Miosge, Nicolai

[["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","115"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Histochemistry and Cell Biology"],["dc.bibliographiccitation.lastpage","124"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Kother, F."],["dc.contributor.author","Heinemann, S."],["dc.contributor.author","Kohfeldt, E."],["dc.contributor.author","Herken, R."],["dc.contributor.author","Timpl, R."],["dc.date.accessioned","2018-11-07T10:28:33Z"],["dc.date.available","2018-11-07T10:28:33Z"],["dc.date.issued","2000"],["dc.description.abstract","Nidogen-1, a key component of basement membranes, is considered to function as a link between laminin and collagen type IV networks. Recently a new member of the nidogen family, nidogen-2, has been characterized. Preliminary immunohistochemical data indicated that nidogen-1 and nidogen-2 show a similar tissue distribution at the light microscopic level. We have now localized nidogen-1 and nidogen-2, as well as their corresponding mRNAs, at the light and electron microscopic levels in adult mouse kidney, by in situ hybridization and immunogold histochemistry, as well as carrying out double labeling with laminin-1. Both nidogen-1 and nidogen-2 mRNAs are found not only in mesenchymal cells of embryonic tissues, but also in all epithelial and endothelial cells in adult mouse kidney. Both nidogens are ubiquitous basement membrane components in the mouse kidney, being found in glomerular, tubular, and capillary compartments and Bowman's capsule. Further more, a substantial fraction of nidogen-1 and nidogen-2 colocalizes with laminin-1. The results indicate that nidogen-1 and nidogen-2 could well substitute for one another in some of their biological activities in kidney, for example, stabilizing basement membrane networks in vivo."],["dc.identifier.doi","10.1007/s004180050014"],["dc.identifier.isi","000086163600006"],["dc.identifier.pmid","10766264"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43446"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0301-5564"],["dc.title","Ultrastructural colocalization of nidogen-1 and nidogen-2 with laminin-1 in murine kidney 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","2711"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Development"],["dc.bibliographiccitation.lastpage","2722"],["dc.bibliographiccitation.volume","129"],["dc.contributor.author","Willem, M."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Halfter, W."],["dc.contributor.author","Smyth, N."],["dc.contributor.author","Jannetti, I."],["dc.contributor.author","Burghart, E."],["dc.contributor.author","Timpl, R."],["dc.contributor.author","Mayer, U."],["dc.date.accessioned","2018-11-07T10:27:32Z"],["dc.date.available","2018-11-07T10:27:32Z"],["dc.date.issued","2002"],["dc.description.abstract","Basement membrane assembly is of crucial importance in the development and function of tissues and during embryogenesis. Nidogen 1 was thought to be central in the assembly processes, connecting the networks formed by collagen type IV and laminins, however, targeted inactivation of nidogen I resulted in no obvious phenotype. We have now selectively deleted the sequence coding for the 56 amino acid nidogen-binding site, gamma1III4, within the Lamc1 gene by gene targeting. Here, we show that mice homozygous for the deletion die immediately after birth, showing renal agenesis and impaired lung development. These developmental defects were attributed to locally restricted ruptures in the basement membrane of the elongating Wolffian duct and of alveolar sacculi. These data demonstrate that an interaction between two basement membrane proteins is required for early kidney morphogenesis in vivo."],["dc.identifier.isi","000176471600014"],["dc.identifier.pmid","12015298"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43249"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0950-1991"],["dc.title","Specific ablation of the nidogen-binding site in the laminin gamma 1 chain interferes with kidney and lung development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","431"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","EUROPEAN JOURNAL OF BIOCHEMISTRY"],["dc.bibliographiccitation.lastpage","442"],["dc.bibliographiccitation.volume","269"],["dc.contributor.author","Sasaki, T."],["dc.contributor.author","Mann, K."],["dc.contributor.author","Miner, Jeffrey H."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Timpl, R."],["dc.date.accessioned","2018-11-07T10:33:02Z"],["dc.date.available","2018-11-07T10:33:02Z"],["dc.date.issued","2002"],["dc.description.abstract","Domain IV, consisting of about 230 residues, represents a particular protein module so far found only in laminin beta1 and beta2 chains. Both domains were obtained by recombinant production in mammalian cells. They showed a globular structure, as expected from electron microscopic examination of laminins. Fragment beta1IV was obtained as a monomer and a disulfide-bonded dimer, and both were modified to approximate to50% by a single chondroitin sulfate chain attached to Ser721 of an SGD consensus sequence. Dimerization is caused by an odd number of cysteines, with three of them having a partial thiol character. Whether both modifications also occur in tissue forms of laminin remains to be established. Fragment beta21V was only obtained as a monomer, as it lacked one crucial cysteine and the SGD sequence. It required, however, the presence of two adjacent LE modules for proper folding. Polyclonal antibodies raised against both fragments showed no cross-reaction with each other and allowed establishment of beta chain-specific radioimmunoassays and light and electron microscopic immunostaining of tissues. This demonstrated a 5-25-fold lower content of beta2 compared with beta1 chains in various tissue extracts of adult mice. Tissues derived from beta2-deficient mice failed to react with the beta2-specific antibodies but showed a twofold higher content of beta1 than heterozygotes. The antibodies to beta2 showed broader tissue staining than reported previously, including in particular a distinct reaction with the extra-synaptic endomysium of skeletal muscle. Immunogold staining localized both beta chains primarily to basement membranes of kidney, muscle and various other tissues."],["dc.identifier.doi","10.1046/j.0014-2956.2001.02663.x"],["dc.identifier.isi","000173651700004"],["dc.identifier.pmid","11856301"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44504"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing Ltd"],["dc.relation.issn","0014-2956"],["dc.title","Domain IV of mouse laminin beta 1 and beta 2 chains - Structure, glycosaminoglycan modification and immunochemical analysis of tissue contents"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6820"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","6830"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Schymeinsky, Juergen"],["dc.contributor.author","Nedbal, S."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Poschl, E."],["dc.contributor.author","Rao, C."],["dc.contributor.author","Beier, D. R."],["dc.contributor.author","Skarnes, W. C."],["dc.contributor.author","Timpl, R."],["dc.contributor.author","Bader, B. L."],["dc.date.accessioned","2018-11-07T10:01:20Z"],["dc.date.available","2018-11-07T10:01:20Z"],["dc.date.issued","2002"],["dc.description.abstract","Nidogens are highly conserved proteins in vertebrates and invertebrates and are found in almost all basement membranes. According to the classical hypothesis of basement membrane organization, nidogens connect the laminin and collagen IV networks, so stabilizing the basement membrane, and integrate other proteins. In mammals two nidogen proteins, nidogen-1 and nidogen-2, have been discovered. Nidogen-2 is typically enriched in endothelial basement membranes, whereas nidogen-1 shows broader localization in most basement membranes. Surprisingly, analysis of nidogen-1 gene knockout mice presented evidence that nidogen-1 is not essential for basement membrane formation and may be compensated for by nidogen-2. In order to assess the structure and in vivo function of the nidogen-2 gene in mice, we cloned the gene and determined its structure and chromosomal location. Next we analyzed mice carrying an insertional mutation in the nidogen-2 gene that was generated by the secretory gene trap approach. Our molecular and biochemical characterization identified the mutation as a phenotypic null allele. Nidogen-2-deficient mice show no overt abnormalities and are fertile, and basement membranes appear normal by ultrastructural analysis and immunostaining. Nidogen-2 deficiency does not lead to hemorrhages in mice as one may have expected. Our results show that nidogen-2 is not essential for basement membrane formation or maintenance."],["dc.identifier.doi","10.1128/MCB.22.19.6820-6830.2002"],["dc.identifier.isi","000177961900017"],["dc.identifier.pmid","12215539"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37994"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","Gene structure and functional analysis of the mouse nidogen-2 gene: Nidogen-2 is not essential for basement membrane formation in mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","35192"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","35199"],["dc.bibliographiccitation.volume","275"],["dc.contributor.author","Talts, J. F."],["dc.contributor.author","Sasaki, T."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Gohring, W."],["dc.contributor.author","Mann, K."],["dc.contributor.author","Mayne, R."],["dc.contributor.author","Timpl, R."],["dc.date.accessioned","2018-11-07T10:58:44Z"],["dc.date.available","2018-11-07T10:58:44Z"],["dc.date.issued","2000"],["dc.description.abstract","The C-terminal G domains of laminin a chains have been implicated in various cellular and other interactions. The G domain of the alpha4 chain was now produced in transfected mammalian cells as two tandem arrays of LG modules, alpha 4LG1-3 and alpha 4LG4-5. The recombinant fragments Were shown to fold into globular structures and could be distinguished by specific antibodies. Both fragments were able to bind to heparin, sulfatides, and the microfibrillar fibulin-1 and fibulin-2. They were, however, poor substrates for cell adhesion and had only a low affinity;for the alpha -dystroglycan receptor when compared with: the G domains of the laminin alpha1 and alpha2 chains. Yet antibodies to alpha 4LG1-3 but not to alpha 4LG4-5 clearly inhibited alpha (6)beta (1) integrin-mediated cell adhesion to laminin-8, indicating the participation of alpha 4LG1-3 in a cell-adhesive structure of higher complexity. Proteolytic: processing within a link region between the alpha 4LG3 and alpha 4LG4 modules was shown to occur during recombinant production and in endothelial and Schwann cell culture. Cleavage could be attributed to three different peptide bonds and is accompanied by the release of the alpha 4LG4-5 segment. Immunohistology demonstrated abundant staining of alpha 4LG1-3 in vessel walls, adipose, and perineural tissue. No significant staining was found for alpha 4LG4-5 indicating their loss from tissues. Immunogold staining demonstrated an association of the alpha4 chain primarily with microfibrillar regions rather than with basement membranes, while laminin alpha2 chains appear primarily associated with various basement membranes."],["dc.identifier.doi","10.1074/jbc.M003261200"],["dc.identifier.isi","000165422800050"],["dc.identifier.pmid","10934193"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50532"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Structural and functional analysis of the recombinant G domain of the laminin alpha 4 chain and its proteolytic processing in tissues"],["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"]]