Krügel, Jenny

[["dc.bibliographiccitation.firstpage","272"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cellular Signalling"],["dc.bibliographiccitation.lastpage","283"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Escobar, Jorge Duque"],["dc.contributor.author","Babaeikelishomi, Rohollah"],["dc.contributor.author","Stahnke, Marie-Jeannette"],["dc.contributor.author","Blume, Roland"],["dc.contributor.author","Schroeder, Sabine"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Maedler, Kathrin"],["dc.contributor.author","Kluth, Oliver"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Oetjen, Elke"],["dc.date.accessioned","2018-11-07T10:16:38Z"],["dc.date.available","2018-11-07T10:16:38Z"],["dc.date.issued","2016"],["dc.description.abstract","The dual leucine zipper kinase DLK induces beta-cell apoptosis by inhibiting the transcriptional activity conferred by the beta-cell protective transcription factor cAMP response element binding protein CREB. This action might contribute to beta-cell loss and ultimately diabetes. Within its kinase domain DLK shares high homology with the mixed lineage kinase (MLK) 3, which is activated by tumor necrosis factor (TNF) alpha and interleukin (IL)-1 beta, known prediabetic signals. In the present study, the regulation of DLK in beta-cells by these cytokines was investigated. Both, TNF alpha and IL-1 beta induced the nuclear translocation of DLK. Mutations within a putative nuclear localization signal (NLS) prevented basal and cytokine-induced nuclear localization of DLK and binding to the importin receptor importin alpha, thereby demonstrating a functional NLS within DLK. DLK NLS mutants were catalytically active as they phosphorylated their down-stream kinase c-Jun N-terminal kinase to the same extent as DLK wild-type but did neither inhibit CREB-dependent gene transcription nor transcription conferred by the promoter of the anti-apoptotic protein BCL-xL In addition, the beta-cell apoptosis-inducing effect of DLK was severely diminished by mutation of its NLS. In a murine model of prediabetes, enhanced nuclear DLK was found. These data demonstrate that DLK exerts distinct functions, depending on its subcellular localization and thus provide a novel level of regulating DLK action. Furthermore, the prevention of the nuclear localization of DLK as induced by prediabetic signals with consecutive suppression of beta-cell apoptosis might constitute a novel target in the therapy of diabetes mellitus. (C) 2016 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.cellsig.2016.01.002"],["dc.identifier.isi","000371188000005"],["dc.identifier.pmid","26776303"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41072"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","1873-3913"],["dc.relation.issn","0898-6568"],["dc.title","Distinct functions of the dual leucine zipper kinase depending on its subcellular localization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","452"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","HNO"],["dc.bibliographiccitation.lastpage","458"],["dc.bibliographiccitation.volume","58"],["dc.contributor.author","Matthes, Philipp"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Karapantzou, Chrisanthi"],["dc.contributor.author","Winterhoff, Jan"],["dc.contributor.author","Laskawi, Rainer"],["dc.date.accessioned","2018-11-07T08:43:33Z"],["dc.date.available","2018-11-07T08:43:33Z"],["dc.date.issued","2010"],["dc.description.abstract","There are no regional data about the prevalence and use of botulinum toxin (BoNT) in otorhinolaryngology (ORL) departments in Germany. In order to obtain an overview of the current applications of BoNT in ORL departments a survey was carried out. Standardized multi-choice questionnaires were mailed to 150 ORL departments. In the analysis a differentiation was made between university and regional departments. Also an analysis of the whole collective of respondent hospitals was carried out. The most commonly treated indication is the Frey syndrome followed by hypersalivation due to a salivary fistula after parotidectomy, dysphagia, aesthetic application and laryngeal dystonia. The rate of return was 62% and 75% of all responding hospitals use BoNT as a therapeutic option, especially where \"off-label-use\" indications are concerned (15 out of 20 indications or 75%). BoNT is widely used as a therapeutic option with an increasing trend. Due to different applications a schedule of hospitals would be helpful in order to be able to find the nearest hospital for the appropriate indications."],["dc.identifier.doi","10.1007/s00106-009-2056-3"],["dc.identifier.isi","000277427800007"],["dc.identifier.pmid","20454883"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19998"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0017-6192"],["dc.title","Use of botulinum toxin in ORL departments in Germany"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Fibrogenesis & Tissue Repair"],["dc.bibliographiccitation.lastpage","10"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Girgert, Rainer"],["dc.contributor.author","Martin, Maria"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Temme, Johanna"],["dc.contributor.author","Eckes, Beate"],["dc.contributor.author","Müller, Gerhard-Anton"],["dc.contributor.author","Gross, Oliver"],["dc.date.accessioned","2019-07-09T11:52:48Z"],["dc.date.available","2019-07-09T11:52:48Z"],["dc.date.issued","2010"],["dc.description.abstract","Background: Integrins are important cellular receptors for collagens. Within the glomerulus, podocytes regulate the integrity of the glomerular basement membrane (GBM) by sensing the presence of collagen and regulating collagen IV synthesis. The present study evaluates the role of integrin a2 (ITGA2) in cell-matrix interaction. Methods and Results: ITGA2-deficient mice had normal renal function but moderate proteinuria and enhanced glomerular and tubulointerstitial matrix deposition. Electron microscopy demonstrated irregular podocyte-matrix interaction, causing pathological protrusions towards the urinary (podocyte) side of the GBM. These characteristic subepithelial bulges mimic the renal phenotype of mice, which are deficient in another collagen receptor, discoidin domain receptor (DDR)1. Using immunogold staining, ITGA2 expression was found to localize to the basolateral site of the podocyte foot processes. ITGA2-deficient mice overexpressed transforming growth factor (TGF)b and connective tissue growth factor (CTGF) compared with wild-type mice. Using in situ hybridization, tubular cells were found to be the primary site of TGFb synthesis and podocytes the source of CTGF in ITGA2- deficient mice. Conclusion: These findings support our hypothesis that both these collagen receptors (ITGA2 and DDR1) play a similar role within the kidney. Further, cell-matrix interaction via collagen receptors seems to be crucial for maintenance of normal GBM architecture and function. Targeting collagen receptors such as ITGA2 might be a new form of treatment for progressive fibrotic diseases."],["dc.identifier.doi","10.1186/1755-1536-3-19"],["dc.identifier.fs","575629"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6018"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60281"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","In goescholar not merged with http://resolver.sub.uni-goettingen.de/purl?gs-1/6905 but duplicate"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Integrin a2-deficient mice provide insights into specific functions of collagen receptors in the kidney"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","28"],["dc.bibliographiccitation.journal","Naunyn-Schmiedeberg s Archives of Pharmacology"],["dc.bibliographiccitation.lastpage","29"],["dc.bibliographiccitation.volume","379"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Oetjen, Elke"],["dc.date.accessioned","2018-11-07T08:31:17Z"],["dc.date.available","2018-11-07T08:31:17Z"],["dc.date.issued","2009"],["dc.identifier.isi","000266563200118"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17088"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.conference","50th Annual Meeting of the Deutsche-Gesellschaft-fur-Experimentelle-und-Klinische-Pharmakologie-und Toxikologie"],["dc.relation.eventlocation","Mainz, GERMANY"],["dc.relation.issn","0028-1298"],["dc.title","Translocation of the mitogen-activated triple kinase DLK to the nucleus"],["dc.type","conference_abstract"],["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","2879"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Cellular and Molecular Life Sciences"],["dc.bibliographiccitation.lastpage","2895"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Miosge, Nicolai"],["dc.date.accessioned","2018-08-20T11:39:20Z"],["dc.date.available","2018-08-20T11:39:20Z"],["dc.date.issued","2010"],["dc.description.abstract","More than three decades ago, basement membranes (BMs) were described as membrane-like structures capable of isolating a cell from and connecting a cell to its environment. Since this time, it has been revealed that BMs are specialized extracellular matrices (sECMs) with unique components that support important functions including differentiation, proliferation, migration, and chemotaxis of cells during development. The composition of these sECM is as unique as the tissues to which they are localized, opening the possibility that such matrices can fulfill distinct functions. Changes in BM composition play significant roles in facilitating the development of various diseases. Furthermore, tissues have to provide sECM for their stem cells during development and for their adult life. Here, we briefly review the latest research on these unique sECM and their components with a special emphasis on embryonic and adult stem cells and their niches."],["dc.identifier.doi","10.1007/s00018-010-0367-x"],["dc.identifier.pmid","20428923"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/4965"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15418"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","1420-9071"],["dc.relation.eissn","1420-682X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Basement membrane components are key players in specialized extracellular matrices"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","S205"],["dc.bibliographiccitation.issue","Suppl B"],["dc.bibliographiccitation.journal","Osteoarthritis and Cartilage"],["dc.bibliographiccitation.lastpage","S206"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Koelling, S."],["dc.contributor.author","Kruegel, J."],["dc.contributor.author","Lochte, T."],["dc.contributor.author","Miosge, N."],["dc.date.accessioned","2018-08-20T12:10:57Z"],["dc.date.available","2018-08-20T12:10:57Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1016/S1063-4584(07)60833-4"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15424"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1063-4584"],["dc.title","P389 Chrondrogenic Progenitorcells derived from late stages of Human Osteoarthirtis"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","170"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nature Reviews Nephrology"],["dc.bibliographiccitation.lastpage","178"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Rubel, Diana"],["dc.contributor.author","Gross, Oliver"],["dc.date.accessioned","2018-11-07T09:27:25Z"],["dc.date.available","2018-11-07T09:27:25Z"],["dc.date.issued","2013"],["dc.description.abstract","In 1927, Arthur C. Alport first published his description of a triad of symptoms in a family with hereditary congenital haemorrhagic nephritis, deafness and ocular changes. A few years after his death, this group of symptoms was renamed Alport syndrome. To this day, Alport syndrome still inevitably leads to end-stage renal disease and the need for renal replacement therapy, starting in young adulthood. During the past two decades, research into this rare disease has focused on the effects of mutations in collagen type IV and the role of changes in podocytes and the glomerular basement membrane that lead to early kidney fibrosis. Animal models of Alport syndrome also demonstrate the pathogenetic importance of interactions between podocytes and the extracellular matrix. Such models might also help researchers to answer basic questions about podocyte function and the development of fibrosis, and to develop new therapeutic approaches that might be of use in other kidney diseases. In this Review, we discuss the latest basic and clinical research on Alport syndrome, focusing on the roles of podocyte pathology and the extracellular matrix. We also highlight early diagnosis and treatment options for young patients with this disorder."],["dc.identifier.doi","10.1038/nrneph.2012.259"],["dc.identifier.isi","000316713800010"],["dc.identifier.pmid","23165304"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30531"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1759-5061"],["dc.title","Alport syndrome-insights from basic and clinical research"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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","346"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Matrix Biology"],["dc.bibliographiccitation.lastpage","356"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Gross, Oliver"],["dc.contributor.author","Girgert, Rainer"],["dc.contributor.author","Beirowski, Bogdan"],["dc.contributor.author","Kretzler, Matthias"],["dc.contributor.author","Kang, Hee Gyung"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Busse, Ann-Christin"],["dc.contributor.author","Segerer, Stephan"],["dc.contributor.author","Vogel, Wolfgang F."],["dc.contributor.author","Mueller, Gerhard-Anton"],["dc.contributor.author","Weber, Manfred"],["dc.date.accessioned","2018-11-07T08:42:54Z"],["dc.date.available","2018-11-07T08:42:54Z"],["dc.date.issued","2010"],["dc.description.abstract","Alport syndrome is a hereditary type IV collagen disease leading to progressive renal fibrosis, hearing loss and ocular changes. End stage renal failure usually develops during adolescence. COL4A3-/- mice serve as an animal model for progressive renal scarring in Alport syndrome. The present study evaluates the role of Discoidin Domain Receptor 1 (DDR1) in cell-matrix interaction involved in pathogenesis of Alport syndrome including renal inflammation and fibrosis. DDR1/COL4A3 Double-knockouts were compared to COL4A3-/- mice with 50% or 100% expression of DDR1, wildtype controls and to DDR1-/- COL4A3+/+ controls for over 6 years. Double-knockouts lived 47% longer, mice with 50% DDR1 lived 29% longer and showed improved renal function (reduction in proteinuria and blood urea nitrogen) compared to animals with 100% DDR1 expression. Loss of DDR1 reduced proinflammtory, profibrotic cells via signaling of TGF beta, CTGF, NF kappa B and IL-6 and decreased deposition of extracellular matrix. Immunogold-staining and in-situ hybridisation identified podocytes as major players in DDR1-mediated fibrosis and inflammation within the kidney. In summary, glomerular epithelial cells (podocytes) express DDR1. Loss of DDR1-expression in the kidney delayed renal fibrosis and inflammation in hereditary type IV collagen disease. This supports our hypothesis that podocyte-matrix interaction via collagen receptors plays an important part in progression of renal fibrosis in Alport disease. The blockade of collagen-receptor DDR1 might serve as an important new therapeutic concept in progressive fibrotic and inflammatory diseases in the future. (C) 2010 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.matbio.2010.03.002"],["dc.identifier.isi","000280726400002"],["dc.identifier.pmid","20307660"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19817"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0945-053X"],["dc.title","Loss of collagen-receptor DDR1 delays renal fibrosis in hereditary type IV collagen disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]