Miosge, Nicolai

[["dc.bibliographiccitation.firstpage","177"],["dc.bibliographiccitation.issue","2-3"],["dc.bibliographiccitation.journal","Journal of Molecular Histology"],["dc.bibliographiccitation.lastpage","184"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Roediger, Matthias"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.date.accessioned","2018-08-20T11:49:34Z"],["dc.date.available","2018-08-20T11:49:34Z"],["dc.date.issued","2010"],["dc.description.abstract","Laminins are the major glycoproteins present in all basement membranes. Previously, we showed that perlecan is present during human development. Although an overview of mRNA-expression of the laminin beta1 and beta2 chains in various developing fetal organs is already available, a systematic localization of the laminin beta1 and beta2 chains on the protein level during embryonic and fetal human development is missing. Therefore, we studied the immunohistochemical expression and tissue distribution of the laminin beta1 and beta2 chains in various developing embryonic and fetal human organs between gestational weeks 8 and 12. The laminin beta1 chain was ubiquitously expressed in the basement membrane zones of the brain, ganglia, blood vessels, liver, kidney, skin, pancreas, intestine, heart and skeletal system. Furthermore, the laminin beta2 chain was present in the basement membrane zones of the brain, ganglia, skin, heart and skeletal system. The findings of this study support and expand upon the theory that these two laminin chains are important during human development."],["dc.identifier.doi","10.1007/s10735-010-9275-5"],["dc.identifier.pmid","20552257"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5016"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15420"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","1567-2387"],["dc.relation.eissn","1567-2379"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Tissue distribution of the laminin β1 and β2 chain during embryonic and fetal human development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1140"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Developmental Dynamics"],["dc.bibliographiccitation.lastpage","1148"],["dc.bibliographiccitation.volume","233"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Mueller, M."],["dc.contributor.author","Otto, S."],["dc.contributor.author","Poschadel, R."],["dc.contributor.author","Hubner, S."],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2018-11-07T09:01:16Z"],["dc.date.available","2018-11-07T09:01:16Z"],["dc.date.issued","2005"],["dc.description.abstract","Basement membranes (BM) are specialized structures of the extracellular matrix known to be involved in various early developmental processes. Despite numerous investigations on the localization of BM components, it remains unknown which molecules are expressed in early developmental stages and by which germ layers these proteins are produced. Therefore, we tested for all known laminin chains, nidogens, collagen type IV, and perlecan by means of light microscopic immunostaining and performed in situ reverse transcriptase-polymerase chain reaction to detect the mRNAs specific for laminin alpha 1, laminin beta 1, the alpha 1 chain of collagen type TV, nidogen-2, and perlecan in the early mouse embryo, day 7, in vivo. Only the laminin chains alpha 1, beta 1, and gamma 1 were detected immunohistochemically throughout the entire endodermal and ectodermal BM zones of the embryo proper. The mRNA of laminin alpha 1, laminin beta 1, collagen type IV, nidogen-2 and perlecan were expressed in the ectoderm-derived mesoderm, in the endoderm. as well as in the ectoderm. In contrast, Reichert's membrane was positive for all laminin chains except for the alpha 4, alpha 5, beta 3, and gamma 3 chains. Moreover, maternal epithelial as well as mesenchymal cells expressed laminins, nidogen-1 and nidogen-2, collagen type IV, and perlecan. In conclusion, laminin-1 might be the only laminin isoform in the early mouse embryo that, together with the other main BM components, nidogens, collagen type IV, and perlecan, is synthesized by all three germ layers. (c) 2005 Wiley-Liss, Inc."],["dc.identifier.doi","10.1002/dvdy.20425"],["dc.identifier.isi","000229892100048"],["dc.identifier.pmid","15895400"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24379"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.relation.issn","1058-8388"],["dc.title","Basement membrane composition in the early mouse embryo day 7"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1081"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Cellular and Molecular Life Sciences"],["dc.bibliographiccitation.lastpage","1096"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Schminke, Boris"],["dc.contributor.author","Muhammad, Hayat"],["dc.contributor.author","Bode, Christa"],["dc.contributor.author","Sadowski, Boguslawa"],["dc.contributor.author","Gerter, Regina"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Buergers, Ralf"],["dc.contributor.author","Monsonego-Ornan, Efrat"],["dc.contributor.author","Rosen, Vicki"],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2018-11-07T09:43:22Z"],["dc.date.available","2018-11-07T09:43:22Z"],["dc.date.issued","2014"],["dc.description.abstract","Discoidin domain receptor 1 (DDR-1)-deficient mice exhibited a high incidence of osteoarthritis (OA) in the temporomandibular joint (TMJ) as early as 9 weeks of age. They showed typical histological signs of OA, including surface fissures, loss of proteoglycans, chondrocyte cluster formation, collagen type I upregulation, and atypical collagen fibril arrangements. Chondrocytes isolated from the TMJs of DDR-1-deficient mice maintained their osteoarthritic characteristics when placed in culture. They expressed high levels of runx-2 and collagen type I, as well as low levels of sox-9 and aggrecan. The expression of DDR-2, a key factor in OA, was increased. DDR-1-deficient chondrocytes from the TMJ were positively influenced towards chondrogenesis by a three-dimensional matrix combined with a runx-2 knockdown or stimulation with extracellular matrix components, such as nidogen-2. Therefore, the DDR-1 knock-out mouse can serve as a novel model for temporomandibular disorders, such as OA of the TMJ, and will help to develop new treatment options, particularly those involving tissue regeneration."],["dc.identifier.doi","10.1007/s00018-013-1436-8"],["dc.identifier.isi","000331653900010"],["dc.identifier.pmid","23912900"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34171"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Basel"],["dc.relation.issn","1420-9071"],["dc.relation.issn","1420-682X"],["dc.title","A discoidin domain receptor 1 knock-out mouse as a novel model for osteoarthritis of the temporomandibular joint"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1077"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","HISTOLOGY AND HISTOPATHOLOGY"],["dc.bibliographiccitation.lastpage","1084"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Otto, S."],["dc.contributor.author","Roediger, Matthias"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2018-11-07T10:58:06Z"],["dc.date.available","2018-11-07T10:58:06Z"],["dc.date.issued","2007"],["dc.description.abstract","Nidogen- 1 and nidogen- 2 are major components of all basement membranes and are considered to function as link molecules between laminin and collagen type IV networks. Surprisingly, the knockout of one or both nidogens does not cause defects in all tissues or in all basement membranes. In this study, we have elucidated the appearance of the major basement membrane components in adult murine kidney lacking nidogen- 1, nidogen- 2, or both nidogens. To this end, we localized laminin- 111, perlecan, and collagen type IV in knockout mice, heterozygous (+/-) or homozygous (-/-) for the nidogen- 1 gene, the nidogen- 2 gene, or both nidogen genes with the help of light microscopic immunostaining. We also performed immunogold histochemistry to determine the occurrence of these molecules in the murine kidney at the ultrastructural level. The renal basement membranes of single knockout mice contained a similar distribution of laminin- 111, perlecan, and collagen type IV compared to heterozygous mice. In nidogen double- knockout animals, the basement membrane underlying the tubular epithelium was sometimes altered, giving a diffuse and thickened pattern, or was totally absent. The normal or thickened basement membrane of double- knockout mice also showed a similar distribution of laminin- 111, perlecan, and collagen type IV. The results indicate that the lack of nidogen- 1, nidogen- 2, or both nidogens, plays no crucial role in the occurrence and localization of laminin- 111, collagen type IV, and perlecan in murine tubular renal basement membranes."],["dc.identifier.isi","000247757300003"],["dc.identifier.pmid","17616934"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50403"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","F Hernandez"],["dc.relation.issn","0213-3911"],["dc.title","The absence of one or both nidogens does not alter basement membrane composition in adult murine kidney"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","31"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Oral Biosciences"],["dc.bibliographiccitation.lastpage","45"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Roediger, Matthias"],["dc.contributor.author","Miró, Xavier"],["dc.contributor.author","Geffers, Robert"],["dc.contributor.author","Irmer, Malte"],["dc.contributor.author","Huels, Alfons"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.date.accessioned","2019-07-09T11:52:27Z"],["dc.date.available","2019-07-09T11:52:27Z"],["dc.date.issued","2009"],["dc.description.abstract","The purpose of this study was to compare gene expression profiles of peri-implantitis and periodontitis to elucidate potential differences at the molecular level. With the help of microarray analysis, genome-wide gene expression of inflamed peri-implant granulation tissue, inflamed and healthy periodontal tissues (n=48 patients) were compared and the data were validated by real-time reverse transcription polymerase chain reaction. After highlighting different gene classes, we focused on the extracellular matrix-receptor interaction pathway and gene expression of extracellular matrix molecules, their receptors and matrix degrading enzymes. Only genes of non-fibril-forming collagens (types IV, VI, VII, and Q) were increased in peri-implantitis compared to periodontitis, whereas the expressions of two fibril-forming collagens (types III and K) were decreased in peri-implantitis, which suggested that peri-implant tissue re-models faster than periodontal tissue in vivo. Furthermore, cathepsin D and cathepsin S seem to participate in the destruction of peri-implant connective tissue. Despite their clinical similarities, the present investigation demonstrated that peri-implantitis and periodontitis are two different disease entities at least at the messanger ribonucleic acid level. The data provide insight for future studies aimed at dissecting the pathogenesis of peri-implant inflammation."],["dc.identifier.doi","10.2330/joralbiosci.51.31"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/4310"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60194"],["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","Profiling of Differentially Expressed Genes in Peri-implantitis and Periodontitis in vivo by Microarray Analysis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","859"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","HISTOLOGY AND HISTOPATHOLOGY"],["dc.bibliographiccitation.lastpage","868"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Roediger, Matthias"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.date.accessioned","2018-11-07T08:28:11Z"],["dc.date.available","2018-11-07T08:28:11Z"],["dc.date.issued","2009"],["dc.description.abstract","A major component of basement membranes (BMs) is perlecan, a five-domain heparan sulphate proteoglycan. During murine embryogenesis, nearly all BMs of mesenchymal origin express perlecan, and it is believed to participate in the supramolecular assembly of BMs. However, the distribution of perlecan in human embryonic and fetal tissues is widely unknown, except for cartilage anlagen of developing extremities and the fetal spine. Clinical syndromes, caused by perlecan-associated mutations or gene-defects, suggest its multifunctional involvement during human development. Here we reveal the immunohistochemistry of perlecan domains III and V during human development from gestational weeks (gw) 6 to 12 in basement membrane zones (BMZs) of the developing brain, nervous system, blood vessels, skin, lung, heart, kidney, liver, intestine and skeletal system. Interestingly, a difference in the distribution of the two perlecan domains was found in the endoneurium of ganglia. Domain III is strongly present from gw 6 onwards, while domain V shows attenuated expression at this stage and has been detected abundantly only from gw 8 onwards, possibly indicating vascularization of the endoneurium during this early stage. We found perlecan to be present particularly at those stages of human development where epithelial-mesenchymal interactions occur."],["dc.identifier.isi","000266407500007"],["dc.identifier.pmid","19475532"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16364"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","F Hernandez"],["dc.relation.issn","0213-3911"],["dc.title","Tissue distribution of perlecan domains III and V during embryonic and fetal human development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","22146"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","22153"],["dc.bibliographiccitation.volume","280"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Kohfeldt, E."],["dc.contributor.author","Sasaki, T."],["dc.contributor.author","Timpl, R."],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2018-11-07T10:02:37Z"],["dc.date.available","2018-11-07T10:02:37Z"],["dc.date.issued","2005"],["dc.description.abstract","Recently a novel laminin γ 3 chain was identified in mouse and human and shown to have the same modular structure as the laminin γ 1 chain. We expressed two fragments of the γ 3 chain in mammalian cells recombinantly. The first, domain VI/V, consisting of laminin N-terminal (domain VI) and four laminin-type epidermal growth factor-like (domain V) and laminin N-terminal modules, was shown to be essential for self-assembly of laminins. The other was domain III3-5, which consists of three laminin-type epidermal growth factor-like modules and is predicted to bind to nidogens. The γ 3 VI/V fragment was a poor inhibitor for laminin-1 polymerization as was the γ 2 VI/ V fragment. The γ 3 III3-5 fragment bound to nidogen-1 and nidogen-2 with lower affinity than the γ 1 III3-5 fragment. These data suggested that laminins containing the γ 3 chain may assemble networks independent of other laminins. Polyclonal antibodies raised against γ 3 VI/V and γ 3 III3-5 showed no cross-reaction with homologous fragments from the γ 1 and γ 2 chains of laminin and allowed the establishment of γ chain-specific radioimmunoassays and light and electron microscopic immunostaining of tissues. This demonstrated a 20-100-fold lower content of the γ 3 chain compared with the γ 1 chain in various tissue extracts of adult mice. The expression of γ 3 chain was highly tissue-specific. In contrast to earlier assumptions, the antibodies against the γ 3 chain showed light microscopic staining exclusively in basement membrane zones of adult and embryonic tissues, such as the brain, kidney, skin, muscle, and testis. Ultrastructural immunogold staining localized the γ 3 chain to basement membranes of these tissues."],["dc.identifier.doi","10.1074/jbc.M501875200"],["dc.identifier.isi","000229557900059"],["dc.identifier.pmid","15824114"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38267"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Laminin gamma 3 chain binds to nidogen and is located in murine basement membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","705"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Histochemistry and Cell Biology"],["dc.bibliographiccitation.lastpage","712"],["dc.bibliographiccitation.volume","126"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Mueller, Matthias"],["dc.contributor.author","Schall, Antje"],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2018-11-07T08:53:48Z"],["dc.date.available","2018-11-07T08:53:48Z"],["dc.date.issued","2006"],["dc.description.abstract","BM-40 is an extracellular matrix-associated protein and is characterized by an extracellular calcium-binding domain as well as a follistatin-like domain. Secreted modular calcium-binding protein-1 (SMOC-1) is a new member of the BM-40 family. It consists of two thyroglobulin-like domains, a follistatin-like domain and a new domain without known homologues and is expressed ubiquitously in many adult murine tissues. Immunofluorescence studies, as well as immunogold electron microscopy, have confirmed the localization of SMOC-1 in or around basement membranes of adult murine skin, blood vessels, brain, kidney, skeletal muscle, and the zona pellucida surrounding the oocyte. In the present work, light microscopic immunohistochemistry has revealed that SMOC-1 is localized in the early mouse embryo day 7 throughout the entire endodermal basement membrane zone of the embryo proper. SMOC-1 mRNA is synthesized, even in early stages of mouse development, by mesenchymal as well as epithelial cells deriving from all three germ layers. In embryonic stage day 12, and fetal stages day 14, 16, and 18, the protein is present in the basement membrane zones of brain, blood vessels, skin, skeletal muscle, lung, heart, liver, pancreas, intestine, and kidney. This broad and organ-specific distribution suggests multifunctional roles of SMOC-1 during mouse embryogenesis."],["dc.identifier.doi","10.1007/s00418-006-0200-7"],["dc.identifier.isi","000242624400007"],["dc.identifier.pmid","16736127"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22513"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0948-6143"],["dc.title","Secreted modular calcium-binding protein-1 localization during mouse embryogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Dental Research Journal"],["dc.bibliographiccitation.lastpage","11"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Miró, Xavier"],["dc.contributor.author","Roediger, Matthias"],["dc.contributor.author","Geffers, Robert"],["dc.contributor.author","Huels, Alfons"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Toepfer, Tanja"],["dc.date.accessioned","2019-07-10T08:12:53Z"],["dc.date.available","2019-07-10T08:12:53Z"],["dc.date.issued","2008"],["dc.description.abstract","Background: In the periodontium, the functions of the cell populations regarding the host-mediated tissue destruction in health and disease are not well understood. The purpose of this study was to measure the expression of genes differentially expressed in chronically inflamed periodontal ligament (PDL) cells compared to healthy PDL cells. Methods: We compared the genome-wide gene expressions of chronically inflamed and healthy PDL cells by microarray analysis, and validated the data by real-time RT-PCR to identify the genes that might play distinct roles in chronic periodontal disease in vivo. Results: The expression rates of 14,239 genes were investigated and 3,165 of them were found differentially expressed by at least two-fold; the expression rates of 1,515 genes were significantly upregulated and the expression rates of 1,650 genes were significantly downregulated in inflamed PDL cells. Conclusion: We focused on mainly structural components, for example, laminins and integrins, as well as degrading enzymes, for example, MMPs and cathepsins. The molecular composition of the laminin network varies in chronically inflamed compared to healthy PDL cells in vivo. Furthermore, integrin alpha6beta4, together with laminin-332, might be involved in chronic periodontal inflammation. Diverse keratins were upregulated, indicating that the epithelial cell rests of Malassez might also be involved in chronic periodontitis. The microarray analysis has identified a profile of genes potentially involved in chronic periodontal inflammation in vivo."],["dc.identifier.fs","432816"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/4309"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61070"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Gene Expression Analysis of Chronically Inflamed and Healthy Human Periodontal Ligament Cells in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]