432-1424
    Keywords: cell fusion ; electrofusion ; dielectrophoresis ; calcium ; magnesium ; membrane lipid ; lymphoma cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Mouse leukemic lymphoblasts (L5178Y) brought into close contact by dielectrophoresis underwent cell fusion following the application of electrical pulses in the presence of electrolytes. The electrically fused cells became spherical after switching off the dielectrophoretic field. Fusion between a cell vitally stained with Janus Green and that with Neutral Red resulted in the homokaryon with a mixed color. Intracellular potentials simultaneously recorded from the two cells located on both sides of the homokaryon were identical. The fusion efficiency was remarkably dependent upon temperature, displaying a discontinuity at about 11°C in the Arrhenius plot. The extracellular application of phospholipase-A2 or-C suppressed the fusion yield. Thus, it appears that the phospholipid domains play a crucial role in the electric pulse-induced cell fusion. Treatment of the cells with proteolytic enzymes markedly enhanced the fusion yield, presumably due to removing the glycocalix and/or giving rise to fusion-potent, protein-free lipid domains. The presence of millimolar concentrations of divalent cations (irrespective of Mg2+ or Ca2+) as well as of micromolar concentrations of Ca2+ (but not Mg2+) was prerequisite to the resealing of membranes suffered from electrical breakdown upon exposure to electric pulses. In addition, extracellular Ca2+ (but not Mg2+) ions at more than micromolar concentrations were indispensable for the cell fusion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871522
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  • 4
    Electronic Resource
    Electronic Resource
    Single Cl− channels in molluscan neurones: Multiplicity of the conductance states (1985)
    Springer
    The journal of membrane biology 86 (1985), S. 9-15 
    Details
    ISSN: 1432-1424
    Keywords: molluscan neurone ; patch voltage-clamp technique ; single Cl channel ; calcium ; potassium ; multiplicity of the condutance states
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Properties of the single Cl− channels were studied in excised patches of surface membrane from molluscan neurones using single-channel recording technique. These channels are controlled by Ca2+ and K+ acting on cytoplasmic and outer membrane surfaces, respectively, and by the membrane potential. The channels display about 16 intermediate conductance sublevels, each of them being multiples of ∼12.5 pS. The upper level of the channel conductance is about 200 pS. The channel behavior is consistent with an aggregation of channel-forming subunits into a cluster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871605
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  • 5
    Electronic Resource
    Electronic Resource
    Ionic and permeability requirements for exocytosis in vitro in sea urchin eggs (1988)
    Springer
    The journal of membrane biology 101 (1988), S. 199-207 
    Details
    ISSN: 1432-1424
    Keywords: exocytosis ; membrane fusion ; secretion ; calcium ; sea urchin egg ; cortical granule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We study exocytosis in the planar isolated cortex of the egg of the sea urchinLytechinus pictus. Solutins bathing the exocytotic apparatus need not contain appreciable amounts of ions: fusion follows addition of submicromolar calcium to solutions containing only nonelectrolyte. We examine the effects of altering the granule membrane permeability to small molecules with ionophores and digitonin. Introducing holes in the secretory granule membrane to the extent of allowing free passage of small molecules does not cause seretion in vitro. We add the amphipathic compound digitonin at 12 to 15 μM concentrations and demonstrate that the granule membrane can become permeable to lucifer yellow, yet that granules remain intact. Granules still undergo exocytosis after digitonin treatment at such concentrations upon subsequent addition of calcium. Higher concentrations of digitonin lead to granule content swelling and vesicle bursting. We conclude that cortical granule hydration during exocytosis is not mediated by small ionic channels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01872835
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  • 6
    Electronic Resource
    Electronic Resource
    The chromaffin granule proton pump and calcium-dependent exocytosis in bovine adrenal medullary cells (1985)
    Springer
    The journal of membrane biology 83 (1985), S. 147-156 
    Details
    ISSN: 1432-1424
    Keywords: Exocytosis ; proton pump ; calcium ; secretion ; adrenal medulla
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Calcium-dependent exocytosis in ‘leaky’ bovine adrenal medullary cells has a requirement for Mg-ATP. One possibility is that exocytosis depends in some way on the operation of the ATP-dependent proton pump that serves to maintain the core of the secretory vesicles both acid and at a positive potential with respect to the cytosol. This possibility has been tested in ‘leaky’ cells by monitoring exocytosis under conditions where the secretory vesicle pH and potential gradients are measuredin situ. The results show rather clearly that exocytosis can persist, with unchanged Ca-activation kinetics, in the virtual absence both of a difference in pH between the cytosol and secretory vesicle core and also of a difference in potential across the vesicle membrane. The results do not, however, exclude a small modulating effect of vesicle pH or potential on exocytosis and shed no light on whether or not the plasma membrane potential, which is maintained close to zero in these experiments, influences exocytosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868746
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  • 7
    Electronic Resource
    Electronic Resource
    Electrophysiological evidence suggests a defective Ca2+ control mechanism in a newParamecium mutant (1987)
    Springer
    The journal of membrane biology 98 (1987), S. 275-283 
    Details
    ISSN: 1432-1424
    Keywords: Paramecium ; calcium ; cilia ; mutants ; Ca2+ pump ; Ca2+ buffering ; ion channels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A new mutant ofParamecium tetraurelia, k-shyA, was characterized behaviorally and electrophysiologically. The mutant cell exhibited prolonged backward swimming episodes in response to depolarizing conditions. Electrophysiological comparison of k-shyA with wild type cells under voltage clamp revealed that the properties of three Ca2+-regulated currents were altered in the mutant. (i) The voltage-dependent Ca2+ current recovered from Ca2+-dependent inactivation two- to 10-fold more slowly than wild type. Ca2+ current amplitudes were also reduced in the mutant, but could be restored by EGTA injection. (ii) The decay of the Ca2+-dependent K+ tail current was slower in the mutant. (iii) The decay of the Ca2+-dependent Na+ tail current was also slower in the mutant. All other membrane properties studied, including the resting membrane potential and resistance and the voltage-sensitive K+ currents, were normal in k-shyA. Considered together, these observations are consistent with a defect in the ability of k-shyA to reduce the free intracellular Ca2+ concentration following stimulation. The possible targets of the genetic lesion and alternative explanations are discussed. The k-shy mutants may provide a useful tool for molecular and physiological analyses of the regulation of Ca2+ metabolism inParamecium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871189
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  • 8
    Electronic Resource
    Electronic Resource
    Parathyroid hormone-induced changes of the brush border topography and cytoskeleton in cultured renal proximal tubular cells (1986)
    Springer
    The journal of membrane biology 92 (1986), S. 151-162 
    Details
    ISSN: 1432-1424
    Keywords: kidney ; parathyroid hormone ; angiotensin II ; calcium ; brush border ; cytoskeleton
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary In order to examine the possibility of parathyroid hormone-mediated ultrastructural rearrangements in target epithelium, isolated canine renal proximal tubular cells were grown on a collagen-coated semipermeable membrane in a defined medium. Scanning and transmission electron microscopy of these monolayers revealed abundant microvilli. Exposure of the proximal tubular cells to parathyroid hormone resulted in a biphasic changes involving: (1) dramatic shortening and rarefaction of microvilli within 1 min; and (2) recovery of microvillar topography after 5 min. A similar shortening of microvilli was observed following exposure to ionomycin, whereas incubation with cyclic AMP resulted in an elongation of microvilli. Parathyroid hormone stimulated cyclic AMP production and increased cytoplasmic free calcium concentration in cultured proximal tubular cells. Pretreatment of cells with a calmodulin inhibitor abolished the effect of parathyroid hormone on brush border topography. Shortening of microvilli was associated with a disappearance of microvillar core filaments. Staining of F-actin with fluoresceinphalloidin showed that parathyroid hormone resulted in fragmentation of stress fibers. It is concluded that parathyroid hormoneinduced cell activation involves cytoplasmic-free calcium, calmodulin, and the cytoskeleton.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870704
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  • 9
    Electronic Resource
    Electronic Resource
    Role of calcium and calmodulin in the regulation of the rabbit ileal brush-border membrane Na+/H+ antiporter (1989)
    Springer
    The journal of membrane biology 108 (1989), S. 207-215 
    Details
    ISSN: 1432-1424
    Keywords: calcium ; calmodulin ; absorption ; ileum ; brush-border vesicle ; phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary In rabbit ileum, Ca2+/calmodulin (CaM) appears to be involved in physiologically inhibiting the linked NaCl absorptive process, since inhibitors of Ca2+/CaM stimulate linked Na+ and Cl− absorption. The role of Ca2+/CaM-dependent phosphorylation in regulation of the brush-border Na+/H+ antiporter, which is believed to be part of the neutral linked NaCl absorptive process, was studied using purified brush-border membrane vesicles, which contain both the Na+/H+ antiporter and Ca2+/CaM-dependent protein kinase(s) and its phosphoprotein substrates. Rabbit ileal villus cell brush-border membrane vesicles were prepared by Mg precipitation and depleted of ATP. Using a freezethaw technique, the ATP-depleted vesicles were loaded with Ca2+, CaM, ATP and an ATP-regenerating system consisting of creatine kinase and creatine phosphate. The combination of Ca2+/CaM and ATP inhibited Na+/H+ exchange by 45±13%. This effect was specific since Ca2+/CaM and ATP did not alter diffusive Na+ uptake, Na+-dependent glucose entry, or Na+ or glucose equilibrium volumes. The inhibition of the Na+/H+ exchanger by Ca2+/CaM/ATP was due to an effect on theV max and not on theK m for Na+. In the presence of CaM and ATP, Ca2+ caused a concentration-dependent inhibition of Na+ uptake, with an effect 50% of maximum occurring at 120nm. This Ca2+ concentration dependence was similar to the Ca2+ concentration dependence of Ca2+/CaM-dependent phosphorylation of specific proteins in the vesicles. The Ca2+/CaM/ATP-inhibition of Na+/H+ exchange was reversed by W13, a Ca2+/CaM antagonist, but not by a hydrophobic control, W12, or by H-7, a protein kinase C antagonist. we conclude that Ca2+, acting through CaM, regulates ileal brush-border Na+/H+ exchange, and that this may be involved in the regulation of neutral linked NaCl absorption.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871735
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  • 10
    Electronic Resource
    Electronic Resource
    Ca2+ and cAMP activate K+ channels in the basolateral membrane of crypt cells isolated from rabbit distal colon (1989)
    Springer
    The journal of membrane biology 110 (1989), S. 19-28 
    Details
    ISSN: 1432-1424
    Keywords: colon ; ion transport ; ion channel ; cyclic nucleotides ; calcium ; potassium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Using patch-clamp techniques, we have studied Ca2+-activated K+ channels in the basolateral membrane of freshly isolated epithelial cells from rabbit distal colon. Epithelial cell clusters were obtained from distal colon by gentle mechanical disruption of isolated crypts. Gigaohm seals were obtained on the basolateral surface of the cell clusters. At the resting potential (approximately −45 mV), with NaCl Ringer's bathing the cell, the predominant channels had a conductance of 131±25 pS. Channel activity depended on voltage as depolarization of the membrane increased the open probability. In excised inside-out patches, channels were found to be selective for K+ over Na+. Channel activity correlated directly with bath Ca2+ concentration in the excised patches. Channel currents were blocked by 5mm TEA+ and 1mm Ba2+. In cell-attached patches, after addition of the Ca2+ ionophore A23187, which increases intracellular Ca2+, open probability was markedly increased. Channel activity was also regulated by cAMP as addition of 1mm dibutyryl-cAMP in the bath solution in cell-attached patches increased channel open probability over 20-fold. Channels that had been activated by cAMP were further activated by Ca2+. We conclude that the basolateral membrane of epithelial cells from descending colon contains a class of potassium channels, which are regulated by intracellular Ca2+ and cAMP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870989
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