TY - JOUR A1 - Zimmermann, Bernhard A1 - Walz, Bernd T1 - Serotonin-induced intercellular calcium waves in salivary glands of the blowfley Calliphora erythrocephala Y1 - 1997 ER - TY - JOUR A1 - Zimmermann, Bernhard A1 - Walz, Bernd T1 - The mechanism mediating regenerative intercellular Ca2+ waves in the blowfly salivary gland Y1 - 1999 ER - TY - JOUR A1 - Zimmermann, Bernhard A1 - Dames, Petra A1 - Walz, Bernd A1 - Baumann, Otto T1 - Distribution and serotonin-induced activation of vacuolar-type H+-ATPase in the salivary glands of the blowfly Calliphora vicina Y1 - 2003 ER - TY - JOUR A1 - Walz, Bernd A1 - Zimmermann, Bernhard A1 - Seidl, Siegfried T1 - Intracellular Ca2+ concentration and latency of light-induced Ca2+ changes in photoreceptors of the honeybee drone Y1 - 1994 ER - TY - JOUR A1 - Walz, Bernd A1 - Ukhanov, Kyrill A1 - Zimmermann, Bernhard T1 - Actions of neomycin on electrical light responses : Ca2+ release and intracellular Ca2+ changes in photoreceptors of the honeybee drone Y1 - 2000 SN - 0340-7594 ER - TY - JOUR A1 - Walz, Bernd A1 - Ukhanov, Kyrill T1 - Light-dependent repetitive Ca2+ spikes induced by extracellular application of neumycin in honeybee drone photoreceptors Y1 - 2000 SN - 0340-7594 ER - TY - JOUR A1 - Walz, Bernd A1 - Baumann, Otto A1 - Zimmermann, Bernhard A1 - Ciriacy-Wantrup, E.v. T1 - Caffeine- and ryanodine-sensitive Ca2+-induced Ca2+ release from the endo plasmatic reticulum in honeybee photoreceptors Y1 - 1995 ER - TY - JOUR A1 - Walz, Bernd A1 - Baumann, Otto A1 - Krach, Christian A1 - Baumann, Arnd A1 - Blenau, Wolfgang T1 - The aminergic control of cockroach salivary glands N2 - The acinar salivary glands of cockroaches receive a dual innervation from the subesophageal ganglion and the stomatogastric nervous system. Acinar cells are surrounded by a plexus of dopaminergic and serotonergic varicose fibers. In addition, seroton-ergic terminals lie deep in the extracellulor spaces between acinar cells. Excitation-secretion coupling in cockroach salivary glands is stimulated by both dopamine and serotonin. These monoamines cause increases in the intracellular concentrations of cAMP and Ca2+. Stimulation of the glands by serotonin results in the production of a protein-rich saliva, whereas stimulation by dopamine results in saliva that is protein-free. Thus, two elementary secretary processes, namely electrolyte/water secretion and protein secretion, are triggered by different aminergic transmitters. Because of its simplicity and experimental accessibility, cockroach salivary glands have been used extensively as a model system to study the cellular actions of biogenic amines and to examine the pharmacological properties of biogenic amine receptors. In this review, we summarize current knowledge concerning the aminergic control of cockroach salivary glands and discuss our efforts to characterize Periplaneta biogenic amine receptors molecularly Y1 - 2006 UR - 1960 = Doi 10.1002/Arch.20128 ER - TY - JOUR A1 - Walz, Bernd A1 - Baumann, Otto T1 - Structure and cellular physiology of Ca2+ stores in invertebrate photoreceptors Y1 - 1995 ER - TY - JOUR A1 - Walz, Bernd T1 - Auch im Süßwasser - die Hydrozoe cordylophora caspia Y1 - 1997 ER - TY - JOUR A1 - Walz, Bernd T1 - Überlebenskünstler aus dem Moospolster N2 - Populärwissenschaftlicher Aufsat Y1 - 1997 ER - TY - JOUR A1 - Voss, Martin A1 - Schmidt, Ruth A1 - Walz, Bernd A1 - Baumann, Otto T1 - Stimulus-induced translocation of the protein kinase A catalytic subunit to the apical membrane in blowfly salivary glands N2 - Secretion in blowfly (Calliphora vicina) salivary glands is regulated by the neurohormone serotonin (5-HT), which activates the InsP(3)/Ca2+ pathway and the cAMP/protein kinase A (PKA) pathway in the secretory cells. The latter signaling cascade induces the activation of a vacuolar H+-ATPase on the apical membrane. Here, we have determined the distribution of PKA by using antibodies against the PKA regulatory subunit-II (PKA-RII) and the PKA catalytic subunit (PKA-C) of Drosophila. PKA is present in high concentrations within the secretory cells. PKA-RII and PKA-C co-distribute in non-stimulated glands, being enriched in the basal portion of the secretory cells. Exposure to 8-CPT-cAMP or 5-HT induces the translocation of PKA-C to the apical membrane, whereas the PKA-RII distribution remains unchanged. The recruitment of PKA-C to the apical membrane corroborates our hypothesis that vacuolar H+-ATPase, which is enriched in this membrane domain, is a target protein for PKA. Y1 - 2009 UR - http://www.springerlink.com/content/100524 U6 - https://doi.org/10.1007/s00441-008-0673-x SN - 0302-766X ER - TY - JOUR A1 - Voss, Martin A1 - Fechner, Lennart A1 - Walz, Bernd A1 - Baumann, Otto T1 - Calcineurin activity augments cAMP/PKA-dependent activation of V-ATPase in blowfly salivary glands N2 - We have examined the role of the Ca2+-dependent protein phosphatase 2B (calcineurin) in the regulation of the vacuolar H+-ATPase (V-ATPase) in blowfly salivary glands. In response to the neurohormone serotonin [5-hydroxytryptamine (5-HT)] and under the mediation of the cAMP/PKA signaling pathway, the secretory cells assemble and activate V-ATPase molecules at the apical membrane. We demonstrate that the inhibition of calcineurin activity by cyclosporin A, by FK- 506, or by prevention of the elevation of Ca2+ diminishes the 5-HT-induced assembly and activation of V-ATPase. The effect of calcineurin on V-ATPase is mediated by the cAMP/PKA signaling pathway, with calcineurin acting upstream of PKA, because 1) cyclosporin A does not influence the 8-(4-chlorophenylthio) adenosine-3',5'-cyclic monophosphate (8-CPT-cAMP)-induced activation of V-ATPase, and 2) the 5-HT-induced rise in cAMP is highly reduced in the presence of cyclosporin A. Moreover, a Ca2+ rise evoked by the sarco(endo) plasmic reticulum Ca2+-ATPase (SERCA) inhibitor cyclopiazonic acid leads to an increase in intracellular cAMP concentration and a calcineurin-mediated PKA- dependent activation of V-ATPase. We propose that calcineurin activity mediates cross talk between the inositol 1,4,5- trisphosphate/Ca2+ and the cAMP/PKA signaling pathways, thereby augmenting the 5-HT-induced rise in cAMP and thus the cAMP/PKA-mediated activation of V-ATPase. Y1 - 2010 UR - http://ajpcell.physiology.org/ U6 - https://doi.org/10.1152/ajpcell.00328.2009 SN - 0363-6143 ER - TY - GEN A1 - Voss, Martin A1 - Blenau, Wolfgang A1 - Walz, Bernd A1 - Baumann, Otto T1 - V-ATPase deactivation in blowfly salivary glands is mediated by protein phosphatase 2C N2 - The activity of vacuolar H+-ATPase (V-ATPase) in the apical membrane of blowfly (Calliphora vicina) salivary glands is regulated by the neurohormone serotonin (5-HT). 5-HT induces, via protein kinase A, the phosphorylation of V-ATPase subunit C and the assembly of V-ATPase holoenzymes. The protein phosphatase responsible for the dephosphorylation of subunit C and V-ATPase inactivation is not as yet known. We show here that inhibitors of protein phosphatases PP1 and PP2A (tautomycin, ocadaic acid) and PP2B (cyclosporin A, FK-506) do not prevent V-ATPase deactivation and dephosphorylation of subunit C. A decrease in the intracellular Mg2+ level caused by loading secretory cells with EDTA-AM leads to the activation of proton pumping in the absence of 5-HT, prolongs the 5-HT-induced response in proton pumping, and inhibits the dephosphorylation of subunit C. Thus, the deactivation of V-ATPase is most probably mediated by a protein phosphatase that is insensitive to okadaic acid and that requires Mg2+, namely, a member of the PP2C protein family. By molecular biological techniques, we demonstrate the expression of at least two PP2C protein family members in blowfly salivary glands. © 2009 Wiley Periodicals, Inc. KW - vacuolar H+-ATPase KW - assembly KW - regulation KW - protein phosphatise KW - dephosphorylation Y1 - 2009 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-44360 ER - TY - JOUR A1 - Ukhanov, Kyrill A1 - Walz, Bernd T1 - The phosphoinositide signaling cascade is involved in photoreception in the leech Hirudo medicinalis Y1 - 2000 SN - 0340-7554 ER - TY - JOUR A1 - Ukhanov, Kyrill A1 - Mills, S. J. A1 - Potter, Barry V. L. A1 - Walz, Bernd T1 - InsP3-induced Ca2+ release in permeabilized invertebrate photoreceptors : a link between phototransduction and Ca2+ stores Y1 - 2001 ER - TY - JOUR A1 - Stürmer, Karoline A1 - Baumann, Otto A1 - Walz, Bernd T1 - Actin-dependent light-induced translocation of mitochondria and ER cisternae in the photoreceptor cells of the locust schistocerca gregaria Y1 - 1995 ER - TY - JOUR A1 - Somlyo, A. V. A1 - Walz, Bernd T1 - Ca2+ in visual transduction and adaptation in vertebrates and invertebrates Y1 - 1995 ER - TY - GEN A1 - Schmidt, Ruth A1 - Baumann, Otto A1 - Walz, Bernd T1 - cAMP potentiates InsP3-induced Ca2+ release from the endoplasmic reticulum in blowfly salivary glands T2 - Postprints der Universität Potsdam : Mathematisch Naturwissenschaftliche Reihe N2 - Background Serotonin induces fluid secretion from Calliphora salivary glands by the parallel activation of the InsP3/Ca2+ and cAMP signaling pathways. We investigated whether cAMP affects 5-HT-induced Ca2+ signaling and InsP3-induced Ca2+ release from the endoplasmic reticulum (ER). Results Increasing intracellular cAMP level by bath application of forskolin, IBMX or cAMP in the continuous presence of threshold 5-HT concentrations converted oscillatory [Ca2+]i changes into a sustained increase. Intraluminal Ca2+ measurements in the ER of ß-escin-permeabilized glands with mag-fura-2 revealed that cAMP augmented InsP3-induced Ca2+ release in a concentration-dependent manner. This indicated that cAMP sensitized the InsP3 receptor Ca2+ channel for InsP3. By using cAMP analogs that activated either protein kinase A (PKA) or Epac and the application of PKA-inhibitors, we found that cAMP-induced augmentation of InsP3-induced Ca2+ release was mediated by PKA not by Epac. Recordings of the transepithelial potential of the glands suggested that cAMP sensitized the InsP3/Ca2+ signaling pathway for 5-HT, because IBMX potentiated Ca2+-dependent Cl- transport activated by a threshold 5-HT concentration. Conclusion This report shows, for the first time for an insect system, that cAMP can potentiate InsP3-induced Ca2+ release from the ER in a PKA-dependent manner, and that this crosstalk between cAMP and InsP3/Ca2+ signaling pathways enhances transepithelial electrolyte transport. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 842 KW - endoplasmic reticulum KW - salivary gland KW - physiological solution KW - fluid secretion KW - cAMP analog Y1 - 2020 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-429770 SN - 1866-8372 IS - 842 ER - TY - JOUR A1 - Schmidt, R. A1 - Walz, Bernd T1 - Serotonin and histamine produce different spatiotemporal Ca2+ signals in blowfly salivary glands Y1 - 2004 SN - 0171-9335 ER -