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  • calcium  (32)
  • Springer  (32)
  • 2000-2004  (5)
  • 1985-1989  (27)
  • 1925-1929
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 96 (1987), S. 243-249 
    ISSN: 1432-1424
    Keywords: cholera toxin ; ionophore ; calcium ; brush-border membrane vesicles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The physiological relevance of an apparent ionophore activity of cholera toxin towards Ca2+ has been examined in several different systems designed to measure affinity, specificity, rates of ion transfer, and effects on intracellular ion concentrations. Half-maximal transfer rates across porcine jejunal brush-border vesicles were obtained at a concentration of 0.20 μM Ca2+. When examined in the presence of competing ions the transfer process was blocked by very low concentrations of La3+ or Cd2+. Sr2+, Ba2+ and Mg2+ were relatively inefficient competitors for Ca2+ transport mediated by cholera toxin. The relative affinities observed would be compatible with a selectivity for Ca2+ transfer at physiological ion concentrations, as well as an inhibition of this ionophore activity by recognized antagonists of cholera toxin such as lanthanum ions. Entry rates of Ca2+ into brush-border vesicles exposed to cholera toxin were large enough to accelerate the collapse of a Ca2+ gradient generated by endogenous Ca, Mg-ATPase activity. The treatment of isolated jejunal enterocytes with cholera toxin caused a significant elevation in cytosolic Ca2+ concentrations as measured by Quin-2 fluorescence. This effect was specifically prevented by prior exposure of the cholera toxin to excess ganglioside GM1. We conclude that cholera toxin has many of the properties required for promoting transmembranes Ca2+ movement in membrane vesicles and appears to be an effective Ca2+ ionophore in isolated mammalian cells.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 89 (1989), S. 127-133 
    ISSN: 1573-4919
    Keywords: mitochondria ; sarcoplasmic reticulum ; calcium ; myocytes ; caffeine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The possible contribution of mitochondrial Ca2+ accumulation and release to contractile phenomena has been investigated. Two intracellular fractions of Ca2+ sequestration can be identified in cardiac myocytes, one ascribed to mitochondria. Two modes of Ca2+ transport exist within the mitochondrial fraction, one dependent upon mitochondrial respiration and the other upon extramitochondrial [Na+]. Experiments with trabeculae show that under appropriate conditions, the rate of relaxation and the amount of tension developed is dependent on these two modes of Ca2+ transport. A model is presented quantifying the contribution of the mitochondria to relaxation.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 105 (1988), S. 207-219 
    ISSN: 1432-1424
    Keywords: choroid plexus ; brush border membrane ; Ca2+-activated K+ channels ; calcium ; barium ; TEA ; intracellular pH ; cerebrospinal fluid secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The properties of Ca2+-activated K+ channels in the apical membrane of theNecturus choroid plexus were studied using single-channel recording techniques in the cell-attached and excised-patch configurations. Channels with large unitary conductances clustered around 150 and 220 pS were most commonly observed. These channels exhibited a high selectivity for K+ over Na+ and K+ over Cs+. They were blocked by high cytoplasmic Na+ concentrations (110mm). Channel activity increased with depolarizing membrane potentials, and with increasing cytoplasmic Ca2+ concentrations. Increasing Ca2+ from 5 to 500nm, increased open probability by an order of magnitude, without changing single-channel conductance. Open probability increased up to 10-fold with a 20-mV depolarization when Ca2+ was 500nm. Lowering intracellular pH one unit, decreased open probability by more than two orders of magnitude, but pH did not affect single-channel conductance. Cytoplasmic Ba2+ reduced both channel-open probability and conductance. The sites for the action of Ba2+ are located at a distance more than halfway through the applied electric field from the inside of the membrane. Values of 0.013 and 117mm were calculated as the apparent Ba2+ dissociation constants (K d (0 mV) for the effects on probability and conductance, respectively. TEA+ (tetraethylammonium) reduced single-channel current. Applied to the cytoplasmic side, it acted on a site 20% of the distance through the membrane, with aK d (0 mV)=5.6mm. A second site, with a higher affinity,K d (0 mV)=0.23mm, may account for the near total block of chanel conductance by 2mm TEA+ applied to the outside of the membrane. It is concluded that the channels inNecturus choroid plexus exhibit many of the properties of “maxi” Ca2+-activated K+ channels found in other tissues.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 105 (1988), S. 221-231 
    ISSN: 1432-1424
    Keywords: choroid plexus ; calcium-activated potassium currents ; cerebrospinal fluid secretion ; calcium ; delayed currents ; patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The tight-seal whole-cell recording method has been used to studyNecturus choroid plexus epithelium. A cell potential of −59±2 mV and a whole cell resistance of 56±6 MΩ were measured using this technique. Application of depolarizing step potentials activated voltage-dependent outward currents that developed with time. For example, when the cell was bathed in 110mm NaCl Ringer solution and the interior of the cell contained a solution of 110mm KCl and 5nm Ca2+, stepping the membrane potential from a holding value of −50 to −10 mV evoked outward currents which, after a delay of greater than 50 msec, increased to a steady state in 500 msec. The voltage dependence of the delayed currents suggests that they may be currents through Ca2+-activated K_ channels. Based on the voltage dependence of the activation of Ca2+-activated K+ channels, we have devised a general method to isolate the delayed currents. The delayed currents were highly selective for K+ as their reversal potential at different K+ concentration gradients followed the Nernst potential for K+. These currents were reduced by the addition of TEA+ to the bath solution and were eliminated when Cs+ or Na+ replaced intracellular K+. Increasing the membrane potential to more positive values decreased both the delay and the half-times (t 1/2) to the steady value. Increasing the pipette Ca2+ also decreased the delay and decreasedt 1/2. For instance, when pipette Ca2+ was increased from 5 to 500nm, the delay andt 1/2 decreased from values greater than 50 and 150 msec to values less than 10 and 50 msec. We conclude that the delayed currents are K+ currents through Ca2+-activated K+ channels. At the resting membrane potential of −60 mV, Ca2+-activated K+ channels contribute between 13 to 25% of the total conductance of the cell. The contribution of these channels to cell conductance nearly doubles with membrane depolarization of 20–30 mV. Such depolarizations have been observed when cerebrospinal fluid (CSF) secretion is stimulated by cAMP and with intracellular Ca2+. Thus the Ca2+-activated K+ channels may play a specific role in maintaining intracellular K+ concentrations during CSF secretion.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 110 (1989), S. 19-28 
    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.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 104 (1988), S. 21-34 
    ISSN: 1432-1424
    Keywords: exocytosis ; secretion ; calcium ; protein kinase C ; adrenal medulla ; catecholamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The calcium sensitivity of exocytosis from electroper-meabilized chromaffin cells is increased by activators of protein kinase C, such as TPA and certain phorbol esters, diacylglycerols, and mezerein. A range of putative inhibitors of protein kinase C block both the phorbol ester-sensitive component of secretion and also the underlying insensitive component. These inhibitors are also shown to inhibit medulla protein kinase C activity in vitro. The extent of secretion is reduced when electropermeabilized cells are exposed to Ca2+ levels much in excess of 50 μm. The onset of inhibition is faster than the relatively slow rate of Ca-dependent exocytosis and is insensitive to inhibitors of proteolysis. Adrenal medulla protein kinase C activity is also irreversibly inhibited by high Ca2+ concentrations. Both the secretory response and the protein kinase C activity in vitro have similar nucleotide and cation specificities. Although these data do not definitely establish an involvement of protein kinase C in exocytosis, none argue against it.
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  • 7
    ISSN: 1573-8221
    Keywords: c-src locus ; calcium ; Na+, K+-cotransport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 45 (1989), S. 377-378 
    ISSN: 1420-9071
    Keywords: Chromatoid body ; spermatids ; calcium ; microtubules ; morphology ; pyroantimonate ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Morphological evidence for probable Ca2+ storage in the vesicular elements of the rat spermatid chromatoid body is documented using the K-pyroantimonate method, combined with EDTA chelation. Some vesicles are related to the microtubules associated with the chromatoid body. A possible involvement of Ca2+ in the intracellular movement and/or structural integrity of the chromatoid body is discussed.
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  • 9
    ISSN: 1572-9605
    Keywords: LaBaCuO ; calcium ; superconductivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Abstract It has been reported that, by adding equal amounts of CaO and CuO to non superconducting La3Ba3Cu6O z (La-336), a series of superconductors with nominal compositions La3Ca y Ba3Cu6+y O z were prepared with maximum Ton c ∼ 80K. Similar studies on addition of CaO and CuO in nonsuperconducting LaBaCu2O z (La-112) resulted into superconducting LaCaBaCu3O z (La-1113). To date no attempt has been made to synthesize La2CaBa2Cu5O z (La-2125) superconducting phase by addition of CaO and CuO to non superconducting La2Ba2Cu4O z (La-224) system. Also no reports are published to study the effect of replacing larger La3+-ions (1.01Å) by smaller rare earth ions viz Y3+(0.89Å), Er3+(0.91Å), Gd3+(0.91Å) on the structural and superconducting properties of (La2−x R x )Ba2(Ca y Cu4+y )O z (LRBCaC); 0.0 ≤ x ≤ 0.5; y=2x system. In this paper, we report the method of synthesis, structural and superconducting property characterization using X-ray diffraction, oxygen content measurements using iodometry, resistivity measurements using d.c. four probe technique and a.c. susceptibility measurements in the temperature range RT to 15K. Also a comparative study, on the evolution of superconducting phase with Ca-concentration for different rare earth substitutions for LRBCaC system in the context of hole doping mechanism, is carried out.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 1048-1051 
    ISSN: 1420-9071
    Keywords: Na, K-ATPase ; calcium ; calmodulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effect of calcium on Na, K-ATPase activity of rat brain homogenates and its modification by the chelating agent EDTA has been investigated. In the absence of EDTA, free calcium (approximately 10−6mol/l) stimulates Na,K-ATPase activity; in the presence of EDTA the same concentration of free calcium is without effect on the enzyme. In the absence of EDTA the stimulation by calcium of Na,-K-ATPase activity is enhanced by the additional presence of calmodulin but in the presence of EDTA, even when calmodulin is added to excess, calcium still fails to stimulate the enzyme. The possibility that EDTA interferes with an interaction between a calcium-calmodulin complex and Na,K-ATPase is discussed.
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