@article{Baumann2000, author = {Baumann, Otto}, title = {Distribution of ryanodine receptor Ca2+ channels in insect photoreceptor cells}, year = {2000}, language = {en} } @article{BaumannArltRoemmlingetal.2000, author = {Baumann, Otto and Arlt, Kathleen and R{\"o}mmling, Katja and Goller, Helmut and Walz, Bernd}, title = {Characterization of an extremely motile cellular network in the rotifer Asplanchna : Structure, kinetics and the cytoskeleton}, year = {2000}, language = {en} } @article{KloseRolkeBaumann2017, author = {Klose, Sascha Peter and Rolke, Daniel and Baumann, Otto}, title = {Morphogenesis of honeybee hypopharyngeal gland during pupal development}, series = {Frontiers in zoology}, volume = {14}, journal = {Frontiers in zoology}, publisher = {BioMed Central}, address = {London}, issn = {1742-9994}, doi = {10.1186/s12983-017-0207-z}, pages = {2866 -- 2875}, year = {2017}, abstract = {Background: The hypopharyngeal gland of worker bees contributes to the production of the royal jelly fed to queens and larvae. The gland consists of thousands of two-cell units that are composed of a secretory cell and a duct cell and that are arranged in sets of about 12 around a long collecting duct. Results: By fluorescent staining, we have examined the morphogenesis of the hypopharyngeal gland during pupal life, from a saccule lined by a pseudostratified epithelium to the elaborate organ of adult worker bees. The hypopharyngeal gland develops as follows. (1) Cell proliferation occurs during the first day of pupal life in the hypopharyngeal gland primordium. (2) Subsequently, the epithelium becomes organized into rosette-like units of three cells. Two of these will become the secretory cell and the duct cell of the adult secretory units; the third cell contributes only temporarily to the development of the secretory units and is eliminated by apoptosis in the second half of pupal life. (3) The three-cell units of flask-shaped cells undergo complex changes in cell morphology. Thus, by mid-pupal stage, the gland is structurally similar to the adult hypopharyngeal gland. (4) Concomitantly, the prospective secretory cell attains its characteristic subcellular organization by the invagination of a small patch of apical membrane domain, its extension to a tube of about 100 mu m in length (termed a canaliculus), and the expansion of the tube to a diameter of about 3 mu m. (6) Finally, the canaliculus-associated F-actin system becomes reorganized into rings of bundled actin filaments that are positioned at regular distances along the membrane tube. Conclusions: The morphogenesis of the secretory units in the hypopharyngeal gland of the worker bee seems to be based on a developmental program that is conserved, with slight modification, among insects for the production of dermal glands. Elaboration of the secretory cell as a unicellular seamless epithelial tube occurs by invagination of the apical membrane, its extension likely by targeted exocytosis and its expansion, and finally the reorganisation of the membrane-associated F-actin system. Our work is fundamental for future studies of environmental effects on hypopharyngeal gland morphology and development.}, language = {en} } @misc{VossBlenauWalzetal.2009, author = {Voss, Martin and Blenau, Wolfgang and Walz, Bernd and Baumann, Otto}, title = {V-ATPase deactivation in blowfly salivary glands is mediated by protein phosphatase 2C}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-44360}, year = {2009}, abstract = {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.}, language = {en} } @article{MalinovaMahlowAlseekhetal.2014, author = {Malinova, Irina and Mahlow, Sebastian and Alseekh, Saleh and Orawetz, Tom and Fernie, Alisdair R. and Baumann, Otto and Steup, Martin and Fettke, J{\"o}rg}, title = {Double knockout mutants of arabidopsis grown under normal conditions reveal that the plastidial phosphorylase isozyme participates in transitory starch metabolism}, series = {Plant physiology : an international journal devoted to physiology, biochemistry, cellular and molecular biology, biophysics and environmental biology of plants}, volume = {164}, journal = {Plant physiology : an international journal devoted to physiology, biochemistry, cellular and molecular biology, biophysics and environmental biology of plants}, number = {2}, publisher = {American Society of Plant Physiologists}, address = {Rockville}, issn = {0032-0889}, doi = {10.1104/pp.113.227843}, pages = {907 -- 921}, year = {2014}, abstract = {In leaves of two starch-related single-knockout lines lacking either the cytosolic transglucosidase (also designated as disproportionating enzyme 2, DPE2) or the maltose transporter (MEX1), the activity of the plastidial phosphorylase isozyme (PHS1) is increased. In both mutants, metabolism of starch-derived maltose is impaired but inhibition is effective at different subcellular sites. Two constitutive double knockout mutants were generated (designated as dpe2-1 x phs1a and mex1 x phs1b) both lacking functional PHS1. They reveal that in normally grown plants, the plastidial phosphorylase isozyme participates in transitory starch degradation and that the central carbon metabolism is closely integrated into the entire cell biology. All plants were grown either under continuous illumination or in a light-dark regime. Both double mutants were compromised in growth and, compared with the single knockout plants, possess less average leaf starch when grown in a light-dark regime. Starch and chlorophyll contents decline with leaf age. As revealed by transmission electron microscopy, mesophyll cells degrade chloroplasts, but degradation is not observed in plants grown under continuous illumination. The two double mutants possess similar but not identical phenotypes. When grown in a light-dark regime, mesophyll chloroplasts of dpe2-1 x phs1a contain a single starch granule but under continuous illumination more granules per chloroplast are formed. The other double mutant synthesizes more granules under either growth condition. In continuous light, growth of both double mutants is similar to that of the parental single knockout lines. Metabolite profiles and oligoglucan patterns differ largely in the two double mutants.}, language = {en} } @article{SchwarzeKellingMuelleretal.2012, author = {Schwarze, Thomas and Kelling, Alexandra and M{\"u}ller, Holger and Trautmann, Michael and Klamroth, Tillmann and Baumann, Otto and Strauch, Peter and Holdt, Hans-J{\"u}rgen}, title = {N-2-Pyridinylmethyl-N '-arylmethyl-diaminomaleonitriles: New Highly Selective Chromogenic Chemodosimeters for Copper(II)}, series = {Chemistry - a European journal}, volume = {18}, journal = {Chemistry - a European journal}, number = {34}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0947-6539}, doi = {10.1002/chem.201201731}, pages = {10506 -- 10510}, year = {2012}, language = {en} } @misc{BlenauRotteWitteetal.2009, author = {Blenau, Wolfgang and Rotte, Cathleen and Witte, Jeannine and Baumann, Otto and Walz, Bernd}, title = {Source, topography and excitatory effects of GABAergic innervation in cockroach salivary glands}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-44353}, year = {2009}, abstract = {Cockroach salivary glands are innervated by dopaminergic and serotonergic neurons. Both transmitters elicit saliva secretion. We studied the distribution pattern of neurons containing gamma-aminobutyric acid ( GABA) and their physiological role. Immunofluorescence revealed a GABA-immunoreactive axon that originates within the subesophageal ganglion at the salivary neuron 2 (SN2) and this extends within the salivary duct nerve towards the salivary gland. GABA-positive fibers form a network on most acinar lobules and a dense plexus in the interior of a minor fraction of acinar lobules. Co-staining with anti-synapsin revealed that some putative GABAergic terminals seem to make pre-synaptic contacts with GABA-negative release sites. Many putative GABAergic release sites are at some distance from other synapses and at distance from the acinar tissue. Intracellular recordings from isolated salivary glands have revealed that GABA does not affect the basolateral membrane potential of the acinar cells directly. When applied during salivary duct nerve stimulation, GABA enhances the electrical response of the acinar cells and increases the rates of fluid and protein secretion. The effect on electrical cell responses is mimicked by the GABA(B) receptor agonists baclofen and SKF97541, and blocked by the GABAB receptor antagonists CGP52432 and CGP54626. These findings indicate that GABA has a modulatory role in the control of salivation, acting presynaptically on serotonergic and/or dopaminergic neurotransmission.}, language = {en} } @article{PitzenSanderBaumannetal.2021, author = {Pitzen, Valentin and Sander, Sophia and Baumann, Otto and Gr{\"a}f, Ralph and Meyer, Irene}, title = {Cep192, a novel missing link between the centrosomal core and corona in Dictyostelium amoebae}, series = {Cells : open access journal}, volume = {10}, journal = {Cells : open access journal}, number = {9}, publisher = {MDPI}, address = {Basel}, issn = {2073-4409}, doi = {10.3390/cells10092384}, pages = {19}, year = {2021}, abstract = {The Dictyostelium centrosome is a nucleus-associated body with a diameter of approx. 500 nm. It contains no centrioles but consists of a cylindrical layered core structure surrounded by a microtubule-nucleating corona. At the onset of mitosis, the corona disassembles and the core structure duplicates through growth, splitting, and reorganization of the outer core layers. During the last decades our research group has characterized the majority of the 42 known centrosomal proteins. In this work we focus on the conserved, previously uncharacterized Cep192 protein. We use superresolution expansion microscopy (ExM) to show that Cep192 is a component of the outer core layers. Furthermore, ExM with centrosomal marker proteins nicely mirrored all ultrastructurally known centrosomal substructures. Furthermore, we improved the proximity-dependent biotin identification assay (BioID) by adapting the biotinylase BioID2 for expression in Dictyostelium and applying a knock-in strategy for the expression of BioID2-tagged centrosomal fusion proteins. Thus, we were able to identify various centrosomal Cep192 interaction partners, including CDK5RAP2, which was previously allocated to the inner corona structure, and several core components. Studies employing overexpression of GFP-Cep192 as well as depletion of endogenous Cep192 revealed that Cep192 is a key protein for the recruitment of corona components during centrosome biogenesis and is required to maintain a stable corona structure.}, language = {en} } @article{KruegerSchwarzeBaumannetal.2018, author = {Kr{\"u}ger, Stefanie and Schwarze, Michael and Baumann, Otto and G{\"u}nter, Christina and Bruns, Michael and K{\"u}bel, Christian and Szabo, Dorothee Vinga and Meinusch, Rafael and Bermudez, Veronica de Zea and Taubert, Andreas}, title = {Bombyx mori silk/titania/gold hybrid materials for photocatalytic water splitting}, series = {Beilstein journal of nanotechnology}, volume = {9}, journal = {Beilstein journal of nanotechnology}, publisher = {Beilstein-Institut zur F{\"o}rderung der Chemischen Wissenschaften}, address = {Frankfurt, Main}, issn = {2190-4286}, doi = {10.3762/bjnano.9.21}, pages = {187 -- 204}, year = {2018}, abstract = {The synthesis, structure, and photocatalytic water splitting performance of two new titania (TiO2)/gold(Au)/Bombyx mori silk hybrid materials are reported. All materials are monoliths with diameters of up to ca. 4.5 cm. The materials are macroscopically homogeneous and porous with surface areas between 170 and 210 m(2)/g. The diameter of the TiO2 nanoparticles (NPs) - mainly anatase with a minor fraction of brookite - and the Au NPs are on the order of 5 and 7-18 nm, respectively. Addition of poly(ethylene oxide) to the reaction mixture enables pore size tuning, thus providing access to different materials with different photocatalytic activities. Water splitting experiments using a sunlight simulator and a Xe lamp show that the new hybrid materials are effective water splitting catalysts and produce up to 30 mmol of hydrogen per 24 h. Overall the article demonstrates that the combination of a renewable and robust scaffold such as B. mori silk with a photoactive material provides a promising approach to new monolithic photocatalysts that can easily be recycled and show great potential for application in lightweight devices for green fuel production.}, language = {en} } @misc{KruegerSchwarzeBaumannetal.2018, author = {Kr{\"u}ger, Stefanie and Schwarze, Michael and Baumann, Otto and G{\"u}nter, Christina and Bruns, Michael and K{\"u}bel, Christian and Szab{\´o}, Doroth{\´e}e Vinga and Meinusch, Rafael and de Zea Bermudez, Ver{\´o}nica and Taubert, Andreas}, title = {Bombyx mori silk/titania/gold hybrid materials for photocatalytic water splitting}, series = {Postprints der Universit{\"a}t Potsdam Mathematisch-Naturwissenschaftliche Reihe}, journal = {Postprints der Universit{\"a}t Potsdam Mathematisch-Naturwissenschaftliche Reihe}, number = {581}, issn = {1866-8372}, doi = {10.25932/publishup-42349}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-423499}, pages = {18}, year = {2018}, abstract = {The synthesis, structure, and photocatalytic water splitting performance of two new titania (TiO 2 )/gold(Au)/Bombyx mori silk hybrid materials are reported. All materials are monoliths with diameters of up to ca. 4.5 cm. The materials are macroscopically homogeneous and porous with surface areas between 170 and 210 m 2/g. The diameter of the TiO 2 nanoparticles (NPs) - mainly anatase with a minor fraction of brookite - and the Au NPs are on the order of 5 and 7-18 nm, respectively. Addition of poly(ethylene oxide) to the reaction mixture enables pore size tuning, thus providing access to different materials with different photocatalytic activities. Water splitting experiments using a sunlight simulator and a Xe lamp show that the new hybrid materials are effective water splitting catalysts and produce up to 30 mmol of hydrogen per 24 h. Overall the article demonstrates that the combination of a renewable and robust scaffold such as B. mori silk with a photoactive material provides a promising approach to new monolithic photocatalysts that can easily be recycled and show great potential for application in lightweight devices for green fuel production.}, language = {en} }