Dietz, Birgit

[["dc.bibliographiccitation.firstpage","207"],["dc.bibliographiccitation.journal","Neuroscience"],["dc.bibliographiccitation.lastpage","222"],["dc.bibliographiccitation.volume","261"],["dc.contributor.author","Witte, M."],["dc.contributor.author","Reinert, T."],["dc.contributor.author","Dietz, B."],["dc.contributor.author","Nerlich, J."],["dc.contributor.author","Ruebsamen, Rudolf"],["dc.contributor.author","Milenkovic, I."],["dc.date.accessioned","2018-11-07T09:42:39Z"],["dc.date.available","2018-11-07T09:42:39Z"],["dc.date.issued","2014"],["dc.description.abstract","Precise regulation of the chloride homeostasis crucially determines the action of inhibitory transmitters GABA and glycine and thereby endows neurons or even discrete neuronal compartments with distinct physiological responses to the same transmitters. In mammals, the signaling mediated by GABAA/glycine receptors shifts during early postnatal life from depolarization to hyperpolarization, due to delayed maturation of the chloride homeostasis system. While the activity of the secondary active, K+-Cl- -extruding cotransporter KCC2, renders GABA/glycine hyperpolarizing in auditory brainstem nuclei of altricial rodents, the mechanisms contributing to the initially depolarizing transmembrane gradient for Cl- in respective neurons remained unknown. Here we used gramicidin-perforated patch recordings, non-invasive Cl- and Ca2+ imaging, and immunohistochemistry to identify the Cl- -loading transporter that renders depolarizing effects of GABA/glycine in early postnatal life of spherical bushy cells in the cochlear nucleus of gerbil. Our data identify the 1Na +: 1K +: 2Cl(-) cotransporter 1 (NKCC1) as the major Cl- -loader responsible for depolarizing action of GABA/glycine at postnatal days 3-5 (P3-5). Extracellular GABA/muscimol elicited calcium signaling through R-, L-, and T-type channels, which was dependent on bumetanideand [Na+](e)-sensitive Cl- accumulation. The \"adult like', low intracellular Cl- concentration is established during the second postnatal week, through a mechanism engaging the NKCC1-down regulation between P5 and P15 and ongoing KCC2-mediated Cl- -extrusion. (C) 2013 IBRO. Published by Elsevier Ltd. All rights reserved."],["dc.description.sponsorship","DFG Grant [954/2-1, MI 954/1-2, RU 390/19-1, GRK 1097]"],["dc.identifier.doi","10.1016/j.neuroscience.2013.12.050"],["dc.identifier.isi","000331095400020"],["dc.identifier.pmid","24388924"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34006"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.relation.issn","1873-7544"],["dc.relation.issn","0306-4522"],["dc.title","DEPOLARIZING CHLORIDE GRADIENT IN DEVELOPING COCHLEAR NUCLEUS NEURONS: UNDERLYING MECHANISM AND IMPLICATION FOR CALCIUM SIGNALING"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","61"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Brain Research"],["dc.bibliographiccitation.lastpage","66"],["dc.bibliographiccitation.volume","1082"],["dc.contributor.author","Dietz, Gunnar P. H."],["dc.contributor.author","Valbuena, Paola C."],["dc.contributor.author","Dietz, Birgit"],["dc.contributor.author","Meuer, Katrin"],["dc.contributor.author","Müller, Patrick"],["dc.contributor.author","Weishaupt, Jochen H."],["dc.contributor.author","Bähr, Mathias"],["dc.date.accessioned","2017-09-07T11:53:10Z"],["dc.date.available","2017-09-07T11:53:10Z"],["dc.date.issued","2006"],["dc.description.abstract","Glial-cell-line-derived neurotrophic factor (GDNF) promotes mesencephalic dopaminergic neuronal survival in several in vitro and in vivo models. As the demise of dopaminergic neurons is the cause for Parkinson's disease (PD) symptoms, GDNF is a promising agent for its treatment However, this neurotrophin is unable to cross the blood-brain barrier, which has complicated its clinical use. Therefore, ways to deliver GDNF into the central nervous system in an effective manner are needed. The HIV-1-Tat-derived cell-penetrating peptide (CPP) provides a means to deliver fusion proteins into the brain. We generated a fusion protein between the 11 amino acid CPP of Tat and the rat GDNF mature protein to deliver GDNF across the blood-brain barrier. We showed previously that Tat-GDNF enhances the neuroprotective effect of GDNF in in vivo models for nerve trauma and ischemia. Here, we tested its effect in a subchronic scheme of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) application into the mouse as a model for PD to evaluate the effect of Tat-GDNF fusion protein in dopaminergic neuron survival. We showed that the fusion protein did indeed reach the dopaminergic neurons. However, the in vivo application of Tat-GDNF did not provide neuroprotection of dopaminergic neurons, as revealed by immunohistochemistry and counting of the number of tyrosine-hydroxylase-immunoreactive neurons in the substantia nigra pars compacta. Possibly, GDNF does protect nigro-striatal projections of those neurons that survive MPTP treatment but does not increase the number of surviving dopaminergic neurons. A concomitant treatment of Tat-GDNF with an anti-apoptotic Tat-fusion protein might be beneficial. (c) 2006 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.brainres.2006.01.083"],["dc.identifier.gro","3143709"],["dc.identifier.isi","000236931400007"],["dc.identifier.pmid","16703672"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1253"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-8993"],["dc.subject","Cell-penetrating peptide (CPP); Protein transduction domain (PTD); Blood–brain barrier; Neuroprotection; MPTP mouse model"],["dc.title","Application of a blood-brain-barrier-penetrating form of GDNF in a mouse model for Parkinson's disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","117"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Brain Research Bulletin"],["dc.bibliographiccitation.lastpage","123"],["dc.bibliographiccitation.volume","70"],["dc.contributor.author","Dietz, G. P. H."],["dc.contributor.author","Dietz, B."],["dc.contributor.author","Bähr, M."],["dc.date.accessioned","2017-09-07T11:52:40Z"],["dc.date.available","2017-09-07T11:52:40Z"],["dc.date.issued","2006"],["dc.description.abstract","The Bcl-2 family of proteins has been characterized as a key regulator of cell death programs. In addition, these proteins also play important roles in cellular differentiation, such as axonal growth. The role of Bcl-2 family members on axonal regeneration and neurite extension has been controversial so far. Here, we examine the influence of Bcl-x(L) on axonal regeneration from adult retina explants in vitro. We delivered recombinant Bcl-x(L) into retinal tissue, mediated by the Tat-protein transduction domain, and observed its effect on retinal axon extension. We found that Bcl-xL increased the number of regenerating neurites, but did not increase their length. Our results indicate that Bcl-x(L) stimulates axonal initiation but not axonal elongation after crush injury to retinal explants, without altering the number of surviving neurons. (c) 2006 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.brainresbull.2006.03.022"],["dc.identifier.gro","3143671"],["dc.identifier.isi","000238866200002"],["dc.identifier.pmid","16782502"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1210"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0361-9230"],["dc.title","Bcl-XL increases axonal numbers but not axonal elongation from rat retinal explants"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","757"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","765"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Dietz, G. P. H."],["dc.contributor.author","Stockhausen (née Peters), K. V."],["dc.contributor.author","Dietz, B."],["dc.contributor.author","Falkenburger, B. H."],["dc.contributor.author","Valbuena, P."],["dc.contributor.author","Opazo, F."],["dc.contributor.author","Lingor, P."],["dc.contributor.author","Meuer, K."],["dc.contributor.author","Weishaupt, J. H."],["dc.contributor.author","Schulz, J. B."],["dc.contributor.author","Bähr, M."],["dc.date.accessioned","2017-09-07T11:48:48Z"],["dc.date.available","2017-09-07T11:48:48Z"],["dc.date.issued","2008"],["dc.description.abstract","The anti-apoptotic Bcl-x(L) is a promising agent to prevent neurodegeneration in Parkinson's disease, which is characterized by a demise of dopaminergic neurons. We linked Bcl-x(L) to a peptide that allows its delivery across biological membranes and the blood-brain barrier. We tested the fusion protein in two models of Parkinson's Disease. Cell-permeable Bcl-x(L) protected neuroblastoma cells from the selective neurotoxin 1-methyl-4-phenylpyridinium. Furthermore, its systemic application in aged mice protected dopaminergic neurons following administration of MPTP as revealed by counting of tyrosine hydroxylase-immunoreactive neurons in the substantia nigra pars compacta. Hence, we present that a cell-permeable form of an anti-apoptotic protein can be delivered to CNS neurons through its systemic application, and we provide the proof that the delivery of this protein to the CNS neurons effectively prevents neuronal cell death in models of chronic neurodegenerative diseases."],["dc.identifier.doi","10.1111/j.1471-4159.2007.05028.x"],["dc.identifier.gro","3143353"],["dc.identifier.isi","000252322600015"],["dc.identifier.pmid","17995935"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/858"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0022-3042"],["dc.title","Membrane-permeable Bcl-x(L) prevents MPTP-induced dopaminergic neuronal loss in the substantia nigra"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","136"],["dc.bibliographiccitation.journal","Brain Research"],["dc.bibliographiccitation.lastpage","141"],["dc.bibliographiccitation.volume","1164"],["dc.contributor.author","Dietz, G. P. H."],["dc.contributor.author","Dietz, B."],["dc.contributor.author","Bähr, M."],["dc.date.accessioned","2017-09-07T11:49:26Z"],["dc.date.available","2017-09-07T11:49:26Z"],["dc.date.issued","2007"],["dc.description.abstract","Neuronal death can take on many different forms, from well-defined apoptosis to caspase-independent processes. While members of the Bcl-2 family of intracellular proteins are known to be involved in classic apoptotic cascades, their role in necrosis has been less well defined. Here, we applied a cell-permeable form of the anti-apoptotic Bcl-2 family member Bcl-x(L) on glutamate-treated rat primary cerebellar granule neurons to test its effect on neuronal survival. Bcl-x(L) inhibited the late phase of cell death, when caspases are activated, but it did not inhibit the early, caspase-independent phase of cell death. These different phases of cell death following glutamate treatment have not been taken into account in many earlier reports either supporting or refuting an involvement of Bcl-2 family members in excitotoxic cell death. Our results suggest that under our experimental conditions, Bcl-x(L) inhibits caspase-dependent apoptosis, but not caspase-independent neuronal death. (c) 2007 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.brainres.2007.06.025"],["dc.identifier.gro","3143451"],["dc.identifier.isi","000249321900015"],["dc.identifier.pmid","17644076"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/966"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-8993"],["dc.subject","Necrosis model; Apoptosis; Cell-penetrating peptide; Neurodegeneration; Cerebellar granule neuron; Protein transduction domain"],["dc.title","Bcl-X-L protects cerebellar granule neurons against the late phase, but not against the early phase of glutamate-induced cell death"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]