Hülsmann, Swen

[["dc.bibliographiccitation.firstpage","797"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","806"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Gomeza, Jesús"],["dc.contributor.author","Ohno, Koji"],["dc.contributor.author","Hülsmann, Swen"],["dc.contributor.author","Armsen, Wencke"],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Richter, Diethelm W."],["dc.contributor.author","Laube, Bodo"],["dc.contributor.author","Betz, Heinrich"],["dc.date.accessioned","2019-07-10T08:11:51Z"],["dc.date.available","2019-07-10T08:11:51Z"],["dc.date.issued","2003-11-13"],["dc.description.abstract","The glycine transporter subtype 2 (GlyT2) is localized in the axon terminals of glycinergic neurons. Mice deficient in GlyT2 are normal at birth but during the second postnatal week develop a lethal neuromotor deficiency that resembles severe forms of human hyperekplexia (hereditary startle disease) and is characterized by spasticity, tremor, and an inability to right. Histological and immunological analyses failed to reveal anatomical or biochemical abnormalities, but the amplitudes of glycinergic miniature inhibitory currents (mIPSCs) were strikingly reduced in hypoglossal motoneurons and dissociated spinal neurons from GlyT2-deficient mice. Thus, postnatal GlyT2 function is crucial for efficient transmitter loading of synaptic vesicles in glycinergic nerve terminals, and the GlyT2 gene constitutes a candidate disease gene in human hyperekplexia patients."],["dc.identifier.pmid","14622583"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11248"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60808"],["dc.language.iso","en"],["dc.relation.issn","0896-6273"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/3.0"],["dc.subject.mesh","Amino Acid Transport Systems, Neutral"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Animals, Newborn"],["dc.subject.mesh","Brain Stem"],["dc.subject.mesh","Disease Models, Animal"],["dc.subject.mesh","Fetus"],["dc.subject.mesh","Gene Deletion"],["dc.subject.mesh","Genes, Lethal"],["dc.subject.mesh","Glycine"],["dc.subject.mesh","Glycine Plasma Membrane Transport Proteins"],["dc.subject.mesh","Heredodegenerative Disorders, Nervous System"],["dc.subject.mesh","Hypoglossal Nerve"],["dc.subject.mesh","Mice"],["dc.subject.mesh","Mice, Knockout"],["dc.subject.mesh","Motor Neurons"],["dc.subject.mesh","Neural Inhibition"],["dc.subject.mesh","Organ Culture Techniques"],["dc.subject.mesh","Phenotype"],["dc.subject.mesh","Presynaptic Terminals"],["dc.subject.mesh","Startle Reaction"],["dc.subject.mesh","Synaptic Transmission"],["dc.subject.mesh","Synaptic Vesicles"],["dc.title","Deletion of the mouse glycine transporter 2 results in a hyperekplexia phenotype and postnatal lethality."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","342"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular and Cellular Neuroscience"],["dc.bibliographiccitation.lastpage","352"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Latal, A. Tobias"],["dc.contributor.author","Kremer, Thomas"],["dc.contributor.author","Gomeza, Jesus"],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Huelsmann, Swen"],["dc.date.accessioned","2018-11-07T08:40:59Z"],["dc.date.available","2018-11-07T08:40:59Z"],["dc.date.issued","2010"],["dc.description.abstract","Mice deficient for the neuronal glycine transporter subtype 2 (GlyT2) die during the second postnatal week after developing neuromotor deficiencies, which resembles severe forms of human hyperekplexia. This phenotype has been attributed to a dramatic reduction in glycinergic neurotransmission. In the present study we analyzed the development of GABAergic and glycinergic synaptic transmission in GlyT2-knockout mice during early postnatal life. Anti-glycine immunohistochemistry in spinal cord and brainstem slices and whole-cell voltage-clamp recordings of glycinergic inhibitory postsynaptic currents (IPSCs) from hypoglossal motoneurons revealed strikingly reduced levels of synaptic glycine already at birth. Since GABA and glycine use the same vesicular inhibitory amino acid transporter (VIAAT or VGAT) we also analysed GABAergic neurotransmission. No increase of GABA immunoreactivity was observed in the spinal cord and brainstem of GlyT2(-/-) mice at any stage of postnatal development. Correspondingly no up-regulation of GABAergic IPSCs was detected in GlyT2(-/-) hypoglossal motoneurons. These data suggest that in the first postnatal week, loss of the glycine transporter 2 is neither compensated by glycine de-novo synthesis nor by up-regulation of the GABAergic transmission in GlyT2(-/-) mice. (C) 2010 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.mcn.2010.04.005"],["dc.identifier.isi","000279525600004"],["dc.identifier.pmid","20447457"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19369"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1044-7431"],["dc.title","Development of synaptic inhibition in glycine transporter 2 deficient mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0129934"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Besser, Stefanie"],["dc.contributor.author","Sicker, Marit"],["dc.contributor.author","Marx, Grit"],["dc.contributor.author","Winkler, Ulrike"],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Huelsmann, Swen"],["dc.contributor.author","Hirrlinger, Johannes"],["dc.date.accessioned","2018-11-07T09:55:52Z"],["dc.date.available","2018-11-07T09:55:52Z"],["dc.date.issued","2015"],["dc.description.abstract","GABAergic inhibitory neurons are a large population of neurons in the central nervous system (CNS) of mammals and crucially contribute to the function of the circuitry of the brain. To identify specific cell types and investigate their functions labelling of cell populations by transgenic expression of fluorescent proteins is a powerful approach. While a number of mouse lines expressing the green fluorescent protein (GFP) in different subpopulations of GABAergic cells are available, GFP expressing mouse lines are not suitable for either crossbreeding to other mouse lines expressing GFP in other cell types or for Ca2+-imaging using the superior green Ca2+-indicator dyes. Therefore, we have generated a novel transgenic mouse line expressing the red fluorescent protein tdTomato in GABAergic neurons using a bacterial artificial chromosome based strategy and inserting the tdTomato open reading frame at the start codon within exon 1 of the GAD2 gene encoding glutamic acid decarboxylase 65 (GAD65). TdTomato expression was observed in all expected brain regions; however, the fluorescence intensity was highest in the olfactory bulb and the striatum. Robust expression was also observed in cortical and hippocampal neurons, Purkinje cells in the cerebellum, amacrine cells in the retina as well as in cells migrating along the rostral migratory stream. In cortex, hippocampus, olfactory bulb and brainstem, 80% to 90% of neurons expressing endogenous GAD65 also expressed the fluorescent protein. Moreover, almost all tdTomato-expressing cells coexpressed GAD65, indicating that indeed only GABAergic neurons are labelled by tdTomato expression. This mouse line with its unique spectral properties for labelling GABAergic neurons will therefore be a valuable new tool for research addressing this fascinating cell type."],["dc.description.sponsorship","\"Deutsche Forschungsgemeinschaft\" (DFG) [HI1414/2-1, HU797/7-1]"],["dc.identifier.doi","10.1371/journal.pone.0129934"],["dc.identifier.isi","000356329900114"],["dc.identifier.pmid","26076353"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11956"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36843"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","A Transgenic Mouse Line Expressing the Red Fluorescent Protein tdTomato in GABAergic Neurons"],["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","1"],["dc.bibliographiccitation.journal","Brain Structure and Function"],["dc.bibliographiccitation.lastpage","26"],["dc.contributor.author","Rahman, Jamilur"],["dc.contributor.author","Besser, Stefanie"],["dc.contributor.author","Schnell, Christian"],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Hirrlinger, Johannes"],["dc.contributor.author","Wojcik, Sonja M."],["dc.contributor.author","Hülsmann, Swen"],["dc.date.accessioned","2019-07-09T11:41:21Z"],["dc.date.available","2019-07-09T11:41:21Z"],["dc.date.issued","2014"],["dc.description.abstract","Both glycinergic and GABAergic neurons require the vesicular inhibitory amino acid transporter (VIAAT) for synaptic vesicle filling. Presynaptic GABA concentrations are determined by the GABA synthesizing enzymes glutamate decarboxylase (GAD)65 and GAD67, whereas the presynaptic glycine content depends on the plasma membrane glycine transporter 2 (GlyT2). Although severely impaired, glycinergic transmission is not completely absent in GlyT2-knockout mice, suggesting that other routes of glycine uptake or de novo synthesis of glycine exist in presynaptic terminals. To investigate the consequences of a complete loss of glycinergic transmission, we generated a mouse line with a conditional ablation of VIAAT in glycinergic neurons by crossing mice with loxP-flanked VIAAT alleles with a GlyT2-Cre transgenic mouse line. Interestingly, conditional VIAAT knockout (VIAAT cKO) mice were not viable at birth. In addition to the dominant respiratory failure, VIAAT cKO showed an umbilical hernia and a cleft palate. Immunohistochemistry revealed an almost complete depletion of VIAAT in the brainstem. Electrophysiology revealed the absence of both spontaneous glycinergic and GABAergic inhibitory postsynaptic currents (IPSCs) from hypoglossal motoneurons. Our results demonstrate that the deletion of VIAAT in GlyT2-Cre expressing neurons also strongly affects GABAergic transmission and suggest a large overlap of the glycinergic and the GABAergic neuron population during early development in the caudal parts of the brain."],["dc.identifier.doi","10.1007/s00429-014-0829-2"],["dc.identifier.pmid","25027639"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11988"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58409"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Genetic ablation of VIAAT in glycinergic neurons causes a severe respiratory phenotype and perinatal death"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Cellular Neuroscience"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Hirrlinger, Johannes"],["dc.contributor.author","Marx, Grit"],["dc.contributor.author","Besser, Stefanie"],["dc.contributor.author","Sicker, Marit"],["dc.contributor.author","Köhler, Susanne"],["dc.contributor.author","Hirrlinger, Petra G."],["dc.contributor.author","Wojcik, Sonja M."],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Winkler, Ulrike"],["dc.contributor.author","Hülsmann, Swen"],["dc.date.accessioned","2020-12-10T18:44:31Z"],["dc.date.available","2020-12-10T18:44:31Z"],["dc.date.issued","2019"],["dc.description.abstract","Inhibitory neurons crucially contribute to shaping the breathing rhythm in the brain stem. These neurons use GABA or glycine as neurotransmitter; or co-release GABA and glycine. However, the developmental relationship between GABAergic, glycinergic and cotransmitting neurons, and the functional relevance of cotransmitting neurons has remained enigmatic. Transgenic mice expressing fluorescent markers or the split-Cre system in inhibitory neurons were developed to track the three different interneuron phenotypes. During late embryonic development, the majority of inhibitory neurons in the ventrolateral medulla are cotransmitting cells, most of which differentiate into GABAergic and glycinergic neurons around birth and around postnatal day 4, respectively. Functional inactivation of cotransmitting neurons revealed an increase of the number of respiratory pauses, the cycle-by-cycle variability, and the overall variability of breathing. In summary, the majority of cotransmitting neurons differentiate into GABAergic or glycinergic neurons within the first 2 weeks after birth and these neurons contribute to fine-tuning of the breathing pattern."],["dc.identifier.doi","10.3389/fncel.2019.00517"],["dc.identifier.eissn","1662-5102"],["dc.identifier.pmid","31803026"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17103"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78488"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1662-5102"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","GABA-Glycine Cotransmitting Neurons in the Ventrolateral Medulla: Development and Functional Relevance for Breathing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2561"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","23"],["dc.contributor.affiliation","Eulenburg, Volker; 1Department for Anesthesiology and Intensive Care, Faculty of Medicine, University of Leipzig, Liebigstraße 20, D-04103 Leipzig, Germany"],["dc.contributor.affiliation","Hülsmann, Swen; 2Department for Anesthesiology, University Medical Center, Georg-August University, Humboldtallee 23, D-37073 Göttingen, Germany"],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Hülsmann, Swen"],["dc.date.accessioned","2022-04-01T10:03:25Z"],["dc.date.available","2022-04-01T10:03:25Z"],["dc.date.issued","2022"],["dc.date.updated","2022-09-03T20:07:06Z"],["dc.description.abstract","In addition to being involved in protein biosynthesis and metabolism, the amino acid glycine is the most important inhibitory neurotransmitter in caudal regions of the brain. These functions require a tight regulation of glycine concentration not only in the synaptic cleft, but also in various intracellular and extracellular compartments. This is achieved not only by confining the synthesis and degradation of glycine predominantly to the mitochondria, but also by the action of high-affinity large-capacity glycine transporters that mediate the transport of glycine across the membranes of presynaptic terminals or glial cells surrounding the synapses. Although most cells at glycine-dependent synapses express more than one transporter with high affinity for glycine, their synergistic functional interaction is only poorly understood. In this review, we summarize our current knowledge of the two high-affinity transporters for glycine, the sodium-dependent glycine transporters 1 (GlyT1; SLC6A9) and 2 (GlyT2; SLC6A5) and the alanine–serine–cysteine-1 transporter (Asc-1; SLC7A10)."],["dc.identifier.doi","10.3390/ijms23052561"],["dc.identifier.pii","ijms23052561"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/106162"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1422-0067"],["dc.rights","CC BY 4.0"],["dc.title","Synergistic Control of Transmitter Turnover at Glycinergic Synapses by GlyT1, GlyT2, and ASC-1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3888"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","3899"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Kubota, Hisahiko"],["dc.contributor.author","Retiounskaia, Marina"],["dc.contributor.author","Harvey, Robert J."],["dc.contributor.author","Harvey, Kirsten"],["dc.contributor.author","O'Sullivan, Gregory A."],["dc.contributor.author","Laube, Bodo"],["dc.contributor.author","Huelsmann, Swen"],["dc.contributor.author","Geiger, Joerg R. P."],["dc.contributor.author","Betz, Heinrich"],["dc.date.accessioned","2018-11-07T10:58:38Z"],["dc.date.available","2018-11-07T10:58:38Z"],["dc.date.issued","2007"],["dc.description.abstract","Collybistin (Cb) is a brain-specific guanine nucleotide exchange factor that has been implicated in plasma membrane targeting of the postsynaptic scaffolding protein gephyrin found at glycinergic and GABAergic synapses. Here we show that Cb-deficient mice display a region-specific loss of postsynaptic gephyrin and GABA(A) receptor clusters in the hippocampus and the basolateral amygdala. Cb deficiency is accompanied by significant changes in hippocampal synaptic plasticity, due to reduced dendritic GABAergic inhibition. Long-term potentiation is enhanced, and long-term depression reduced, in Cb-deficient hippocampal slices. Consistent with the anatomical and electro-physiological findings, the animals show increased levels of anxiety and impaired spatial learning. Together, our data indicate that Cb is essential for gephyrin-dependent clustering of a specific set of GABA(A) receptors, but not required for glycine receptor postsynaptic localization."],["dc.description.sponsorship","Medical Research Council [G0601585, G0501258]"],["dc.identifier.doi","10.1038/sj.emboj.7601819"],["dc.identifier.isi","000249691800002"],["dc.identifier.pmid","17690689"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50510"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","Impaired GABAergic transmission and altered hippocampal synaptic plasticity in collybistin-deficient mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2019"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Hülsmann, Swen; \t\t \r\n\t\t Department for Anesthesiology, University Medical Center, Georg-August University, Humboldtallee 23, D-37073 Göttingen, Germany, shuelsm2@uni-goettingen.de"],["dc.contributor.affiliation","Hagos, Liya; \t\t \r\n\t\t Department for Anesthesiology, University Medical Center, Georg-August University, Humboldtallee 23, D-37073 Göttingen, Germany, liya.hagos@stud.uni-goettingen.de"],["dc.contributor.affiliation","Eulenburg, Volker; \t\t \r\n\t\t Department for Anesthesiology and Intensive Care, Faculty of Medicine, University of Leipzig, Liebigstraße 20, D-04103 Leipzig, Germany, Volker.Eulenburg@medizin.uni-leipzig.de"],["dc.contributor.affiliation","Hirrlinger, Johannes; \t\t \r\n\t\t Carl-Ludwig-Institute for Physiology, Faculty of Medicine, University of Leipzig, Liebigstr. 27, D-04103 Leipzig, Germany, johannes.hirrlinger@medizin.uni-leipzig.de\t\t \r\n\t\t Department of Neurogenetics, Max-Planck-Institute of Experimental Medicine, Hermann-Rein-Str. 3, D-37075 Göttingen, Germany, johannes.hirrlinger@medizin.uni-leipzig.de"],["dc.contributor.author","Hülsmann, Swen"],["dc.contributor.author","Hagos, Liya"],["dc.contributor.author","Eulenburg, Volker"],["dc.contributor.author","Hirrlinger, Johannes"],["dc.date.accessioned","2021-04-14T08:27:54Z"],["dc.date.available","2021-04-14T08:27:54Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-05T10:12:20Z"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/ijms22042019"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82444"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1422-0067"],["dc.relation.orgunit","Klinik für Anästhesiologie"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Inspiratory Off-Switch Mediated by Optogenetic Activation of Inhibitory Neurons in the preBötzinger Complex In Vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]