Vasko, Radovan

[["dc.bibliographiccitation.firstpage","222"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Therapeutic Apheresis and Dialysis"],["dc.bibliographiccitation.lastpage","225"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Koziolek, Michael"],["dc.contributor.author","Fuezesi, Laszlo"],["dc.contributor.author","Koenig, Fatima"],["dc.contributor.author","Strutz, Frank M."],["dc.contributor.author","Mueller, Gerhard Anton"],["dc.date.accessioned","2018-11-07T08:44:57Z"],["dc.date.available","2018-11-07T08:44:57Z"],["dc.date.issued","2010"],["dc.description.abstract","We report a case of a 27-year-old female with thrombotic microangiopathy as an initial presentation of an unexpected disseminated gastric carcinoma. Based on clinical features and laboratory findings, thrombotic thrombocytopenic purpura (TTP) was diagnosed and plasma exchange started. However, she had responded poorly to plasmapheresis, developed multiorgan failure and died 72 h after admission. Autopsy revealed a disseminated gastric adenocarcinoma with metastatic infiltration of dura mater and disseminated tumor cell emboli in the microcirculation of the liver and lungs. Genetic analysis revealed amplification of KRAS oncogene and aberrations in DCC tumor suppressor gene, which can explain the young age and advanced disease at presentation. The role of plasmapheresis in cancer-associated TTP is uncertain. Plasmapheresis delivers fresh coagulation factors and may theoretically promote microthrombi formation and lead to worsening of the disease. Thrombotic thrombocytopenic purpura seems to be a late and prognostically poor manifestation of an underlying malignancy, with majority of patients dying soon after diagnosis. It is important to be aware of this possibility in thrombotic microangiopathy, especially with atypical features and poor response to standard treatment."],["dc.identifier.doi","10.1111/j.1744-9987.2009.00710.x"],["dc.identifier.isi","000276036600014"],["dc.identifier.pmid","20438546"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20315"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","1744-9979"],["dc.title","Fulminant Plasmapheresis-refractory Thrombotic Microangiopathy Associated With Advanced Gastric Cancer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","217"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Antioxidants and Redox Signaling"],["dc.bibliographiccitation.lastpage","231"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Vasko, Radovan"],["dc.date.accessioned","2018-11-07T10:11:19Z"],["dc.date.available","2018-11-07T10:11:19Z"],["dc.date.issued","2016"],["dc.description.abstract","Significance: Peroxisomes are organelles present in most eukaryotic cells. The organs with the highest density of peroxisomes are the liver and kidneys. Peroxisomes possess more than fifty enzymes and fulfill a multitude of biological tasks. They actively participate in apoptosis, innate immunity, and inflammation. In recent years, a considerable amount of evidence has been collected to support the involvement of peroxisomes in the pathogenesis of kidney injury. Recent Advances: The nature of the two most important peroxisomal tasks, beta-oxidation of fatty acids and hydrogen peroxide turnover, functionally relates peroxisomes to mitochondria. Further support for their communication and cooperation is furnished by the evidence that both organelles share the components of their division machinery. Until recently, the majority of studies on the molecular mechanisms of kidney injury focused primarily on mitochondria and neglected peroxisomes. Critical Issues: The aim of this concise review is to introduce the reader to the field of peroxisome biology and to provide an overview of the evidence about the contribution of peroxisomes to the development and progression of kidney injury. The topics of renal ischemia-reperfusion injury, endotoxin-induced kidney injury, diabetic nephropathy, and tubulointerstitial fibrosis, as well as the potential therapeutic implications of peroxisome activation, are addressed in this review. Future Directions: Despite recent progress, further studies are needed to elucidate the molecular mechanisms induced by dysfunctional peroxisomes and the role of the dysregulated mitochondria-peroxisome axis in the pathogenesis of renal injury."],["dc.identifier.doi","10.1089/ars.2016.6666"],["dc.identifier.isi","000380271000004"],["dc.identifier.pmid","26972522"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40014"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Mary Ann Liebert, Inc"],["dc.relation.issn","1557-7716"],["dc.relation.issn","1523-0864"],["dc.title","Peroxisomes and Kidney Injury"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs219014"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Rubel, Diana"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2020-12-10T18:41:52Z"],["dc.date.available","2020-12-10T18:41:52Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1242/jcs.219014"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77711"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation.iserratumof","/handle/2/29071"],["dc.title","Correction: Secretion of ERP57 is important for extracellular matrix accumulation and progression of renal fibrosis, and is an early sign of disease onset (doi:10.1242/jcs.125088)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1215"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Mini Reviews in Medicinal Chemistry"],["dc.bibliographiccitation.lastpage","1228"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Koziolek, M."],["dc.contributor.author","Vasko, R."],["dc.contributor.author","Bramlage, C."],["dc.contributor.author","Muller, G."],["dc.contributor.author","Strutz, F."],["dc.date.accessioned","2021-06-01T10:48:35Z"],["dc.date.available","2021-06-01T10:48:35Z"],["dc.date.issued","2009"],["dc.description.abstract","The chemokine CX3C-L/FKN is expressed in both soluble and transmembrane/mucin hybrid forms, thus combining chemoattractant functions together with receptor/adhesion molecule properties. In contrast to other chemokine receptors, CX3C-R is expressed not only on lymphoid cell populations, but also on several intrinsic cells including tubular epithelial cells and renal fibroblasts where it regulates various aspects of cell viability, matrix synthesis and degradation, migration, inflammation as well as oxidative stress. In the kidney, the chemokines/receptor pair has been shown to play a role in nephrogenesis as well as in the pathogenesis primary and secondary nephropathies. In several animal models and human specimens with acute and chronic renal failure including allograft nephropathy, CX3C-L/CX3C-R has been shown to exert immune and non-immune mediated renal damages. A blockade of this chemokine system ameliorated acute and chronic renal damages, though the latter to a more robust extent. There seems to a role of the CX3C-L/CX3C-R pair in mediating acute renal inflammation as well as in progressive chronic renal failure. However, functional studies are lacking for many aspects and further studies are necessary to better define the functional properties of CX3 C-L/FKN and its receptor."],["dc.identifier.doi","10.2174/138955709789055252"],["dc.identifier.isi","000271619500007"],["dc.identifier.pmid","19817712"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85989"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Bentham Science Publ Ltd"],["dc.relation.issn","1389-5575"],["dc.title","The CX3C-Chemokine Fractalkine in Kidney Diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","276"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of the American Society of Nephrology"],["dc.bibliographiccitation.lastpage","291"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Xavier, Sandhya"],["dc.contributor.author","Chen, Jun"],["dc.contributor.author","Lin, Chi Hua Sarah"],["dc.contributor.author","Ratliff, Brian B."],["dc.contributor.author","Rabadi, May M."],["dc.contributor.author","Maizel, Julien"],["dc.contributor.author","Tanokuchi, Rina"],["dc.contributor.author","Zhang, Frank"],["dc.contributor.author","Cao, Jian"],["dc.contributor.author","Goligorsky, Michael S."],["dc.date.accessioned","2018-11-07T09:43:53Z"],["dc.date.available","2018-11-07T09:43:53Z"],["dc.date.issued","2014"],["dc.description.abstract","Sirtuin 1 (SIRT1) depletion in vascular endothelial cells mediates endothelial dysfunction and premature senescence in diverse cardiovascular and renal diseases. However, the molecular mechanisms underlying these pathologic effects remain unclear. Here, we examined the phenotype of a mouse model of vascular senescence created by genetically ablating exon 4 of Sirt1 in endothelial cells (Sirt1(endo-/-)). Under basal conditions, Sirt1(endo-/-) mice showed impaired endothelium-dependent vasorelaxation and angiogenesis, and fibrosis occurred spontaneously at low levels at an early age. In contrast, induction of nephrotoxic stress (acute and chronic folic acid-induced nephropathy) in Sirt1(endo-/-) mice resulted in robust acute renal functional deterioration followed by an exaggerated fibrotic response compared with control animals. Additional studies identified matrix metalloproteinase-14 (MMP-14) as a target of SIRT1. In the kidneys of Sirt1(endo-/-) mice, impaired angiogenesis, reduced matrilytic activity, and retention of the profibrotic cleavage substrates tissue transglutaminase and endoglin accompanied MMP-14 suppression. Furthermore, restoration of MMP-14 expression in SIRT1-depeleted mice improved angiogenic and matrilytic functions of the endothelium, prevented renal dysfunction, and attenuated nephrosclerosis. Our findings establish a novel mechanistic molecular link between endothelial SIRT1 depletion, downregulation of MMP-14, and the development of nephrosclerosis."],["dc.identifier.doi","10.1681/ASN.2013010069"],["dc.identifier.isi","000337971700011"],["dc.identifier.pmid","24136919"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34274"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Nephrology"],["dc.relation.issn","1533-3450"],["dc.relation.issn","1046-6673"],["dc.title","Endothelial Sirtuin 1 Deficiency Perpetrates Nephrosclerosis through Downregulation of Matrix Metalloproteinase-14: Relevance to Fibrosis of Vascular Senescence"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","H1691"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","AJP Heart and Circulatory Physiology"],["dc.bibliographiccitation.lastpage","H1704"],["dc.bibliographiccitation.volume","307"],["dc.contributor.author","Maizel, Julien"],["dc.contributor.author","Xavier, Sandhya"],["dc.contributor.author","Chen, Jun"],["dc.contributor.author","Lin, Chi Hua Sarah"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Goligorsky, Michael S."],["dc.date.accessioned","2018-11-07T09:31:15Z"],["dc.date.available","2018-11-07T09:31:15Z"],["dc.date.issued","2014"],["dc.description.abstract","Discordant myocardial growth and angiogenesis can explain left ventricular (LV) hypertrophy progressing toward heart failure with aging. Sirtuin 1 expression declines with age; therefore we explored the role played by angiogenesis and Sirtuin 1 in the development of cardiomyopathy. We compared the cardiac function of 10-to 15-wk-old (wo), 30-40 wo, and 61-70 wo endothelial Sirtuin 1-deleted (Sirt1(endo-/-)) mice and their corresponding knockout controls (Sirt1(Flox)/(Flox)). After 30-40 wk, Sirt1(endo-/)-animals exhibited diastolic dysfunction (DD), decreased mRNA expression of Serca2a in the LV, and decreased capillary density compared with control animals despite a similar VEGFa mRNA expression. However, LV fibrosis and hypoxia-inducible factor (HIF)1 alpha expression were not different. The creation of a transverse aortic constriction (TAC) provoked more severe DD and LV fibrosis in Sirt1(endo-/)-compared with control TAC animals. Although the VEGFa mRNA expression was not different and the protein expression of HIF1 alpha was higher in the Sirt1(endo-/)-TAC animals, capillary density remained reduced. In cultured endothelial cells administration of Sirtuin 1 inhibitor decreased mRNA expression of VEGF receptors FLT 1 and FLK 1. Ex vivo capillary sprouting from aortic explants showed impaired angiogenic response to VEGF in the Sirt1(endo-/-) mice. In conclusion, the data demonstrate 1) a defect in angiogenesis preceding development of DD; 2) dispensability of endothelial Sirtuin 1 under unstressed conditions and during normal aging; and 3) impaired angiogenic adaptation and aggravated DD in Sirt1(endo-/-) mice challenged with LV overload."],["dc.identifier.doi","10.1152/ajpheart.00281.2014"],["dc.identifier.isi","000346478200002"],["dc.identifier.pmid","25239805"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31500"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1522-1539"],["dc.relation.issn","0363-6135"],["dc.title","Sirtuin 1 ablation in endothelial cells is associated with impaired angiogenesis and diastolic dysfunction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","International Journal of Obesity"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Schulz, Egbert Godehard"],["dc.contributor.author","Hesse, A. K."],["dc.contributor.author","Popov, A."],["dc.contributor.author","Ibrovic, S."],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Fischer, N."],["dc.contributor.author","Bargfeldt, M."],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2018-11-07T10:55:21Z"],["dc.date.available","2018-11-07T10:55:21Z"],["dc.date.issued","2005"],["dc.format.extent","S11"],["dc.identifier.isi","000233803400044"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49767"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.publisher.place","London"],["dc.relation.conference","4th International Symposium on Obesity and Hypertension"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","0307-0565"],["dc.title","The possible role of an endothelin-1-gene-polymorphism in the promotor region for severe essential hypertension, atherosclerosis and vascular events"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Hypertension"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Schulz, Egbert Godehard"],["dc.contributor.author","Bahri, S."],["dc.contributor.author","Freudenthaler, S."],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Ibrovic, S."],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2018-11-07T10:38:40Z"],["dc.date.available","2018-11-07T10:38:40Z"],["dc.date.issued","2003"],["dc.format.extent","S66"],["dc.identifier.isi","000184406700229"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45865"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.publisher.place","Philadelphia"],["dc.relation.conference","13th European Meeting on Hypertension"],["dc.relation.eventlocation","MILAN, ITALY"],["dc.relation.issn","0263-6352"],["dc.title","Candesartan in hypertensive patients on hemodialysis"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","96"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Kidney International"],["dc.bibliographiccitation.lastpage","109"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Heeg, MHJ"],["dc.contributor.author","Koziolek, Michael Johann"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Schaefer, L."],["dc.contributor.author","Sharma, K."],["dc.contributor.author","Mueller, Gerhard A."],["dc.contributor.author","Strutz, Frank M."],["dc.date.accessioned","2018-11-07T09:23:04Z"],["dc.date.available","2018-11-07T09:23:04Z"],["dc.date.issued","2005"],["dc.description.abstract","Background. The peptide hormone relaxin has been demonstrated to exert antifibrotic effects in renal and extrarenal tissues. The aims of this study were to identify potential anti-fibrotic effects of relaxin on human renal fibroblasts in vitro and to analyze their mechanisms. Methods. All experiments were performed in established renal fibroblast cell lines and in primary cortical fibroblasts. Effects of relaxin were analyzed on cell proliferation, apoptosis, activation of renal fibroblasts, synthesis and secretion of collagen type I and fibronectin, as well as on the secretion of matrix metalloproteinases (MMPs). Effects on transforming growth factor-beta 1 (TGF-beta 1) receptor binding were analyzed by flow cytometry and on TGF-beta 1 signal transduction by immunoblot analyses for Smad4 and 7, translocation from cytosol to nucleus for Smad2 and 3 as well as for phosphorylated and unphosphorylated forms of p38, c-Jun NH2 terminal kinase (JNK) and extracellular-regulated protein kinase (ERK). Finally, specific siRNAs for Smad2 and 3 were applied to assess the signal transduction pathway. Results. After stimulation with relaxin, tyrosine phosphorylation of a 220 kD protein was demonstrated, indicating interaction with the receptor. Relaxin had only modest inhibitory effects on cell proliferation, and no effects on apoptosis. Conversely, relaxin exerted robust effects on TGF-beta 1-induced fibroblast to myofibroblast transformation as well as on matrix synthesis and secretion even at the smallest dose tested. The secretion of MMP-2 and MMP-9 was induced noticeably by all investigated relaxin concentrations. TGF-beta 1 receptor binding was not influenced by relaxin; however, it prevented Smad2 phosphorylation, translocation to nucleus, and complex formation between Smad2 and 3 indicating a possible interaction with TGF-beta 1 signaling. These findings were corroborated by studies using siRNAs to Smad2 and 3 where siRNA to Smad2 but not to Smad3 inhibited the TGF-beta 1 induction of fibronectin synthesis. There was no influence of relaxin on intracellular Smad3, Smad4, and Smad7 translocation or phosphorylation of mitogen-activated protein (MAP) kinases. Conclusion. Relaxin is a potent inhibitor of TGF-beta 1-induced extracellular matrix (ECM) synthesis and secretion as well as fibroblast activation. Furthermore, it induces ECM degradation by induction of MMP-2 and MMP-9. These effects are mediated, at least in part, by inhibition of TGF-beta 1 signaling."],["dc.identifier.doi","10.1111/j.1523-1755.2005.00384.x"],["dc.identifier.isi","000229636800009"],["dc.identifier.pmid","15954899"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29491"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing Inc"],["dc.relation.issn","0085-2538"],["dc.title","The antifibrotic effects of relaxin in human renal fibroblasts are mediated in part by inhibition of the Smad2 pathway"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","51"],["dc.bibliographiccitation.journal","Nephrology Dialysis Transplantation"],["dc.bibliographiccitation.lastpage","52"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Vasko, Radovan"],["dc.contributor.author","Koziolek, Michael"],["dc.contributor.author","Kurz, Bernd"],["dc.contributor.author","Mueller, Gerhard Anton"],["dc.contributor.author","Strutz, Frank M."],["dc.date.accessioned","2018-11-07T09:38:39Z"],["dc.date.available","2018-11-07T09:38:39Z"],["dc.date.issued","2006"],["dc.identifier.isi","000239919000138"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33113"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.eventlocation","Glasgow, SCOTLAND"],["dc.relation.issn","0931-0509"],["dc.title","Hyperglycemia induces the expression of basic fibroblast growth factor (FGF-2) through activation of the protein kinase C beta-1 and p65 nf-kappa b in human renal fibroblasts"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]