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  • 1
    Electronic Resource
    Electronic Resource
    Photoelectrochemical sterilization of microbial cells by semiconductor powders (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 29 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract We report the novel concept of photochemical sterilization. Microbial cells were killed photoelectrochemically with semiconductor powder (platinum-loaded titanium oxide, TiO2/Pt). Coenzyme A, (CoA) in the whole cells was photo-electrochemically oxidized and, as a result, the respiration of cells was inhibited. Inhibition of respiratory activity caused death of the cells. Lactobacillus acidophilus, Saccharomyces cerevisiae and Escherichia coli (103 cells/ml respectively) were completely sterilized when they were incubated with TiO2/Pt particles under metal halide lamp irradiation for 60–120 min.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb00864.x
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  • 2
    Electronic Resource
    Electronic Resource
    Calcitonin gene-related peptide regulates calcium current in heart muscle (1989)
    [s.l.] : Nature Publishing Group
    Nature 340 (1989), S. 721-724 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Our initial experiments consistently showed that, in single atrial myocytes from bullfrog hearts, CGRP increased /Ca in a potent (threshold CGRP concentration, 10~9 M), dose-depen-dent and reversible fashion. In CGRP of concentration 3 x 10~7 M, /Ca recorded at +10 mV increased from 108 ±27 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/340721a0
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  • 3
    Electronic Resource
    Electronic Resource
    Coenzyme Q10 attenuates cyanide-activation of the ATP-sensitive K+ channel current in single cardiac myocytes of the guinea-pig (1991)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 344 (1991), S. 133-136 
    Details
    ISSN: 1432-1912
    Keywords: Coenzyme Q10 ; ATP-sensitive K channel ; Cyanide ; Cardiac myocyte
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effect of coenzyme Q10 (CoQ10) on the cyanide (CN−)-induced ATP-sensitive K+ channel current (KATP) was examined in single atrial myocytes, using the patch clamp technique. Superfusion of the cells with a CN−/low glucose bathing solution induced an outward current in the whole-cell clamp condition. Glibenclamide (1 μM) abolished this current, indicating that the current was carried through the KATP channel. After steady-state activation by CN−, pinacidil (a KATP channel opener, 300 μM) failed to further increase the current. In cell-attached patches, CN−, when applied to the bath, induced bursting openings of an 80 pS channel (the KATP channel). In cells preincubated for 30 min in a solution containing CoQ10 (100 μg/ml), CN−-activation of the KATP channel was markedly attenuated both at the whole cell and at the single channel level. At the steady-state effect of CN− in CoQ10-treated cells, pinacidil (300 μM) activated the current to the maximum level achieved by CN− in the control cells. These results suggest that CoQ10 reduces in the CN−-induced KATP current not by affecting the channel itself but by preventing depletion of intracellular ATP caused by CN−.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00167394
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  • 4
    Electronic Resource
    Electronic Resource
    On the mechanism of activation of muscarinic K+ channels by adenosine in isolated atrial cells: involvement of GTP-binding proteins (1986)
    Springer
    Pflügers Archiv 407 (1986), S. 264-274 
    Details
    ISSN: 1432-2013
    Keywords: adenosine receptor ; Muscarinie receptor ; A potassium channel ; Single atrial cell ; GTP-binding proteins ; Pertussis toxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The molecular mechanisms underlying activation of a K+ channel by adenosine (Ado) and acetylcholine (ACh) were examined in single atrial cells of guinea-pig. Whole cell clamp and patch clamp techniques were used to characterize the K+ channel. In the whole cell clamp conditions, Ado and ACh increased the K+ channel current in a dose-dependent manner. The maximum responses and the apparent dissociation constants were different for Ado and ACh activations of the current. Theophylline blocked activation of the K+ current by Ado, while atropine blocked ACh-activation, indicating that two different membrane receptors were involved. Measurements of the conductance and kinetic properties of both whole cell and single channel currents indicate that Ado and ACh regulate the same K+ channels. In “inside-out” patch conditions, GTP was required in the intracellular side of the membrane for activation of the K+ channel by agonists (present in the patch electrode). The A protomer of pertussis toxin inhibited the channel activation only when NAD was also present. Furthermore, GTP-γS, a non-hydrolyzable GTP analogue, gradually caused activation of the K+ channel in the absence of agonists. Therefore, it was concluded that Ado and m-ACh receptors link with the same population of K+ channels via GTP-binding proteins Ni and/or No in the atrial cell membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00585301
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  • 5
    Electronic Resource
    Electronic Resource
    Short-term desensitization of muscarinic K+ channel current in isolated atrial myocytes and possible role of GTP-binding proteins (1987)
    Springer
    Pflügers Archiv 410 (1987), S. 227-233 
    Details
    ISSN: 1432-2013
    Keywords: Muscarinic K+ channel ; Desensitization ; GTP-binding proteins ; Atrial cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The short-term desensitization of the acetylcholine (ACh)-induced K+ channel current was examined in single atrial cells of guinea-pig heart. The tight-seal whole cell voltage clamp technique was used. The solution in the pipettes contained GTP or guanosine-5′-O-(3-thiotriphosphate) (GTP-γS, a non-hydrolyzable GTP analogue). In GTP-loaded cells, ACh evoked a specific K+ channel current via GTP-binding proteins (G) in a dose-dependent manner. The K+ current showed agonist-dependent desensitization similar to those reported in other cardiac tissues (Nilius 1983; Carmeliet and Mubagwa 1986). The cellular response to ACh was also desensitized by activation of P1-purinergic receptors with adenosine (Ado). In GTP-γS-loaded cells, the K+ current was gradually induced even in the absence of agonists, probably due to direct activation of G proteins by GTP-γS. In the early phase of the spontaneous current increase, ACh evoked a large current transiently. As the GTP-γS-induced activation of the current progressed, the magnitude of the ACh-evoked current transient became smaller and finally negligible. Similar results were obtained when Ado was used as an agonist instead of ACh to induce the K+ current. Therefore, it is indicated that the agonistreceptor interaction may not be essential for the desensitization of ACh-induced K+ current in atrial myocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00580270
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  • 6
    Electronic Resource
    Electronic Resource
    Effects of calcitonin gene-related peptide on membrane currents in mammalian cardiac myocytes (1991)
    Springer
    Pflügers Archiv 419 (1991), S. 644-650 
    Details
    ISSN: 1432-2013
    Keywords: Calcitonin gene-related peptide ; Calcitonin ; Single cardiac myocytes ; Whole-cell voltage-clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We examined the effects of calcitonin gene-related peptide (CGRP) on the membrane currents of single atrial and ventricular cells of guinea pig heart. The tightseal whole-cell voltage-clamp technique was used. In atrial cells, like isoproterenol, CGRP increased the L-type Ca channel current (I Ca.L) in a concentration-dependent manner. Human CGRP-(8-37), a putative CGRP receptor antagonist, completely abolished the CGRP-induced increase of I Ca.L. Although the effects of CRGP were similar to those of isoproterenol, propranolol, a β-adrenergic receptor antagonist, did not affect the CGRP-induced increase of I Ca.L. After I Ca.L had been maximally activated by isoproterenol (2 μM) or intracellular cyclic adenosine 5′-monophosphate (100 μM), CGRP failed to increase I Ca.L. Acetylcholine antagonized the effects of CGRP on I Ca.L. Unlike the effects on atrial cells, CGRP had no significant effects on the membrane currents of ventricular myocytes. Thes results indicate that CGRP increases I Ca.L via adenylate cyclase activation by binding to specific membrane receptors in cardiac atrial myocytes. Furthermore, CGRP receptors are expressed in atrial cells but probably not in ventricular cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00370309
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  • 7
    Electronic Resource
    Electronic Resource
    Ionic basis of neurokinin-A-induced depolarization in single smooth muscle cells isolated from guinea-pig trachea (1995)
    Springer
    Pflügers Archiv 430 (1995), S. 552-562 
    Details
    ISSN: 1432-2013
    Keywords: Neurokinin A ; Single tracheal smooth muscle cells ; Ca2+-dependent Cl− current ; K+ currents
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Neurokinin A (NKA) caused single tracheal smooth muscle cells (TSMCs) to contract. The effects of NKA on the electrical activity of guinea-pig TSMCs were examined using the tight-seal whole-cell patch-clamp technique. Under current-clamp conditions at rest, the membrane potential of TSMCs spontaneously oscillated at about −40 mV and NKA rapidly depolarized the membrane potential to nearly 0 mV, which then gradually repolarized to about −20 mV in the presence of NKA. The oscillations in potential disappeared transiently during the rapid phase of depolarization in response to NKA and reappeared during the sustained phase of depolarization. Under voltage-clamp conditions, NKA evoked an inward current which faded quickly. Subsequently, the cell conductance in the presence of NKA at potentials greater than −40 mV decreased gradually. The reversal potential of the NKA-induced inward current was about 0 mV, and shifted with changes in the Cl− equilibrium potential. The Cl− current was not elicited by NKA when using a pipette solution containing 10 mM ethylenebis(oxonitrilo) tetraacetic acid (EGTA). During the sustained phase, K+ currents evoked by depolarizing voltage steps were inhibited by NKA. The present results indicate that NKA causes rapid and sustained depolarization of TSMCs by two distinct mechanisms: (1) initial transient activation of the Ca2+-dependent Cl− current, and (2) sustained inhibition of K+ currents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00373892
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  • 8
    Electronic Resource
    Electronic Resource
    Role of intracellular Mg2+ in the activation of muscarinic K+ channel in cardiac atrial cell membrane (1986)
    Springer
    Pflügers Archiv 407 (1986), S. 572-574 
    Details
    ISSN: 1432-2013
    Keywords: muscarinic K+ channel ; GTP-binding protein ; intracellular Mg2+ ; single atrial cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Effects of intracellular Mg2+ in the activation of a muscarinic K+ channel were examined in single atrial cells, using patch-recording techniques. In “cell-attached” patch recordings, acetylcholine (ACh) or adenosine (Ado), present in the pipette, activated a specific population of K+ channels. In “inside-out” patches, openings of the K+ channel by ACh or Ado diminished and did not resume until Mg2+ was added to the perfusate which contained GTP or GTP-γS, a non-hydrolyzable GTP analogue. Channel openings caused by GTP faded by removing Mg2+, while GTP-γS-induced openings persisted steadily even when both Mg2+ and GTP-γS were removed. In contrast to the case of GTP-induced channel openings, the GTP-γS-induced openings were not inhibited by the A protomer of pertussi toxin with NAD. From these observations, we concluded: 1) Intracellular Mg2+ is essential for GTP to activate the GTP-binding protein. 2) Deactivation of the N protein may be caused by hydrolysis of GTP to GDP. This process may not require Mg2+. 3) During the activation by GTP analogues, the N protein may be dissociated into its subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00657521
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  • 9
    Electronic Resource
    Electronic Resource
    Quinidine inhibition of the muscarine receptor-activated K+ channel current in atrial cells of guinea pig (1987)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 335 (1987), S. 216-218 
    Details
    ISSN: 1432-1912
    Keywords: Quinidine ; Anticholinergic effects ; Muscarine receptor-activated K+ channels ; Atrial cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Postsynaptic mechanisms underlying the anticholinergic effects of quinidine were examined in single atrial cells, using the tight-seal whole-cell recording technique. The solution in the glass pipettes contained guanosine-5′triphosphate (GTP) or guanosine-5′-O-(3-thiotriphosphate) (GTP-γS, a non-hydrolyzable GTP analogue). In both cases, acetylcholine (ACh), applied to the bath, induced a specific K+ current. In GTP-loaded cells, quinidine in the bath solution depressed the ACh-induced K+ current concentration-dependently. Atropine also blocked the K+ current. On the other hand, in GTP-γS-loaded cells, the ACh-induced current was not blocked by atropine and persisted even when ACh was washed out from the bath, indicating that GTP-γS causes uncoupling of the K+ channels from the muscarine receptors. Quinidine, however, did depress the increased K+ current concentration-dependently. The percent inhibition curves for quinidine to depress the K+ current were very similar between GTP-loaded and GTP-γS-loaded cells. From these observations, we suggest that direct inhibition of the muscarine receptor-activated K+ channel current by quinidine, and not blockade of the muscarine receptor itself, is mainly responsible for the anticholinergic effects of the drug in atrial myocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00177726
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  • 10
    Electronic Resource
    Electronic Resource
    Isolation and radiation hybrid mapping of a highly polymorphic CA repeat sequence at the human nuclear factor kappa-beta subunit 1 (NFKB1) locus (1999)
    Springer
    Journal of human genetics 44 (1999), S. 129-130 
    Details
    ISSN: 1435-232X
    Keywords: Key words nuclear factor kappa-beta subunit 1 ; dinucleotide repeat ; immune response ; cell differentiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The transcriptional factor nuclear factor kappa-beta (NFKB) consists of a multicomponent protein complex that plays a major role in the regulation of many viral and cellular genes. The NFKB complex has two alternative DNA binding subunits. We isolated a polymorphic dinucleotide (CA) repeat sequence from a genomic clone containing the NFKB subunit 1 (NFKB1) gene located at 4q23–24. High heterozygosity (0.813) makes this polymorphism a useful marker in the genetic study of disorders affecting the immune response and cell differentiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100380050125
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