Herken, Rainer

[["dc.bibliographiccitation.artnumber","PII S0945-053X(03)00016-7"],["dc.bibliographiccitation.firstpage","93"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Matrix Biology"],["dc.bibliographiccitation.lastpage","96"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Reinhardt, D. P."],["dc.contributor.author","Charbonneau, N. L."],["dc.contributor.author","Pophal, G."],["dc.contributor.author","Sakai, L. Y."],["dc.contributor.author","Herken, R."],["dc.date.accessioned","2018-11-07T10:40:41Z"],["dc.date.available","2018-11-07T10:40:41Z"],["dc.date.issued","2003"],["dc.identifier.doi","10.1016/S0945-053X(03)00016-7"],["dc.identifier.isi","000182967400010"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46358"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0945-053X"],["dc.title","Fibrillin-1 and fibrillin-2 in human embryonic and early fetal development (vol 21, pg 637, 2002)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]

[["dc.bibliographiccitation.journal","Glia"],["dc.contributor.author","Nico, B."],["dc.contributor.author","Corsi, P."],["dc.contributor.author","Frigeri, A."],["dc.contributor.author","Nicchia, G. P."],["dc.contributor.author","Mangieri, D."],["dc.contributor.author","Frontino, A."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Ribatti, D."],["dc.contributor.author","Svelto, M."],["dc.contributor.author","Roncali, L."],["dc.date.accessioned","2018-11-07T10:36:31Z"],["dc.date.available","2018-11-07T10:36:31Z"],["dc.date.issued","2003"],["dc.format.extent","29"],["dc.identifier.isi","000184938300123"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45347"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.publisher.place","New york"],["dc.relation.conference","6th European Meeting on Glial Cell Function in Health and Disease"],["dc.relation.eventlocation","BERLIN, GERMANY"],["dc.relation.issn","0894-1491"],["dc.title","Blood-brain barrier alterations in dystrophic mdx mice"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","215"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Developmental Dynamics"],["dc.bibliographiccitation.lastpage","221"],["dc.bibliographiccitation.volume","234"],["dc.contributor.author","Mueller, M."],["dc.contributor.author","Berger, Joachim"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Cecconi, F."],["dc.contributor.author","Herken, R."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.date.accessioned","2018-11-07T10:56:02Z"],["dc.date.available","2018-11-07T10:56:02Z"],["dc.date.issued","2005"],["dc.description.abstract","Apoptosis is an essential ubiquitous process that controls the duration of the life span of cells, thus playing a crucial role in morphogenetic, histogenetic, and phylogenetic developmental processes. Apaf1 (apoptosis protease activating factor 1) is one of the central mediators of the intrinsic apoptotic pathway and a part of the apoptosome, which activates procaspase-3 and promotes cell death. Gene knockout of Apaf1 in mice leads to late embryonic lethality with malformations such as the persistence of interdigital webs and hyperplasia of brain and retina. Therefore, Apaf1 is generally believed to play a crucial role in developmental apoptosis and have a widespread expression. However, its pattern of expression in early development remains unknown. To specify whether Apaf1 indeed plays this key role, we investigated the pattern of gene expression for Apaf1 in mouse embryos on day 7,9, and 12 of development. Our results show, that gene expression for Apafl first occurs within the embryo between day 7 and 9 of development, becoming more widespread toward day 12 and then includes structures, such as yolk sac, mesenchyme, cartilage, heart anlage, otic vesicle, peridermis, and anlagen of the spinal ganglia and vertebral bodies. Our results also show that gene expression for Apaf1 is not ubiquitous in early mouse development. This finding indicates that cell death processes are independent of or less dependent on Apaf1 during this time. Of interest, an active gene expression for Apafl is also present in organ anlagen such as heart or intestine, in which no obvious phenotype is seen after Apafl deletion. This finding suggests a possible role for Apafl in such anlagen as a putative alternative compensatory pathway, which could he switched on in the case of defects in the mediators that are normally involved in such organs. (c) 2005 Wiley-Liss, Inc."],["dc.description.sponsorship","Telethon [TCP99038]"],["dc.identifier.doi","10.1002/dvdy.20534"],["dc.identifier.isi","000231353700022"],["dc.identifier.pmid","16086359"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49920"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1058-8388"],["dc.title","Localization of Apafl1 gene expression in the early development of the mouse by means of in situ reverse transcriptase-polymerase chain reaction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","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","1199"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","HISTOLOGY AND HISTOPATHOLOGY"],["dc.bibliographiccitation.lastpage","1207"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Diedrich, A."],["dc.contributor.author","Bock, Hans-Christoph"],["dc.contributor.author","Koenig, Fatima Barbara"],["dc.contributor.author","Schulz, Thomas G."],["dc.contributor.author","Ludwig, H.-C."],["dc.contributor.author","Herken, R."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.date.accessioned","2018-11-07T09:01:18Z"],["dc.date.available","2018-11-07T09:01:18Z"],["dc.date.issued","2006"],["dc.description.abstract","Glutathione S-transferases (GSTs) play a central role in a number of metabolic processes. Glutathione S-transferase T1 (GSTT1) is a polymorphic cytosolic enzyme and a member of the theta class of GSTs. Typical substrates for GSTT1 are industrial compounds, such as dichloromethane and ethylene oxide. It has been shown that also chemotherapeutic drugs such as BCNU [i.e. 1,3-bis(2-chloroethyl)-1nitrosourea] are efficiently inactivated by GSTT1. BCNU is a drug which is increasingly used locally in the chemotherapy of glioblastoma multiforme WHO grade IV. Therefore, if GSTT1 were expressed in neoplastic cells of brain tumours it could be a factor for chemoresistance. In order to clarify a possible role of GSTT1 in chemoresistance, as a first step, we localized this enzyme in malignant gliomas such as glioblastoma multiforme WHO grade IV and oligodendroglioma WHO grade II. Because of its polymorphism we first genotyped the samples for GSTT1 by PCR. Using in situ hybridization, we then demonstrated that GSTT1 transcripts are expressed in neoplastic cells of both tumour types. Immunohistochemistry revealed then that whereas neoplastic cells in glioblastoma multiforme WHO grade IV contain GSTT1, it was not localized in oligodendroglioma cells. Given the polymorphism of GSTT1 and its potential activity towards BCNU, the localization of GSTT1 in glioblastoma cells can be considered as a possible factor of non-homogeneous chemotherapy response among patients with different GSTT1 genotypes."],["dc.identifier.isi","000239239800008"],["dc.identifier.pmid","16874663"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24391"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","F Hernandez"],["dc.relation.issn","0213-3911"],["dc.title","Expression of glutathione S-transferase T1 (GSTT1) in human brain tumours"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1297"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","1307"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Nico, B."],["dc.contributor.author","Frigeri, A."],["dc.contributor.author","Nicchia, G. P."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Errede, M."],["dc.contributor.author","Ribatti, D."],["dc.contributor.author","Svelto, M."],["dc.contributor.author","Roncali, L."],["dc.date.accessioned","2018-11-07T09:12:56Z"],["dc.date.available","2018-11-07T09:12:56Z"],["dc.date.issued","2001"],["dc.description.abstract","In this study, we have investigated the expression of aquaporin 4 during blood-brain barrier development in the optic tectum of chick embryos and newly hatched chicks, by means of western-blot! reverse transcriptase-polymerase chain reaction, immunohistochemistry, and freeze-fracture and high-resolution immunogold electron microscopy In the optic tecta of day-14 embryos, western blot analysis revealed an approx, 30 kDa band, immunoreactive for aquaporin-4, which was increased in day-20 embryos and in chicks, Semi-quantitative reverse transcriptase chain reaction experiments showed that there was already a high level of aquaporin-4 mRNA in day-9 embryos as well as in the subsequent stages and in newly hatched chicks, Immunohistochemically, reactivity for aquaporin-4 was detected in the optic tectum of day-14 embryos; similar results were obtained in telencephalon and cerebellum, Ultrastructurally; the microvessels of the tectum showed immunoreactivity. for aquaporin-4 on the astroglial endfeet, which discontinuously surrounded endothelial cells joined hy immature tight junctions, In the tectum, telencephalon and cerebellum of 20-day embryos and chicks, aquaporin-4 strongly labeled the ependymal cells and the subpial glial membranes, as well as the bodies and processes of astroglial cells. A continuous aquaporin-4 staining was found around the microvessel endothelial cells, which were sealed off from one another by extensive tight junctions, A complete astrocytic sheath, labeled hg anti-aquaporin-4 gold particles, enveloped the endothelial-pericyte layer. Orthogonal arrays of particles were observed on fractured astrocytic membranes, starting from embryonic day 14 when the aquaporin-4 immunogold staining revealed clusters of gold particles, often forming square or rectangular clusters, The results showed that aquaporin-4 expression and organization of the intramembrane particles in orthogonal arrays followed the same temporal sequence, Finally, the lipopolysaccharide, a substance that induces blood-brain barrier distruption, determines a remarkable reduction in aquaporin-4 labeling, expressed by a few aquaporin-4 gold particles attached on swollen perivascular glial membranes, All these data show that aquaporin-4 expression occurs in the chick embryonic brain, in parallel with maturation and functioning of the blood-brain barrier and suggest that there is a close relationship between water transport regulation and brain development."],["dc.description.sponsorship","Telethon [983]"],["dc.identifier.isi","000168205200007"],["dc.identifier.pmid","11256996"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27058"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0021-9533"],["dc.title","Role of aquaporin-4 water channel in the development and integrity of the blood-brain barrier"],["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"]]