Miosge, Nicolai

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Investigative Dermatology"],["dc.bibliographiccitation.volume","125"],["dc.contributor.author","Baranowsky, A."],["dc.contributor.author","Mokkapati, S."],["dc.contributor.author","Wickenhauser, C."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Krieg, Thomas"],["dc.contributor.author","Nischt, R."],["dc.date.accessioned","2018-11-07T10:56:16Z"],["dc.date.available","2018-11-07T10:56:16Z"],["dc.date.issued","2005"],["dc.format.extent","A17"],["dc.identifier.isi","000231862600097"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49975"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.publisher.place","Oxford"],["dc.relation.conference","35th Annual Meeting of the European-Society-for-Dermatological-Research"],["dc.relation.eventlocation","Tubingen, GERMANY"],["dc.relation.issn","0022-202X"],["dc.title","Role of the basement membrane proteins nidogen-1 and-2 for skin physiology and pathology"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1375"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Clinical Oral Investigations"],["dc.bibliographiccitation.lastpage","1384"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Batschkus, Sarah"],["dc.contributor.author","Cingoez, Goekhan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Kirschneck, Christian"],["dc.contributor.author","Meyer-Marcotty, Philipp"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2020-12-10T14:11:03Z"],["dc.date.available","2020-12-10T14:11:03Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1007/s00784-017-2213-0"],["dc.identifier.eissn","1436-3771"],["dc.identifier.issn","1432-6981"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70949"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A new albumin-depletion strategy improves proteomic research of gingival crevicular fluid from periodontitis patients"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","482"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Pathology"],["dc.bibliographiccitation.lastpage","494"],["dc.bibliographiccitation.volume","228"],["dc.contributor.author","Ryu, M. I."],["dc.contributor.author","Migliorini, Adriana"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Gross, Oliver"],["dc.contributor.author","Shankland, Stuart"],["dc.contributor.author","Brinkkoetter, Paul T."],["dc.contributor.author","Hagmann, Henning"],["dc.contributor.author","Romagnani, Paola"],["dc.contributor.author","Liapis, Helen"],["dc.contributor.author","Anders, Hans-Joachim"],["dc.date.accessioned","2018-11-07T09:02:32Z"],["dc.date.available","2018-11-07T09:02:32Z"],["dc.date.issued","2012"],["dc.description.abstract","Glomerular crescents are most common in rapidly progressive glomerulonephritis but also occur in noninflammatory chronic glomerulopathies; thus, factors other than inflammation should trigger crescent formation, eg vascular damage and plasma leakage. Here we report that Alport nephropathy in Col4A3-deficient Sv129 mice is complicated by diffuse and global crescent formation in which proliferating parietal epithelial cells are the predominant cell type. Laminin staining and transmission and acellular scanning electron microscopy of acellular glomeruli documented disruptions and progressive disintegration of the glomerular basement membrane in Col4A3-deficient mice. FITC-dextran perfusion further revealed vascular leakage from glomerular capillaries into Bowman's space, further documented by fibrin deposits in the segmental crescents. Its pathogenic role was validated by showing that the fibrinolytic activity of recombinant urokinase partially prevented crescent formation. In addition, in vitro studies confirmed an additional mitogenic potential of serum on murine and human parietal epithelial cells. Furthermore, loss of parietal cell polarity and unpolarized secretion of extracellular matrix components were evident within fibrocellular crescents. Among 665 human Alport nephropathy biopsies, crescent formation was noted in 0.4%. We conclude that glomerular vascular injury and GBM breaks cause plasma leakage which triggers a wound healing programme involving the proliferation of parietal cells and their loss of polarity. This process can trigger cellular and fibrocellular crescent formation even in the absence of cellular inflammation and rupture of the Bowman's capsule. Copyright (C) 2012 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd."],["dc.identifier.doi","10.1002/path.4046"],["dc.identifier.isi","000313949800007"],["dc.identifier.pmid","22553158"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24705"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0022-3417"],["dc.title","Plasma leakage through glomerular basement membrane ruptures triggers the proliferation of parietal epithelial cells and crescent formation in non-inflammatory glomerular injury"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1691"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","1699"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Ko, Y. P."],["dc.contributor.author","Kobbe, B."],["dc.contributor.author","Nicolae, C."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Paulsson, M."],["dc.contributor.author","Wagener, R."],["dc.contributor.author","Aszodi, A."],["dc.date.accessioned","2018-11-07T10:51:30Z"],["dc.date.available","2018-11-07T10:51:30Z"],["dc.date.issued","2004"],["dc.description.abstract","Matrilin-3 belongs to the matrilin family of extracellular matrix (ECM) proteins and is primarily expressed in cartilage. Mutations in the gene encoding human matrilin-3 (MATN-3) lead to autosomal dominant skeletal disorders, such as multiple epiphyseal dysplasia (MED), which is characterized by short stature and early-onset osteoarthritis, and bilateral hereditary microepiphyseal dysplasia, a variant form of MED characterized by pain in the hip and knee joints. To assess the function of matrilin-3 during skeletal development, we have generated Matn-3 null mice. Homozygous mutant mice appear normal, are fertile, and show no obvious skeletal malformations. Histological and ultrastructural analyses reveal endochondral bone formation indistinguishable from that of wild-type animals. Northern blot, immunohistochemical, and biochemical analyses indicated no compensatory upregulation of any other member of the matrilin family. Altogether, our findings suggest functional redundancy among matrilins and demonstrate that the phenotypes of MED disorders are not caused by the absence of matrilin-3 in cartilage ECM."],["dc.identifier.doi","10.1128/MCB.24.4.1691-1699.2004"],["dc.identifier.isi","000188744000023"],["dc.identifier.pmid","14749384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48907"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","Matrilin-3 is dispensable for mouse skeletal growth and development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","67"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Matrix Biology"],["dc.bibliographiccitation.lastpage","85"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Schmitz, Markus"],["dc.contributor.author","Niehoff, Anja"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Smyth, Neil"],["dc.contributor.author","Paulsson, Mats"],["dc.contributor.author","Zaucke, Frank"],["dc.date.accessioned","2018-11-07T11:17:51Z"],["dc.date.available","2018-11-07T11:17:51Z"],["dc.date.issued","2008"],["dc.description.abstract","In humans, mutations in cartilage oligomeric matrix protein (COMP) cause autosomal dominantly inherited skeletal dysplasias. We have generated transgenic mouse lines to study the role of mutant D469 Delta COMP in the pathogenesis of pseudoachondroplasia. Biochemical characterization of cartilage tissue demonstrated that transgenic and endogenous COMP subunits were able to form mixed, pentameric molecules in vivo. Mutant COMP was more difficult to extract than the wildtype protein, suggesting an altered anchorage within the matrix. Although both transgenic wildtype and mutant COMP were detected throughout the growth plate, mutant molecules were restricted to the pericellular matrix while wildtype COMP showed a uniform distribution throughout the extracellular matrix. Mice expressing the mutant transgene showed a slight gender specific growth retardation. In mutant animals, the columnar organization in the growth plate was disturbed, proteoglycans were lost and improperly formed collagen fibrils were observed. In some chondrocytes the endoplasmic reticulum was dilated, most probably due to an impaired secretion of mutant COMP similar to that observed in patients. Later in development, the growth plate was irregularly shaped and prematurely invaded by bony tissue. In addition, a fusion of the third and fourth sternebrae was frequently observed. (c) 2007 Elsevier B.V./International Society of Matrix Biology. All rights reserved."],["dc.identifier.doi","10.1016/j.matbio.2007.08.001"],["dc.identifier.isi","000253798800001"],["dc.identifier.pmid","17889519"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54911"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1569-1802"],["dc.relation.issn","0945-053X"],["dc.title","Transgenic mice expressing D469 Delta mutated cartilage oligomeric matrix protein (COMP) show growth plate abnormalities and sternal malformations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","PII S0945-053X(02)00070-7"],["dc.bibliographiccitation.firstpage","611"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Matrix Biology"],["dc.bibliographiccitation.lastpage","621"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Sasaki, T."],["dc.contributor.author","Timpl, R."],["dc.date.accessioned","2018-11-07T09:53:49Z"],["dc.date.available","2018-11-07T09:53:49Z"],["dc.date.issued","2002"],["dc.description.abstract","Previous studies have shown that inhibition of nidogen-laminin binding interferes with basement membrane stabilization in various mouse organ cultures while no overt phenotype has been observed following inactivation of the nidogen-1 gene in mice. We have now used recombinant mouse nidogen-1 and nidogen-2 in order to evaluate a possible compensation between the two isoforms in the knock-out mice. Essentially, a comparable in vitro binding of nidogens-1 and -2 to the same laminin-1 chain structure and to several other basement membrane proteins has been revealed. Quantitative radioimmuno-assays have demonstrated high concentrations of nidogen-1 exceeding those of laminin gamma1 and nidogen-2 by factors of 5 and 20-50, respectively, in tissue extracts of wild-type mice. A three- to sevenfold increase in nidogen-2 was observed in heart and muscle of mice with nidogen-1 deficiency and confirmed by a similar increase in the intensity of immunogold staining of these tissues. However, a few of the tissues from mice with the gene knock-out still contained some nidogen-1-like immunoreactivity (1% of wild-type). Furthermore, both nidogen isoforms showed a similar distribution in various organs during embryonic development which, however, as shown previously, changed in some adult tissues. The data support the nidogen-2 compensation hypothesis to explain the limited phenotype observed following elimination of the nidogen-1 gene. (C) 2002 Elsevier Science B.V. and International Society of Matrix Biology. All rights reserved."],["dc.identifier.doi","10.1016/S0945-053X(02)00070-7"],["dc.identifier.isi","000179928600007"],["dc.identifier.pmid","12475645"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36411"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0945-053X"],["dc.title","Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","589"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","British Journal of Cancer"],["dc.bibliographiccitation.lastpage","598"],["dc.bibliographiccitation.volume","91"],["dc.contributor.author","Schweyer, Stefan"],["dc.contributor.author","Soruri, Afsaneh"],["dc.contributor.author","Meschter, O."],["dc.contributor.author","Heintze, A."],["dc.contributor.author","Zschunke, F."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Thelen, Paul"],["dc.contributor.author","Schlott, T."],["dc.contributor.author","Radzun, H.-J."],["dc.contributor.author","Fayyazi, Afshin"],["dc.date.accessioned","2018-11-07T10:46:28Z"],["dc.date.available","2018-11-07T10:46:28Z"],["dc.date.issued","2004"],["dc.description.abstract","Testicular germ cell tumours (TGCT) represent the most common malignancies in young males. Whereas in 1970s, the survival rate in patients with metastatic testicular tumours was only 5%, these days, 80% of the patients treated by modern chemotherapy will survive their disease. The drug that revolutionised the cure rate for patients with metastatic testicular tumours was cisdiamminedichloroplatinum ( cisplatin, CDDP). In vitro experiments on neoplastic germ cell lines showed that their exquisite sensitivity to CDDP could be attributed to p53-dependent and -independent pathways. Applying cDNA macroarray, semiquantitative RT-PCR and Western blot analyses, blocking experiments, caspase activity assays, and morphological methods, we sought here to define the p53-independent pathway(s) involved in the CDDP-induced apoptosis. For this purpose, we used the human TGCT cell line NCCIT, the mutated p53 of which is known to remain inactive during the course of CDDP-induced apoptosis. Our experiments showed that within hours of CDDP application, two prototype members of the 'mitogen-activated protein kinase' ( MAPK) family, designated 'MAPK ERK kinase' (MEK) and 'extracellular signal-regulated kinase' ( ERK), were dually phosphorylated and caspase-3 became active. Functional assays using MEK inhibitors demonstrated that the phosphorylation of MEK and ERK was required for the activation of caspase-3 as the executing caspase. Interestingly, experiments with the human malignant germ cell line NTERA, which is known to possess wild-type p53, revealed the same results. Thus, our data suggest that CDDP mediates its p53-independent apoptosis-inducing effect on the malignant human testicular germ cells - at least partially - through activation of the MEK - ERK signalling pathway."],["dc.identifier.doi","10.1038/sj.bjc.6601919"],["dc.identifier.isi","000222930400029"],["dc.identifier.pmid","15266324"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/47752"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0007-0920"],["dc.title","Cisplatin-induced apoptosis in human malignant testicular germ cell lines depends on MEK/ERK activation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","73"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Therapeutic Drug Monitoring"],["dc.bibliographiccitation.lastpage","78"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Brandhorst, Gunnar"],["dc.contributor.author","Brehmer, Franziska"],["dc.contributor.author","Petrova, Darinka T"],["dc.contributor.author","Gross, Oliver"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Armstrong, Victor W"],["dc.contributor.author","Oellerich, Michael"],["dc.date.accessioned","2021-06-01T10:46:58Z"],["dc.date.available","2021-06-01T10:46:58Z"],["dc.date.issued","2010"],["dc.description.abstract","Within the scope of this study, the potential antifibrotic effect of mycophenolate mofetil (MMF) on COL4A3-deficient mice as an animal model for progressive renal fibrosis was investigated regarding kidney function and survival. Thirty-five animals were randomly assigned to one of five groups and treated with doses of 0, 10, 50, 100, or 150 mg/kg MMF per day, respectively. When increasing somnolence was observed, indicating end-stage renal disease, the mice were euthanized and blood was obtained. Serum concentrations of creatinine, urea nitrogen, total protein, mycophenolic acid (MPA), and mycophenolic acid glucuromide (MPAG) were quantified. The kidney histology was examined using hematoxylin and eosin as well as trichrome staining. The mean overall survival was 65.9 (+/- 6.1) days with no significant difference between the treatment groups (P > 0.05, Mantel-Cox test). Serum predose concentrations of MPA and MPAG showed considerable interindividual variability. There was no correlation between Survival time and MPA or MPAG concentrations (P > 0.05, Spearman rank correlation). However, an apparent decrease in serum creatinine and urea nitrogen concentrations was observed at higher doses of MMF, eg, -54% for creatinine in the 150-mg/kg/day group compared with placebo. A highly significant reciprocal correlation between MPA concentrations and serum creatinine was demonstrated (P < 0.01, r = -0.655, Spearman rank correlation). In conclusion, MMF may be a candidate drug for preserving kidney function in progressive renal fibrosis."],["dc.identifier.doi","10.1097/FTD.0b013e3181c91fc4"],["dc.identifier.isi","000274072000011"],["dc.identifier.pmid","20042922"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85439"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","0163-4356"],["dc.title","Mycophenolic Acid Predose Concentrations and Renal Function in a Mouse Model for Progressive Renal Fibrosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","194760352096706"],["dc.bibliographiccitation.journal","CARTILAGE"],["dc.contributor.author","Schminke, Boris"],["dc.contributor.author","Kauffmann, Philipp"],["dc.contributor.author","Schubert, Andrea"],["dc.contributor.author","Altherr, Manuel"],["dc.contributor.author","Gelis, Thomas"],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2021-04-14T08:31:21Z"],["dc.date.available","2021-04-14T08:31:21Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1177/1947603520967069"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83568"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1947-6043"],["dc.relation.issn","1947-6035"],["dc.title","SMURF1 and SMURF2 in Progenitor Cells from Articular Cartilage and Meniscus during Late-Stage Osteoarthritis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","382"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The Anatomical Record"],["dc.bibliographiccitation.lastpage","388"],["dc.bibliographiccitation.volume","254"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Heinemann, Steffen"],["dc.contributor.author","Leissling, Andreas"],["dc.contributor.author","Klenczar, Christina"],["dc.contributor.author","Herken, Rainer"],["dc.date.accessioned","2021-12-08T12:28:19Z"],["dc.date.available","2021-12-08T12:28:19Z"],["dc.date.issued","1999"],["dc.identifier.doi","10.1002/(SICI)1097-0185(19990301)254:3<382::AID-AR9>3.0.CO;2-O"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/95643"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1097-0185"],["dc.relation.issn","0003-276X"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","Ultrastructural triple localization of laminin-1, nidogen-1, and collagen type IV helps elucidate basement membrane structure in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]