Miosge, Nicolai

[["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"]]

[["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","799"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","HISTOLOGY AND HISTOPATHOLOGY"],["dc.bibliographiccitation.lastpage","806"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Kempkensteffen, C."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Sonnenberg, Anton S. M."],["dc.contributor.author","Herken, R."],["dc.date.accessioned","2018-11-07T10:47:40Z"],["dc.date.available","2018-11-07T10:47:40Z"],["dc.date.issued","2004"],["dc.description.abstract","Normal liver sinusoids are not lined by a basement membrane (BM). In contrast, in the course of development of liver cirrhosis, a structured BM is formed de novo in the space of Disse. This BM contributes to the inhibition of the metabolic function of the liver but the pathogenic background of the formation of this perisinusoidal BM is still unclear. Integrins of the beta1-class are generally essential for BM stability and some of them (such as alpha2beta1, alpha3beta1 and alpha6beta1) appear de novo in the perisinusoidal space of the cirrhotic liver. Their cellular distribution in capillarized sinusoids as well as the correlation between their cellular distribution and the formation of the microvascular BM in the cirrhotic liver has not been shown at the ultrastructural level. In the present work we aimed to clarify this issue. We focused on integrins alpha3beta1 and alpha6beta1 and localised them ultrastructurally in human cirrhotic liver microvessels using postembedding immunogold which allows the ultrastructural localization of antigens with high resolution in the tissue. The newly formed basement membrane of capillarized sinusoids was visualized by means of fixation with addition of tannic acid, which enables the visualization of structures of the extracellular matrix with the highest resolution. Also, we carried out laminin detection using postembedding immunogold. Our results show that both alpha3beta1 and alpha6beta1 are expressed on the surface of both hepatocytes and endothelial cells, i.e. on both sides of the newly formed basement membrane. This latter shows zones of higher density both in close proximity to the endothelial and to the hepatocytic surfaces which resemble laminae densae. We propose that hepatocytes and endothelial cells may, therefore, by expressing such integrins, contribute to the formation of this pathological BM in the microvessels of the human cirrhotic liver. On stellate cells, which are major producers of BM components, both integrins alpha3beta1 and alpha6beta1 were also localized."],["dc.identifier.isi","000222112300018"],["dc.identifier.pmid","15168343"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48015"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","F Hernandez"],["dc.relation.issn","0213-3911"],["dc.title","Ultrastructural localization of integrin subunits alpha 3 and alpha 6 in capillarized sinusoids of the human cirrhotic liver"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","229"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Histochemistry and Cell Biology"],["dc.bibliographiccitation.lastpage","236"],["dc.bibliographiccitation.volume","122"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Hartmann, M."],["dc.contributor.author","Maelicke, C."],["dc.contributor.author","Herken, R."],["dc.date.accessioned","2018-11-07T10:45:57Z"],["dc.date.available","2018-11-07T10:45:57Z"],["dc.date.issued","2004"],["dc.description.abstract","In normal hyaline cartilage the predominant collagen type is collagen type II along with its associated collagens, for example, types IX and XI, produced by normal chondrocytes. In contrast, investigations have demonstrated that in vitro a switch from collagen type II to collagen type I occurs. Some authors have detected collagen type I in osteoarthritic cartilage also in vivo, especially in late stages of osteoarthritis, while others have not. In the light of these diverging results, we have attempted to elucidate which type of collagen, type I and/or type II, is synthesized in the consecutive stages of human osteoarthritis. We performed in situ hybridization and immunohistochemistry with cartilage tissue samples from patients suffering from various stages of osteoarthritis. Furthermore, we quantitated our results on the gene expression of collagen type I and type II with the help of real-time PCR. We found that with the progression of the disease not only collagen type II, but also increasing amounts of collagen type I mRNA were produced. This supports the conclusion that collagen type I gradually becomes one of the factors involved in the pathogenesis of osteoarthritis."],["dc.identifier.doi","10.1007/s00418-004-0697-6"],["dc.identifier.isi","000224512000007"],["dc.identifier.pmid","15316793"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/47626"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0948-6143"],["dc.title","Expression of collagen type I and type II in consecutive stages of human osteoarthritis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","229"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Histochemistry and Cytochemistry"],["dc.bibliographiccitation.lastpage","237"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Klenczar, Christina"],["dc.contributor.author","Herken, Rainer"],["dc.date.accessioned","2018-08-20T09:46:59Z"],["dc.date.available","2018-08-20T09:46:59Z"],["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 and is expressed by mesenchymal cells during embryonic and fetal development. It is not clear which cells produce nidogen-1 in early developmental stages when no mesenchyme is present. We therefore localized nidogen-1 and its corresponding mRNA at the light and electron microscopic level in Day 7 mouse embryos during the onset of mesoderm formation by in situ hybridization, light microscopic immunostaining, and immunogold histochemistry. Nidogen-1 mRNA was found not only in the cells of the ectoderm-derived mesoderm but also in the cytoplasm of the endoderm and ectoderm, indicating that all three germ layers express it. Nidogen-1 was localized only in fully developed basement membranes of the ectoderm and was not seen in the developing endodermal basement membrane or in membranes disrupted during mesoderm formation. In contrast, laminin-1 and collagen Type IV were present in all basement membrane types at this developmental stage. The results indicate that, in the early embryo, nidogen-1 may be expressed by epithelial and mesenchymal cells, that both cell types contribute to embryonic basement membrane formation, and that nidogen-1 might serve to stabilize basement membranes in vivo. (J Histochem Cytochem 48:229-237, 2000)"],["dc.identifier.doi","10.1177/002215540004800208"],["dc.identifier.pmid","10639489"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15412"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","0022-1554"],["dc.title","Nidogen-1. Expression and ultrastructural localization during the onset of mesoderm formation in the early mouse embryo"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","593"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Histochemistry & Cytochemistry"],["dc.bibliographiccitation.lastpage","604"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Tornte, L. T."],["dc.contributor.author","Annatshah, Y."],["dc.contributor.author","Schlueter, N. K."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.date.accessioned","2018-11-07T09:53:08Z"],["dc.date.available","2018-11-07T09:53:08Z"],["dc.date.issued","2006"],["dc.description.abstract","Nidogen-1 and -2 are key components of basement membranes (BMs). Despite the presence of nidogen molecules in the parenchyma of the developing liver, no BMs are formed therein. This suggests that, in the liver, nidogens may also have functions other than BM formation. As a first step toward the elucidation of the possible cell biological functions of nidogens in the developing liver, we aimed to study their cellular origin. We localized expression of nidogen-1 and nidogen-2 on prenatal days 12, 14, and 16 in the developing mouse liver using in situ hybridization at the light and electron microscopic level and light microscopic immunohistochemistry. Our results show that nidogens are produced both in portal anlagen and in the parenchyma during liver development. In the parenchyma, transcripts can be found in hepatocytes, precursors of stellate cells, endothelial cells and, most interestingly, hematopoietic cells. Using real-time PCR, we found that the gene expression for both proteins shows a decrease from day 14 to day 16 concomitant with a decrease in the hepatic hematopoiesis. We suggest that nidogens may, to some extent, take part in the regulation of hepatic hematopoiesis."],["dc.identifier.doi","10.1369/jhc.5A6810.2006"],["dc.identifier.isi","000237101200011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36269"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Histochemical Soc Inc"],["dc.relation.issn","0022-1554"],["dc.title","Hematopoietic cells are a source of nidogen-1 and nidogen-2 during mouse liver development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","399"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Blood Cells Molecules and Diseases"],["dc.bibliographiccitation.lastpage","406"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Reinhardt, D."],["dc.contributor.author","Witt, Olaf"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Pekrun, Arnulf"],["dc.date.accessioned","2018-11-07T09:18:16Z"],["dc.date.available","2018-11-07T09:18:16Z"],["dc.date.issued","2001"],["dc.description.abstract","Purpose: Red cells in hereditary spherocytosis are characterized by a reduced surface area/volume ratio. The mechanisms leading to the loss of membrane material and subsequent elimination of the cells have still not been clarified. It was the aim of the present study to analyze band 3 distribution in the red cell membrane and its putative role in red cell elimination. Methods/Results: Immunogold histochemistry was performed to detect band 3 in red cell membranes. Band 3 density and distribution were visualized by electron microscopy. Unsplenectomized spherocytosis patients (n = 12) showed reduced band 3 density and aggregation compared to controls (n = 15) (density: 1.2 +/- 0.1 gold particles/mum circumference of red cell membrane vs 1.5 +/- 0.07 gold particles/mum, x +/- SEM; P < 0.05; aggregation: 0.26 +/- 0.02 aggregates/mum vs 0.3 +/- 0.02 aggregates/mum). By contrast, band 3 density and aggregation were increased in spherocytosis patients who had undergone splenectomy (density: 2.8 +/- 0.1 gold particles/mum vs 2.0 +/- 0.1 gold particles/mum; P < 0.05; aggregation: 1.5 +/- 0.1 aggregates/mum vs 0.5 +/- 0.03 aggregates/mum; P < 0.01). Artificial ageing of red cells from healthy controls (n = 6) led to a significant increase in band 3 aggregation (2.06 +/- 0.2 aggregates/mum vs 0.33 +/- 0.1 aggregates/mum; P-Wilcoxon < 0.01) but no change in band 3 density. In hereditary spherocytosis (n = 6), both band 3 density and aggregation increased significantly, after artificial ageing of the red cells. The elevated band 3 aggregation was associated with a stimulated erythrophagocytosis in vitro. Conclusion: Band 3 aggregation characterizes the red cells in hereditary spherocytosis. It may be the cause of selective splenic phagocytosis of both spherocytes and senescent erythrocytes, (C) 2001 Academic Press."],["dc.identifier.doi","10.1006/bcmd.2001.0396"],["dc.identifier.isi","000169361800007"],["dc.identifier.pmid","11259161"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28372"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc"],["dc.relation.issn","1079-9796"],["dc.title","Increase in band 3 density and aggregation in hereditary spherocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","243"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The Anatomical Record"],["dc.bibliographiccitation.lastpage","251"],["dc.bibliographiccitation.volume","258"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Zieger, Jörg"],["dc.contributor.author","Götz, Werner"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Herken, Rainer"],["dc.date.accessioned","2021-06-01T10:50:45Z"],["dc.date.available","2021-06-01T10:50:45Z"],["dc.date.issued","2000"],["dc.description.abstract","Recently we observed that in human embryos and fetuses with a variety of malformations, not only malformed tissues, but also several non-malformed tissues displayed alterations in the glycosylation pattern. It was the aim of this work to investigate this more or less inexplicable phenomenon under experimental conditions. To this end, we studied a well known mouse model, the mouse mutant undulated, which has an exactly defined genetic defect (substitution in the pax-1 gene) leading to a localized malformation in the vertebral column. The glycosylation pattern was studied using lectin histochemistry. Distribution of binding sites for the lectins RCA I, Con A, SNA, SEA, PNA, LTA and WGA was studied during the organogenesis stages (i.e., days 11-18). It was striking that in mutants, changes in the glycosylation pattern were found not only in the malformed organ (i.e., vertebral anlage), but also in other embryonic tissues, which showed normal morphology. This suggests that the altered glycosylation seems to be a part of genetically determined phenomena throughout the entire organism. Our results show that a defect in a gene with a very restricted expression can cause universal changes in the glycosylation pattern during development. Anat Rec 258:243-251, 2000. (C) 2000 Wiley-Liss, Inc."],["dc.identifier.doi","10.1002/(SICI)1097-0185(20000301)258:3<243::AID-AR3>3.0.CO;2-I"],["dc.identifier.isi","000085629500003"],["dc.identifier.pmid","10705344"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86776"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.relation.eissn","1097-0185"],["dc.relation.issn","0003-276X"],["dc.title","Extensive glycosylation changes revealed by lectin histochemistry in morphologically normal prenatal tissues of the mouse mutantundulated (un/un)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","267"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Histochemical Journal"],["dc.bibliographiccitation.lastpage","272"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Miosge, N."],["dc.date.accessioned","2018-08-20T09:40:57Z"],["dc.date.available","2018-08-20T09:40:57Z"],["dc.date.issued","1991"],["dc.description.abstract","A method is presented which permits the ultrastructural localization of laminin and its E4 and P1 subunits in the renal cortex of the mouse embedded in LR-White or LR-Gold. It was performed with postembedding immunogold histochemistry using polyclonal antibodies against either the entire laminin molecular or the E4 fragment or with a monoclonal antibody against the P1 fragment. Localization of laminin was achieved in LR-White and in LR-Gold embedded kidney. Using polyclonal antibodies against the entire laminin molecule, laminin could be localized with direct as well as with indirect immunogold histochemistry with a gold labelled IgG as secondary antibody. In contrast, immunostaining for the E4 or the P1 fragments was possible only with antibodies directly labelled with gold."],["dc.identifier.pmid","1938473"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15411"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","0018-2214"],["dc.title","Postembedding immunogold histochemistry for the localization of laminin and its E4 and P1 fragments in mouse kidney embedded in LR-White and LR-Gold"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","355"],["dc.bibliographiccitation.issue","5-6"],["dc.bibliographiccitation.journal","ANATOMY AND EMBRYOLOGY"],["dc.bibliographiccitation.lastpage","363"],["dc.bibliographiccitation.volume","205"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Kluge, JGA"],["dc.contributor.author","Studzinski, A."],["dc.contributor.author","Zelent, C."],["dc.contributor.author","Bode, C."],["dc.contributor.author","Sprysch, P."],["dc.contributor.author","Burgeson, R. E."],["dc.contributor.author","Herken, R."],["dc.date.accessioned","2018-11-07T09:57:07Z"],["dc.date.available","2018-11-07T09:57:07Z"],["dc.date.issued","2002"],["dc.description.abstract","Laminin-5 is known to be an integral part of the hemidesmosome and therefore responsible for the integrity of the connection of the epithelium to the basement membrane. This is also an important mechanism during embryonic development, as documented by studies in mice. In an attempt to elucidate its implication for human development we localised the mRNA of the alpha3 chain of laminin with the help of in situ RT-PCR, and the laminin-5 protein immunohistochemically. We systematically investigated kidney, lung, skin and intestinal tissue of consecutive developmental stages during human embryogenesis. From gw 6.5 onwards, the mRNA of the alpha3 chain of laminin was found exclusively in the cytoplasm of epithelial cells of the developing kidney, lung, skin and intestine. Interestingly, in the skin and intestine from gw 8 onwards, the superficial cell layers also stained positive for the mRNA, while the protein was still only found in the dermal-epidermal and enteric basement membrane zones. In all developing organs investigated, the mRNA of the alpha3 chain of laminin is strictly of epithelial origin and the corresponding protein localised in the underlying basement membrane zones. Due to this discrepancy, we postulate a broader role for laminin-5 during human embryogenesis, for example, for epithelial cell development, beyond its involvement in hemidesmosome formation and cell adhesion."],["dc.identifier.doi","10.1007/s00429-002-0256-7"],["dc.identifier.isi","000178975000002"],["dc.identifier.pmid","12382139"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37096"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0340-2061"],["dc.title","In situ-RT-PCR and immunohistochemistry for the localisation of the mRNA of the alpha 3 chain of laminin and laminin-5 during human organogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]