Zschüntzsch, Jana

[["dc.bibliographiccitation.firstpage","189"],["dc.bibliographiccitation.journal","Experimental Neurology"],["dc.bibliographiccitation.lastpage","197"],["dc.bibliographiccitation.volume","271"],["dc.contributor.author","Muth, Ingrid E."],["dc.contributor.author","Zschuentzsch, Jana"],["dc.contributor.author","Kleinschnitz, Konstanze"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Balcarek, Peter"],["dc.contributor.author","Schreiber-Katz, Olivia"],["dc.contributor.author","Zierz, Stephan"],["dc.contributor.author","Dalakas, Marinas C."],["dc.contributor.author","Voll, Reinhard E."],["dc.contributor.author","Schmidt, Jens"],["dc.date.accessioned","2018-11-07T09:52:13Z"],["dc.date.available","2018-11-07T09:52:13Z"],["dc.date.issued","2015"],["dc.description.abstract","Inflammation is associated with protein accumulation in IBM, but precise mechanisms are elusive. The \"alarmin\" HMGB1 is upregulated in muscle inflammation. Its receptor RAGE is crucial for S-amyloid-associated neurodegeneration. Relevant signaling via HMGB1/RAGE is expected in IBM pathology. By real-time-PCR, mRNA-expression levels of HMGB1 and RAGE were upregulated in muscle biopsies of patients with IBM and PM, but not in muscular dystrophy or non-myopathic controls. By immunohistochemistry, both molecules displayed the highest signal in IBM, where they distinctly co-localized to intra-fiber accumulations of beta-amyloid and neurofilament/tau. In these fibers, identification of phosphorylated Erk suggested that relevant downstream activation is present upon HMGB1 signaling via RAGE. Protein expressions of HMGB1, RAGE, Erk and phosphorylated Erk were confirmed by Western blot. In a well established cell-culture model for pro-inflammatory cell-stress, exposure of human muscle-cells to 1L-1 beta + IFN-gamma induced cytoplasmic translocation of HMGB1 and subsequent release as evidenced by ELISA. Upregulation of RAGE on the cell surface was demonstrated by immunocytochemistry and flow-cytometry. Recombinant HMGB1 was equally potent as IL-1 beta + IFN-gamma in causing amyloid-accumulation and cell-death, and both were abrogated by the HMGB1-blocker BoxA. The findings strengthen the concept of unique interactions between degenerative and inflammatory mechanisms and suggest that HMGB1/RAGE signaling is a critical pathway in IBM pathology. (C) 2015 Elsevier Inc. All rights reserved."],["dc.description.sponsorship","Association Francaise contre les Myopathies (AFM) [13512, 14952]"],["dc.identifier.doi","10.1016/j.expneurol.2015.05.023"],["dc.identifier.isi","000362627200020"],["dc.identifier.pmid","26048613"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36071"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1090-2430"],["dc.relation.issn","0014-4886"],["dc.title","HMGB1 and RAGE in skeletal muscle inflammation: Implications for protein accumulation in inclusion body myositis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","101433"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Best Practice & Research. Clinical Rheumatology"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Glaubitz, Stefanie"],["dc.contributor.author","Schmidt, Karsten"],["dc.contributor.author","Zschüntzsch, Jana"],["dc.contributor.author","Schmidt, Jens"],["dc.date.accessioned","2020-12-10T14:22:35Z"],["dc.date.available","2020-12-10T14:22:35Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.berh.2019.101433"],["dc.identifier.issn","1521-6942"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71664"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Myalgia in myositis and myopathies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9567"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Merckx, Caroline"],["dc.contributor.author","Zschüntzsch, Jana"],["dc.contributor.author","Meyer, Stefanie"],["dc.contributor.author","Raedt, Robrecht"],["dc.contributor.author","Verschuere, Hanne"],["dc.contributor.author","Schmidt, Jens"],["dc.contributor.author","De Paepe, Boel"],["dc.contributor.author","De Bleecker, Jan L."],["dc.date.accessioned","2022-10-04T10:21:22Z"],["dc.date.available","2022-10-04T10:21:22Z"],["dc.date.issued","2022"],["dc.description.abstract","Duchenne Muscular Dystrophy (DMD) is a debilitating muscle disorder that condemns patients to year-long dependency on glucocorticoids. Chronic glucocorticoid use elicits many unfavourable side-effects without offering satisfying clinical improvement, thus, the search for alternative treatments to alleviate muscle inflammation persists. Taurine, an osmolyte with anti-inflammatory effects, mitigated pathological features in the mdx mouse model for DMD but interfered with murine development. In this study, ectoine is evaluated as an alternative for taurine in vitro in CCL-136 cells and in vivo in the mdx mouse. Pre-treating CCL-136 cells with 0.1 mM taurine and 0.1 mM ectoine prior to exposure with 300 U/mL IFN-γ and 20 ng/mL IL-1β partially attenuated cell death, whilst 100 mM taurine reduced MHC-I protein levels. In vivo, histopathological features of the tibialis anterior in mdx mice were mitigated by ectoine, but not by taurine. Osmolyte treatment significantly reduced mRNA levels of inflammatory disease biomarkers, respectively, CCL2 and SPP1 in ectoine-treated mdx mice, and CCL2, HSPA1A, TNF-α and IL-1β in taurine-treated mdx mice. Functional performance was not improved by osmolyte treatment. Furthermore, ectoine-treated mdx mice exhibited reduced body weight. Our results confirmed beneficial effects of taurine in mdx mice and, for the first time, demonstrated similar and differential effects of ectoine."],["dc.identifier.doi","10.3390/ijms23179567"],["dc.identifier.pii","ijms23179567"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114389"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-600"],["dc.relation.eissn","1422-0067"],["dc.title","Exploring the Therapeutic Potential of Ectoine in Duchenne Muscular Dystrophy: Comparison with Taurine, a Supplement with Known Beneficial Effects in the mdx Mouse"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","224"],["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.lastpage","226"],["dc.bibliographiccitation.volume","210"],["dc.contributor.author","Zhang, Y."],["dc.contributor.author","Zschuentzsch, Jana"],["dc.contributor.author","Schmidt, J."],["dc.contributor.author","Brinkmeier, Heinrich"],["dc.date.accessioned","2018-11-07T09:42:49Z"],["dc.date.available","2018-11-07T09:42:49Z"],["dc.date.issued","2014"],["dc.identifier.isi","000332259900586"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34043"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","Dystrophin deficiency leads to drastic weakness of mdx diaphragm muscle, but has little influence on soleus muscle force"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1102"],["dc.bibliographiccitation.journal","Brain"],["dc.bibliographiccitation.lastpage","1114"],["dc.bibliographiccitation.volume","135"],["dc.contributor.author","Schmidt, Jens"],["dc.contributor.author","Barthel, Konstanze"],["dc.contributor.author","Zschuentzsch, Jana"],["dc.contributor.author","Muth, Ingrid E."],["dc.contributor.author","Swindle, Emily J."],["dc.contributor.author","Hombach, Anja"],["dc.contributor.author","Sehmisch, Stephan"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Luehder, Fred"],["dc.contributor.author","Gold, Ralf"],["dc.contributor.author","Dalakas, Marinas C."],["dc.date.accessioned","2018-11-07T09:11:33Z"],["dc.date.available","2018-11-07T09:11:33Z"],["dc.date.issued","2012"],["dc.description.abstract","Sporadic inclusion body myositis is a severely disabling myopathy. The design of effective treatment strategies is hampered by insufficient understanding of the complex disease pathology. Particularly, the nature of interrelationships between inflammatory and degenerative pathomechanisms in sporadic inclusion body myositis has remained elusive. In Alzheimer's dementia, accumulation of beta-amyloid has been shown to be associated with upregulation of nitric oxide. Using quantitative polymerase chain reaction, an overexpression of inducible nitric oxide synthase was observed in five out of ten patients with sporadic inclusion body myositis, two of eleven with dermatomyositis, three of eight with polymyositis, two of nine with muscular dystrophy and two of ten non-myopathic controls. Immunohistochemistry confirmed protein expression of inducible nitric oxide synthase and demonstrated intracellular nitration of tyrosine, an indicator for intra-fibre production of nitric oxide, in sporadic inclusion body myositis muscle samples, but much less in dermatomyositis or polymyositis, hardly in dystrophic muscle and not in non-myopathic controls. Using fluorescent double-labelling immunohistochemistry, a significant co-localization was observed in sporadic inclusion body myositis muscle between beta-amyloid, thioflavine-S and nitrotyrosine. In primary cultures of human myotubes and in myoblasts, exposure to interleukin-1 beta in combination with interferon-gamma induced a robust upregulation of inducible nitric oxide synthase messenger RNA. Using fluorescent detectors of reactive oxygen species and nitric oxide, dichlorofluorescein and diaminofluorescein, respectively, flow cytometry revealed that interleukin-1 beta combined with interferon-gamma induced intracellular production of nitric oxide, which was associated with necrotic cell death in muscle cells. Intracellular nitration of tyrosine was noted, which partly co-localized with amyloid precursor protein, but not with desmin. Pharmacological inhibition of inducible nitric oxide synthase by 1400W reduced intracellular production of nitric oxide and prevented accumulation of beta-amyloid, nitration of tyrosine as well as cell death inflicted by interleukin-1 beta combined with interferon-gamma. Collectively, these data suggest that, in skeletal muscle, inducible nitric oxide synthase is a central component of interactions between interleukin-1 beta and beta-amyloid, two of the most relevant molecules in sporadic inclusion body myositis. The data further our understanding of the pathology of sporadic inclusion body myositis and may point to novel treatment strategies."],["dc.identifier.doi","10.1093/brain/aws046"],["dc.identifier.isi","000302948700017"],["dc.identifier.pmid","22436237"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26748"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0006-8950"],["dc.title","Nitric oxide stress in sporadic inclusion body myositis muscle fibres: inhibition of inducible nitric oxide synthase prevents interleukin-1 beta-induced accumulation of beta-amyloid and cell death"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4094"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Arthritis & Rheumatism"],["dc.bibliographiccitation.lastpage","4103"],["dc.bibliographiccitation.volume","64"],["dc.contributor.author","Zschuentzsch, Jana"],["dc.contributor.author","Voss, Joachim"],["dc.contributor.author","Creus, Kim"],["dc.contributor.author","Sehmisch, Stephan"],["dc.contributor.author","Raju, Raghavan"],["dc.contributor.author","Dalakas, Marinas C."],["dc.contributor.author","Schmidt, Jens"],["dc.date.accessioned","2018-11-07T09:02:40Z"],["dc.date.available","2018-11-07T09:02:40Z"],["dc.date.issued","2012"],["dc.description.abstract","Objective. In sporadic inclusion body myositis (IBM), inflammation and accumulation of beta-amyloid-associated molecules cause muscle fiber damage. We undertook this study to determine why intravenous immunoglobulin (IVIG) and prednisone are not effective in sporadic IBM despite their effectiveness in other inflammatory myopathies. Methods. Relevant inflammatory and degeneration-associated markers were assessed by quantitative polymerase chain reaction and immunohistochemistry in repeated muscle biopsy specimens from patients with sporadic IBM treated in a controlled study with IVIG and prednisone (n = 5) or with prednisone alone (n = 5). Functional effects were assessed in a muscle cell culture model. Results. In muscle biopsy specimens, messenger RNA (mRNA) expression of the proinflammatory chemokines CXCL9, CCL3, and CCL4 and of the cytokines interferon-gamma (IFN gamma), transforming growth factor beta, interleukin-10 (IL-10), and IL-1 beta was significantly reduced after treatment in both groups. No consistent changes were observed for tumor necrosis factor alpha, IL-6, inducible costimulator (ICOS), its ligand ICOSL, and perforin. Messenger RNA expression of the degeneration-associated molecule ubiquitin and the heat-shock protein alpha B-crystallin was also reduced, but no changes were noted for amyloid precursor protein (APP) or desmin. By immunohistochemistry, a significant down-modulation of chemokines was observed, but not of inducible nitric oxide (NO) synthase, nitrotyrosine, IL-1 beta, APP, and ubiquitin; beta-amyloid was reduced in 6 of 10 patients. Pronounced staining of IgG was observed in the muscle after treatment with IVIG, indicating penetration of infused IgG into the muscle and a possible local effect. In muscle cells exposed to IFN gamma plus IL-1 beta, IgG and/or prednisone downregulated mRNA expression of IL-1 beta 2.5-fold. Accumulation of beta-amyloid, overexpression of alpha B-crystallin, and cell death were prevented. In contrast, NO-associated cell stress remained unchanged. Conclusion. IVIG and prednisone reduce some inflammatory and degenerative molecules in muscle of patients with sporadic IBM and in vitro, but do not sufficiently suppress myotoxic and cell stress mediators such as NO. The data provide an explanation for the resistance of sporadic IBM to immunotherapy and identify markers that may help to design novel treatment strategies."],["dc.identifier.doi","10.1002/art.37692"],["dc.identifier.isi","000311706300033"],["dc.identifier.pmid","22941914"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24739"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0004-3591"],["dc.title","Provision of an Explanation for the Inefficacy of Immunotherapy in Sporadic Inclusion Body Myositis Quantitative Assessment of Inflammation and beta-Amyloid in the Muscle"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Journal of Neuroimmunology"],["dc.bibliographiccitation.volume","275"],["dc.contributor.author","Haas, Christina"],["dc.contributor.author","Zschüntzsch, Jana"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Schmidt, Jens"],["dc.date.accessioned","2018-11-07T09:33:34Z"],["dc.date.available","2018-11-07T09:33:34Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.jneuroim.2014.08.161"],["dc.identifier.isi","000345192100153"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31995"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.eventlocation","Mainz, GERMANY"],["dc.title","Endoplasmic reticulum stress induced by inflammation in skeletal muscle cells is associated with protein accumulation and reduced by methylene blue: Implications for inclusion body myositis"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1933"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Neuroscience Research"],["dc.bibliographiccitation.lastpage","1952"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Prukop, Thomas"],["dc.contributor.author","Wernick, Stephanie"],["dc.contributor.author","Boussicault, Lydie"],["dc.contributor.author","Ewers, David"],["dc.contributor.author","Jäger, Karoline"],["dc.contributor.author","Adam, Julia"],["dc.contributor.author","Winter, Lorenz"],["dc.contributor.author","Quintes, Susanne"],["dc.contributor.author","Linhoff, Lisa"],["dc.contributor.author","Barrantes‐Freer, Alonso"],["dc.contributor.author","Bartl, Michael"],["dc.contributor.author","Czesnik, Dirk"],["dc.contributor.author","Zschüntzsch, Jana"],["dc.contributor.author","Schmidt, Jens"],["dc.contributor.author","Primas, Gwenaël"],["dc.contributor.author","Laffaire, Julien"],["dc.contributor.author","Rinaudo, Philippe"],["dc.contributor.author","Brureau, Anthony"],["dc.contributor.author","Nabirotchkin, Serguei"],["dc.contributor.author","Schwab, Markus H."],["dc.contributor.author","Nave, Klaus‐Armin"],["dc.contributor.author","Hajj, Rodolphe"],["dc.contributor.author","Cohen, Daniel"],["dc.contributor.author","Sereda, Michael W."],["dc.date.accessioned","2021-04-14T08:23:41Z"],["dc.date.available","2021-04-14T08:23:41Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1002/jnr.24679"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81010"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1097-4547"],["dc.relation.issn","0360-4012"],["dc.title","Synergistic PXT3003 therapy uncouples neuromuscular function from dysmyelination in male Charcot–Marie–Tooth disease type 1A (CMT1A) rats"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","9-10"],["dc.bibliographiccitation.journal","Neuromuscular Disorders"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Zschuentzsch, Jana"],["dc.contributor.author","Makosch, Gregor"],["dc.contributor.author","Klinge, Lars"],["dc.contributor.author","Tiburcy, Malte"],["dc.contributor.author","Brinkmeier, Heinrich"],["dc.contributor.author","Liebetan, D."],["dc.contributor.author","Schmidt, J."],["dc.date.accessioned","2018-11-07T08:51:10Z"],["dc.date.available","2018-11-07T08:51:10Z"],["dc.date.issued","2011"],["dc.format.extent","710"],["dc.identifier.doi","10.1016/j.nmd.2011.06.984"],["dc.identifier.isi","000295955900233"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21866"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.publisher.place","Oxford"],["dc.relation.conference","16th International Congress of the World-Muscle-Society"],["dc.relation.eventlocation","Algarve, PORTUGAL"],["dc.relation.issn","0960-8966"],["dc.title","Human IgG improves the performance of mdx mice in voluntary wheel running"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e167"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Neurology Genetics"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Smogavec, Mateja"],["dc.contributor.author","Zschüntzsch, Jana"],["dc.contributor.author","Kress, Wolfram"],["dc.contributor.author","Mohr, Julia"],["dc.contributor.author","Hellen, Peter"],["dc.contributor.author","Zoll, Barbara"],["dc.contributor.author","Pauli, Silke"],["dc.contributor.author","Schmidt, Jens"],["dc.date.accessioned","2020-12-10T18:41:39Z"],["dc.date.available","2020-12-10T18:41:39Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1212/NXG.0000000000000167"],["dc.identifier.eissn","2376-7839"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77641"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Novel fukutin mutations in limb-girdle muscular dystrophy type 2M with childhood onset"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]