Kobe, Fritz

[["dc.bibliographiccitation.firstpage","2915"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","2930"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Kobe, Fritz"],["dc.contributor.author","Guseva, Daria"],["dc.contributor.author","Jensen, Thomas P."],["dc.contributor.author","Wirth, Alexander"],["dc.contributor.author","Renner, Ute"],["dc.contributor.author","Hess, Dietmar"],["dc.contributor.author","Müller, Michael"],["dc.contributor.author","Medrihan, Lucian"],["dc.contributor.author","Zhang, Weiqi"],["dc.contributor.author","Zhang, Mingyue"],["dc.contributor.author","Braun, Katharina"],["dc.contributor.author","Westerholz, Sören"],["dc.contributor.author","Herzog, Andreas"],["dc.contributor.author","Radyushkin, Konstantin"],["dc.contributor.author","El-Kordi, Ahmed"],["dc.contributor.author","Ehrenreich, Hannelore"],["dc.contributor.author","Richter, Diethelm W."],["dc.contributor.author","Rusakov, Dmitri A."],["dc.contributor.author","Ponimaskin, Evgeni"],["dc.date.accessioned","2017-09-07T11:46:22Z"],["dc.date.available","2017-09-07T11:46:22Z"],["dc.date.issued","2012"],["dc.description.abstract","The common neurotransmitter serotonin controls different aspects of early neuronal differentiation, although the underlying mechanisms are poorly understood. Here we report that activation of the serotonin 5-HT7 receptor promotes synaptogenesis and enhances synaptic activity in hippocampal neurons at early postnatal stages. An analysis of Gα12-deficient mice reveals a critical role of G12-protein for 5-HT7 receptor-mediated effects in neurons. In organotypic preparations from the hippocampus of juvenile mice, stimulation of 5-HT7R/G12 signaling potentiates formation of dendritic spines, increases neuronal excitability, and modulates synaptic plasticity. In contrast, in older neuronal preparations, morphogenetic and synaptogenic effects of 5-HT7/G12 signaling are abolished. Moreover, inhibition of 5-HT7 receptor had no effect on synaptic plasticity in hippocampus of adult animals. Expression analysis reveals that the production of 5-HT7 and Gα12-proteins in the hippocampus undergoes strong regulation with a pronounced transient increase during early postnatal stages. Thus, regulated expression of 5-HT7 receptor and Gα12-protein may represent a molecular mechanism by which serotonin specifically modulates formation of initial neuronal networks during early postnatal development."],["dc.identifier.doi","10.1523/JNEUROSCI.2765-11.2012"],["dc.identifier.gro","3150488"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7258"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.title","5-HT₇R/G₁₂ signaling regulates neuronal morphology and function in an age-dependent manner"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","72"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Hepatology"],["dc.bibliographiccitation.lastpage","80"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Tron, Kyrylo"],["dc.contributor.author","Samoylenko, Aantoly"],["dc.contributor.author","Musikowski, Gernot"],["dc.contributor.author","Kobe, Fritz"],["dc.contributor.author","Immenschuh, Stephan"],["dc.contributor.author","Schaper, Fred"],["dc.contributor.author","Ramadori, Giuliano"],["dc.contributor.author","Kietzmann, Thomas"],["dc.date.accessioned","2018-11-07T09:36:49Z"],["dc.date.available","2018-11-07T09:36:49Z"],["dc.date.issued","2006"],["dc.description.abstract","Background/Aims: Heme oxygenase-1 (HO-1) can be induced by various stimuli, one of which is interleukin-6 (IL-6). Therefore, the aim of this study was to elucidate the molecular mechanisms responsible for IL-6-dependent HO-1 induction in the liver. Methods: The IL-6-dependent HO-1 regulation in rat primary hepatocytes and HepG2 hepatoma cells was studied by Northern and Western blot analyses, HO-1 promoter reporter gene assays and EMSA. Results: The HO-1 expression was transcriptionally induced by IL-6 in a time- and dose-dependent manner. Activation of signal transducers and activators of transcription (STAT) factors by the IL-6 receptor was crucial for HO-1 induction. By contrast, negative regulation of HO-1 expression appeared to be mediated through the SH2-domain-containing tyrosine phosphatase-2 (SHP2)/suppressors of cytokine signaling-3 (SOCS3) binding site within the gp130 IL-6 receptor subunit. Among the three putative STAT binding elements (SBE) in the HO-1 promoter, only the distal one was functional and when deleted, the remaining Luc induction was completely obliterated by the phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002. Conclusions: The HO-1 SBE3 mediates HO-1 gene induction by IL-6 mainly via activation of the Jak/STAT pathway. (c) 2006 European Association for the Study of the Liver. Published by Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.jhep.2005.12.019"],["dc.identifier.isi","000238782200010"],["dc.identifier.pmid","16510205"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32701"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0168-8278"],["dc.title","Regulation of rat heme oxygenase-1 expression by interleukin-6 via the Jak/STAT pathway in hepatocytes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5412"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","5423"],["dc.bibliographiccitation.volume","95"],["dc.contributor.author","Salonikidis, Petrus S."],["dc.contributor.author","Zeug, Andre"],["dc.contributor.author","Kobe, Fritz"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.contributor.author","Richter, Diethelm W."],["dc.date.accessioned","2018-11-07T11:08:21Z"],["dc.date.available","2018-11-07T11:08:21Z"],["dc.date.issued","2008"],["dc.description.abstract","Forster resonance energy transfer (FRET)-based biosensors for the quantitative analysis of intracellular signaling, including sensors for monitoring cyclic adenosine monophosphate (cAMP), are of increasing interest. The measurement of the donor/acceptor emission ratio in tandem biosensors excited at the donor excitation wavelength is a commonly used technique. A general problem, however, is that this ratio varies not only with the changes in cAMP concentration but also with the changes of the ionic environment or other factors affecting the folding probability of the fluorophores. Here, we use a spectral FRET analysis on the basis of two excitation wavelengths to obtain a reliable measure of the absolute cAMP concentrations with high temporal and spatial resolution by using an \"exchange protein directly activated by cAMP\". In this approach, FRET analysis is simplified and does not require additional calibration routines. The change in FRET efficiency (E) of the biosensor caused by [cAMP] changes was determined as Delta E=15%, whereas E varies between 35% at low and 20% at high [cAMP], allowing quantitative measurement of cAMP concentration in the range from 150 nM to 15 mu M. The method described is also suitable for other FRET-based biosensors with a 1: 1 donor/acceptor stoichiometry. As a proof of principle, we measured the specially resolved cAMP concentration within living cells and determined the dynamic changes of cAMP levels after stimulation of the Gs-coupled serotonin receptor subtype 7 (5-HT7)."],["dc.identifier.doi","10.1529/biophysj.107.125666"],["dc.identifier.isi","000260999500039"],["dc.identifier.pmid","18708470"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7766"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52756"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biophysical Soc"],["dc.relation.issn","0006-3495"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Quantitative Measurement of cAMP Concentration Using an Exchange Protein Directly Activated by a cAMP-Based FRET-Sensor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8897"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","8907"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.contributor.author","Dityateva, Galina"],["dc.contributor.author","Ruonala, Mika O."],["dc.contributor.author","Fukata, Masaki"],["dc.contributor.author","Fukata, Yuko"],["dc.contributor.author","Kobe, Fritz"],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Delling, Markus"],["dc.contributor.author","Bredt, David S."],["dc.contributor.author","Schachner, Melitta"],["dc.contributor.author","Dityatev, Alexander"],["dc.date.accessioned","2018-11-07T11:10:59Z"],["dc.date.available","2018-11-07T11:10:59Z"],["dc.date.issued","2008"],["dc.description.abstract","During development of the nervous system, short- and long-range signals cooperate to promote axonal growth, guidance, and target innervation. Particularly, a short- range signal transducer, the neural cell adhesion molecule ( NCAM), stimulates neurite outgrowth via mechanisms that require posttranslational modification of NCAM and signaling via receptors to a long-range messenger, the fibroblast growth factor ( FGF). In the present study we further characterized a mechanism which regulates the functional interplay between NCAM and FGF receptor(s). We show that activation of FGF receptor( s) by FGF2 leads to palmitoylation of the two major transmembrane NCAM isoforms, NCAM140 and NCAM180, translocation of NCAM to GM1 ganglioside-containing lipid rafts, and stimulation of neurite outgrowth of hippocampal neurons. Ablation of NCAM, mutation of NCAM140 or NCAM180 palmitoylation sites, or pharmacological suppression of NCAM signaling inhibited FGF2-stimulated neurite outgrowth. Of the 23 members of the aspartate-histidine-histidine-cysteine (DHHC) domain containing proteins, DHHC-7 most strongly stimulated palmitoylation of NCAM, and enzyme activity was enhanced by FGF2. Thus, our study uncovers a molecular mechanism by which a growth factor regulates neuronal morphogenesis via activation of palmitoylation, which in turn modifies subcellular location and thus signaling via an adhesion molecule."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [PO 732/1-2]"],["dc.identifier.doi","10.1523/JNEUROSCI.2171-08.2008"],["dc.identifier.isi","000258890900006"],["dc.identifier.pmid","18768683"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6109"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53327"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Fibroblast growth factor-regulated palmitoylation of the neural cell adhesion molecule determines neuronal morphogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1503"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1516"],["dc.bibliographiccitation.volume","1783"],["dc.contributor.author","Kobe, Fritz"],["dc.contributor.author","Renner, Ute"],["dc.contributor.author","Woehler, Andrew"],["dc.contributor.author","Wlodarczyk, Jakub"],["dc.contributor.author","Papusheva, Ekaterina"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Zeug, Andre"],["dc.contributor.author","Richter, Diethelm W."],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.date.accessioned","2018-11-07T11:12:17Z"],["dc.date.available","2018-11-07T11:12:17Z"],["dc.date.issued","2008"],["dc.description.abstract","In the present study we analyzed the oligomerization state of the serotonin 5-HT1A receptor and studied oligomerization dynamics in living cells. We also investigated the role of receptor palmitoylation in this process. Biochemical analysis performed in neuroblastoma N1E-115 cells demonstrated that both palmitoylated and non-palmitoylated 5-HT1A receptors form homo-oligomers and that the prevalent receptor species at the plasma membrane are dimers. A combination of an acceptor-photobleaching FRET approach with fluorescence lifetime measurements verified the interaction of CFP- and YFP-labeled wild-type as well as acylation-deficient 5-HT1A receptors at the plasma membrane of living cells. Using a novel FRET technique based on the spectral analysis we also confirmed the specific nature of receptor oligomerization. The analysis of oligomerization dynamics revealed that apparent FRET efficiency measured for wild-type oligomers significantly decreased in response to agonist stimulation, and our combined results suggest that this decrease was mediated by accumulation of FRET-negative complexes rather than by dissociation of oligomers to monomers. In contrast, the agonist-mediated decrease of FRET signal was completely abolished in oligomers composed by non-palmitoylated receptor mutants, demonstrating the importance of palmitoylation in modulation of the structure of oligomers. (C) 2008 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2008.02.021"],["dc.identifier.isi","000257641600004"],["dc.identifier.pmid","18381076"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7758"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53629"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0167-4889"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Stimulation- and palmitoylation-dependent changes in oligomeric conformation of serotonin 5-HT1A receptors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","986"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1000"],["dc.bibliographiccitation.volume","94"],["dc.contributor.author","Wlodarczyk, Jakub"],["dc.contributor.author","Woehler, Andrew"],["dc.contributor.author","Kobe, Fritz"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.contributor.author","Zeug, Andre"],["dc.contributor.author","Neher, Erwin"],["dc.date.accessioned","2018-11-07T11:18:28Z"],["dc.date.available","2018-11-07T11:18:28Z"],["dc.date.issued","2008"],["dc.description.abstract","A method for spectral analysis of Forster resonance energy transfer (FRET) signals is presented, taking into consideration both the contributions of unpaired donor and acceptor fluorophores and the in fluence of incomplete labeling of the interacting partners. It is shown that spectral analysis of intermolecular FRET cannot yield accurate values of the Forster energy transfer efficiency E, unless one of the interactors is in large excess and perfectly labeled. Instead, analysis of donor quenching yields a product of the form Ef(d)p(a), where f(d) is the fraction of donor-type molecules participating in donor-acceptor complexes and p(a) is the labeling probability of the acceptor. Similarly, analysis of sensitized emission yields a product involving Ef(a). The analysis of intramolecular FRET (e. g., of tandem constructs) yields the product Ep(a). We use our method to determine these values for a tandem construct of cyan fluorescent protein and yellow fluorescent protein and compare them with those obtained by standard acceptor photobleaching and fluorescence lifetime measurements. We call the method lux-FRET, since it relies on linear unmixing of spectral components."],["dc.identifier.doi","10.1529/biophysj.107.111773"],["dc.identifier.isi","000252243200025"],["dc.identifier.pmid","17921223"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7747"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55040"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","0006-3495"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Analysis of FRET signals in the presence of free donors and acceptors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]