Reinert, Jochim

[["dc.bibliographiccitation.firstpage","871"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Alzheimer s Disease"],["dc.bibliographiccitation.lastpage","881"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Reinert, Jochim"],["dc.contributor.author","Martens, Henrik"],["dc.contributor.author","Huettenrauch, Melanie"],["dc.contributor.author","Kolbow, Tekla"],["dc.contributor.author","Lannfelt, Lars"],["dc.contributor.author","Ingelsson, Martin"],["dc.contributor.author","Paetau, Anders"],["dc.contributor.author","Verkkoniemi-Ahola, Auli"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2018-11-07T09:46:32Z"],["dc.date.available","2018-11-07T09:46:32Z"],["dc.date.issued","2014"],["dc.description.abstract","The pathogenesis of Alzheimer's disease (AD) is believed to be closely dependent on deposits of neurotoxic amyloid-beta peptides (A beta), which become abundantly present throughout the central nervous system in advanced stages of the disease. The different A beta peptides existing are generated by subsequent cleavage of the amyloid-beta protein precursor (A beta PP) and may vary in length and differ at their C-terminus. Despite extensive studies on the most prevalent species A beta(40) and A beta(42), A beta peptides with other C-termini such as A beta(38) have not received much attention. In the present study, we used a highly specific and sensitive antibody against A beta(38) to analyze the distribution of this A beta species in cases of sporadic and familial AD, as well as in the brains of a series of established transgenic AD mouse models. We found A beta(38) to be present as vascular deposits in the brains of the majority of sporadic AD cases, whereas it is largely absent in non-demented control cases. A beta(38)-positive extracellular plaques were virtually limited to familial cases. Interestingly we observed A beta(38)-positive plaques not only among familial cases due to A beta PP mutations, but also in cases of familial AD caused by presenilin (PSEN) mutations. Furthermore we demonstrate that A beta(38) deposits in the form of extracellular plaques are common in several AD transgenic mouse models carrying either only A beta PP, or combinations of A beta PP, PSEN1, and tau transgenes."],["dc.identifier.doi","10.3233/JAD-131373"],["dc.identifier.isi","000331842500017"],["dc.identifier.pmid","24305500"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34892"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.title","A beta(38) in the Brains of Patients with Sporadic and Familial Alzheimer's Disease and Transgenic Mouse Models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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.artnumber","24"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Acta Neuropathologica Communications"],["dc.bibliographiccitation.lastpage","12"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Reinert, Jochim"],["dc.contributor.author","Richard, Bernhard C."],["dc.contributor.author","Klafki, Hans W."],["dc.contributor.author","Friedrich, Beate"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Kovacs, Gabor G."],["dc.contributor.author","Ingelsson, Martin"],["dc.contributor.author","Lannfelt, Lars"],["dc.contributor.author","Paetau, Anders"],["dc.contributor.author","Bergquist, Jonas"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2017-09-07T11:44:29Z"],["dc.date.available","2017-09-07T11:44:29Z"],["dc.date.issued","2016"],["dc.description.abstract","In Alzheimer’s disease (AD) a variety of amyloid β-peptides (Aβ) are deposited in the form of extracellular diffuse and neuritic plaques (NP), as well as within the vasculature. The generation of Aβ from its precursor, the amyloid precursor protein (APP), is a highly complex procedure that involves subsequent proteolysis of APP by β- and γ-secretases. Brain accumulation of Aβ due to impaired Aβ degradation and/or altered ratios between the different Aβ species produced is believed to play a pivotal role in AD pathogenesis. While the presence of Aβ40 and Aβ42 in vascular and parenchymal amyloid have been subject of extensive studies, the deposition of carboxyterminal truncated Aβ peptides in AD has not received comparable attention. In the current study, we for the first time demonstrate the immunohistochemical localization of Aβ37 and Aβ39 in human sporadic AD (SAD). Our study further included the analysis of familial AD (FAD) cases carrying the APP mutations KM670/671NL, E693G and I716F, as well as a case of the PSEN1 ΔExon9 mutation. Aβ37 and Aβ39 were found to be widely distributed within the vasculature in the brains of the majority of studied SAD and FAD cases, the latter also presenting considerable amounts of Aβ37 containing NPs. In addition, both peptides were found to be present in extracellular plaques but only scarce within the vasculature in brains of a variety of transgenic AD mouse models. Taken together, our study indicates the importance of C-terminally truncated Aβ in sporadic and familial AD and raises questions about how these species are generated and regulated."],["dc.identifier.doi","10.1186/s40478-016-0294-7"],["dc.identifier.gro","3151681"],["dc.identifier.pmid","26955942"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12971"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8499"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","2051-5960"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Deposition of C-terminally truncated Aβ species Aβ37 and Aβ39 in Alzheimer’s disease and transgenic mouse models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1449"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Acta Neurochirurgica"],["dc.bibliographiccitation.lastpage","1458"],["dc.bibliographiccitation.volume","157"],["dc.contributor.author","Zweifel-Zehnder, Antoinette E."],["dc.contributor.author","Stienen, Martin Nikolaus"],["dc.contributor.author","Chicherio, Christian"],["dc.contributor.author","Studerus-Germann, Aline"],["dc.contributor.author","Blaesi, Stefan"],["dc.contributor.author","Rossi, Stefania"],["dc.contributor.author","Gutbrod, Klemens"],["dc.contributor.author","Schmid, Nicole"],["dc.contributor.author","Beaud, Valerie"],["dc.contributor.author","Mondadori, Christian"],["dc.contributor.author","Brugger, Peter"],["dc.contributor.author","Sacco, Leonardo"],["dc.contributor.author","Mueri, Rene"],["dc.contributor.author","Hildebrandt, Gerhard"],["dc.contributor.author","Fournier, Jean-Yves"],["dc.contributor.author","Keller, Emanuela"],["dc.contributor.author","Regli, Luca"],["dc.contributor.author","Fandino, Javier"],["dc.contributor.author","Mariani, Luigi"],["dc.contributor.author","Raabe, Andreas"],["dc.contributor.author","Daniel, Roy Thomas"],["dc.contributor.author","Reinert, T."],["dc.contributor.author","Robert, Thomas"],["dc.contributor.author","Schatlo, Bawarjan"],["dc.contributor.author","Bijlenga, Philippe"],["dc.contributor.author","Schaller, Karl"],["dc.contributor.author","Monsch, Andreas U."],["dc.date.accessioned","2018-11-07T09:52:48Z"],["dc.date.available","2018-11-07T09:52:48Z"],["dc.date.issued","2015"],["dc.description.abstract","In a high proportion of patients with favorable outcome after aneurysmal subarachnoid hemorrhage (aSAH), neuropsychological deficits, depression, anxiety, and fatigue are responsible for the inability to return to their regular premorbid life and pursue their professional careers. These problems often remain unrecognized, as no recommendations concerning a standardized comprehensive assessment have yet found entry into clinical routines. To establish a nationwide standard concerning a comprehensive assessment after aSAH, representatives of all neuropsychological and neurosurgical departments of those eight Swiss centers treating acute aSAH have agreed on a common protocol. In addition, a battery of questionnaires and neuropsychological tests was selected, optimally suited to the deficits found most prevalent in aSAH patients that was available in different languages and standardized. We propose a baseline inpatient neuropsychological screening using the Montreal Cognitive Assessment (MoCA) between days 14 and 28 after aSAH. In an outpatient setting at 3 and 12 months after bleeding, we recommend a neuropsychological examination, testing all relevant domains including attention, speed of information processing, executive functions, verbal and visual learning/memory, language, visuo-perceptual abilities, and premorbid intelligence. In addition, a detailed assessment capturing anxiety, depression, fatigue, symptoms of frontal lobe affection, and quality of life should be performed. This standardized neuropsychological assessment will lead to a more comprehensive assessment of the patient, facilitate the detection and subsequent treatment of previously unrecognized but relevant impairments, and help to determine the incidence, characteristics, modifiable risk factors, and the clinical course of these impairments after aSAH."],["dc.identifier.doi","10.1007/s00701-015-2480-y"],["dc.identifier.isi","000359862500001"],["dc.identifier.pmid","26179382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36200"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.issn","0942-0940"],["dc.relation.issn","0001-6268"],["dc.title","Call for uniform neuropsychological assessment after aneurysmal subarachnoid hemorrhage: Swiss recommendations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]