Dressel, Ralf

[["dc.bibliographiccitation.firstpage","3957"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Immunology"],["dc.bibliographiccitation.lastpage","3965"],["dc.bibliographiccitation.volume","166"],["dc.contributor.author","Ioannidu, S."],["dc.contributor.author","Walter, L."],["dc.contributor.author","Dressel, Ralf"],["dc.contributor.author","Gunther, E."],["dc.date.accessioned","2018-11-07T09:16:35Z"],["dc.date.available","2018-11-07T09:16:35Z"],["dc.date.issued","2001"],["dc.description.abstract","The rat is an important model for studying organ graft rejection and susceptibility to certain complex diseases. The MHC, the RT1 complex, plays a decisive role in controlling these traits. We have cloned the telomeric class I region of the RT1 complex, RT1-C/E/M, of the BN inbred rat strain in a contig of overlapping pi-derived artificial chromosome clones encompassing similar to2 Mb, and present a physical map of this MHC region, Forty-five class I exon ii-hybridizing BamHI fragments were detected, including the previously known rat class I genes RT1-E, RT-BM1, RT1-N, RT1-M2, RT1-M3 and RT1-M4, Twenty-six non-class I genes known to map to the corresponding part of the human and mouse MHC were tested and could be fine mapped in the RT1-C/E/M region at orthologous position. Four previously known microsatellite markers were fine mapped in the RT1-C/E/M region and found to occur in multiple copies. In addition, a new, single-copy polymorphic microsatellite has been defined. The expression profiles of several class I genes and the 26 non-class I genes were determined in 13 different tissues and exhibited restricted patterns in most cases. The data provide further molecular information on the MHC for analyzing disease susceptibility and underline the usefulness of the rat model."],["dc.identifier.isi","000167437700044"],["dc.identifier.pmid","11238641"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27965"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Immunologists"],["dc.relation.issn","0022-1767"],["dc.title","Physical map and expression profile of genes of the telomeric class I gene region of the rat MHC"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","970"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The Journal of Immunology"],["dc.bibliographiccitation.lastpage","975"],["dc.bibliographiccitation.volume","174"],["dc.contributor.author","Roos, Christian"],["dc.contributor.author","Dressel, Ralf"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Günther, Eberhard"],["dc.contributor.author","Walter, Lutz"],["dc.date.accessioned","2022-10-06T13:26:53Z"],["dc.date.available","2022-10-06T13:26:53Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.4049/jimmunol.174.2.970"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115191"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1550-6606"],["dc.relation.issn","0022-1767"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","The Rat Expresses Two Complement Factor C4 Proteins, but Only One Isotype Is Expressed in the Liver"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1398"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","1411"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Schneppenheim, Janna"],["dc.contributor.author","Huettl, Susann"],["dc.contributor.author","Mentrup, Torben"],["dc.contributor.author","Luellmann-Rauch, Renate"],["dc.contributor.author","Rothaug, Michelle"],["dc.contributor.author","Engelke, Michael"],["dc.contributor.author","Dittmann, Kai"],["dc.contributor.author","Dressel, Ralf"],["dc.contributor.author","Araki, Masatake"],["dc.contributor.author","Araki, Kimi"],["dc.contributor.author","Wienands, Juergen"],["dc.contributor.author","Fluhrer, Regina"],["dc.contributor.author","Saftig, Paul"],["dc.contributor.author","Schroeder, Bernd"],["dc.date.accessioned","2018-11-07T09:42:09Z"],["dc.date.available","2018-11-07T09:42:09Z"],["dc.date.issued","2014"],["dc.description.abstract","We reported recently that the presenilin homologue signal peptide peptidase-like 2a (SPPL2a) is essential for B cell development by cleaving the N-terminal fragment (NTF) of the invariant chain (li, CD74). Based on this, we suggested that pharmacological modulation of SPPL2a may represent a novel approach to deplete B cells in autoimmune disorders. With regard to reported overlapping substrate spectra of SPPL2a and its close homologue, SPPL2b, we investigated the role of SPPL2b in CD74 NTF proteolysis and its impact on B and dendritic cell homeostasis. In heterologous expression experiments, SPPL2b was found to cleave CD74 NTF with an efficiency simliar to that of SPPL2a. For in vivo analysis, SPPL2b single-deficient and SPPL2a/SPPL2b double-deficient mice were generated and examined for CD74 NTF turnover/accumulation, B cell maturation and functionality, and dendritic cell homeostasis. We demonstrate that in vivo SPPL2b does not exhibit a physiologically relevant contribution to CD74 proteolysis in B and dendritic cells. Furthermore, we reveal that both proteases exhibit divergent subcellular localizations in B cells and different expression profiles in murine tissues. These findings suggest distinct functions of SPPL2a and SPPL2b and, based on a high abundance of SPPL2b in brain, a physiological role of this protease in the central nervous system."],["dc.identifier.doi","10.1128/MCB.00038-14"],["dc.identifier.isi","000333338600003"],["dc.identifier.pmid","24492962"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33889"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","The Intramembrane Proteases Signal Peptide Peptidase-Like 2a and 2b Have Distinct Functions In Vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Wiener klinische Wochenschrift"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Novota, P."],["dc.contributor.author","Sviland, Lisbet"],["dc.contributor.author","Opitz, Lennart"],["dc.contributor.author","Hitt, Reiner"],["dc.contributor.author","Dickinson, Anne M."],["dc.contributor.author","Walter, L."],["dc.contributor.author","Dressel, Ralf"],["dc.date.accessioned","2018-11-07T11:12:51Z"],["dc.date.available","2018-11-07T11:12:51Z"],["dc.date.issued","2008"],["dc.format.extent","124"],["dc.identifier.isi","000259367100404"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53754"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.issn","0043-5325"],["dc.title","Major histocompatibility complex (MHC) gene expression profiling of the graft versus host reaction in skin explant assays"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","874"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Cellular and Molecular Medicine"],["dc.bibliographiccitation.lastpage","887"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Stangl, Stefan"],["dc.contributor.author","Gehrmann, Mathias"],["dc.contributor.author","Dressel, Ralf"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Dullin, Christian"],["dc.contributor.author","Themelis, George"],["dc.contributor.author","Ntziachristos, Vasilis"],["dc.contributor.author","Staeblein, Eva"],["dc.contributor.author","Walch, Axel"],["dc.contributor.author","Winkelmann, Isabel"],["dc.contributor.author","Multhoff, Gabriele"],["dc.date.accessioned","2018-11-07T08:57:12Z"],["dc.date.available","2018-11-07T08:57:12Z"],["dc.date.issued","2011"],["dc.description.abstract","The major stress-inducible heat shock protein 70 (Hsp70) is frequently present on the cell surface of human tumours, but not on normal cells. Herein, the binding characteristics of the cmHsp70.1 mouse monoclonal antibody (mAb) were evaluated in vitro and in a syngeneic tumour mouse model. More than 50% of the CT26 mouse colon carcinoma cells express Hsp70 on their cell surface at 4 degrees C. After a temperature shift to 37 degrees C, the cmHsp70.1-fluorescein isothiocyanate mAb translocates into early endosomes and lysosomes. Intraoperative and near-infrared fluorescence imaging revealed an enrichment of Cy5.5-conjugated mAb cmHsp70.1, but not an identically labelled IgG1 isotype-matched control, in i.p. and s.c. located CT26 tumours, as soon as 30 min. after i.v. injection into the tail vein. Due to the rapid turnover rate of membrane-bound Hsp70, the fluorescence-labelled cmHsp70.1 mAb became endocytosed and accumulated in the tumour, reaching a maximum after 24 hrs and remained detectable at least up to 96 hrs after a single i.v. injection. The tumour-selective internalization of mAb cmHsp70.1 at the physiological temperature of 37 degrees C might enable a targeted uptake of toxins or radionuclides into Hsp70 membrane-positive tumours. The anti-tumoral activity of the cmHsp70.1 mAb is further supported by its capacity to mediate antibody-dependent cytotoxicity."],["dc.identifier.doi","10.1111/j.1582-4934.2010.01067.x"],["dc.identifier.isi","000290312700015"],["dc.identifier.pmid","20406322"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23338"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1582-1838"],["dc.title","In vivo imaging of CT26 mouse tumours by using cmHsp70.1 monoclonal antibody"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Tissue Antigens"],["dc.bibliographiccitation.volume","84"],["dc.contributor.author","Monecke, Sebastian"],["dc.contributor.author","Hamann, Carina"],["dc.contributor.author","Elsner, Leslie"],["dc.contributor.author","Nolte, Jessica"],["dc.contributor.author","Engel, Wolfgang"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Guan, Kaomei"],["dc.contributor.author","Mansouri, Ahmed"],["dc.contributor.author","Dressel, Ralf"],["dc.date.accessioned","2018-11-07T09:38:32Z"],["dc.date.available","2018-11-07T09:38:32Z"],["dc.date.issued","2014"],["dc.format.extent","5"],["dc.identifier.isi","000337546000002"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33083"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Stockholm, SWEDEN"],["dc.relation.issn","1399-0039"],["dc.relation.issn","0001-2815"],["dc.title","PLURIPOTENT STEM CELLS VARYING IN A SINGLE MINOR HISTOCOMPATIBILITY ANTIGEN ELICIT CELLULAR AND HUMORAL IMMUNE RESPONSES THAT CAN MEDIATE GRAFT REJECTION"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5523"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The Journal of Immunology"],["dc.bibliographiccitation.lastpage","5533"],["dc.bibliographiccitation.volume","179"],["dc.contributor.author","Elsner, Leslie"],["dc.contributor.author","Muppala, Vijayakumar"],["dc.contributor.author","Gehrmann, Mathias"],["dc.contributor.author","Lozano, Jingky"],["dc.contributor.author","Malzahn, Dörthe"],["dc.contributor.author","Bickeböller, Heike"],["dc.contributor.author","Brunner, Edgar"],["dc.contributor.author","Zientkowska, Marta"],["dc.contributor.author","Herrmann, Thomas"],["dc.contributor.author","Walter, Lutz"],["dc.contributor.author","Dressel, Ralf"],["dc.date.accessioned","2022-06-08T07:57:36Z"],["dc.date.available","2022-06-08T07:57:36Z"],["dc.date.issued","2007"],["dc.description.abstract","The stress-inducible heat shock protein (HSP) 70 is known to function as an endogenous danger signal that can increase the immunogenicity of tumors and induce CTL responses. We show in this study that HSP70 also activates mouse NK cells that recognize stress-inducible NKG2D ligands on tumor cells. Tumor size and the rate of metastases derived from HSP70-overexpressing human melanoma cells were found to be reduced in T and B cell-deficient SCID mice, but not in SCID/beige mice that lack additionally functional NK cells. In the SCID mice with HSP70-overexpressing tumors, NK cells were activated so that they killed ex vivo tumor cells that expressed NKG2D ligands. In the tumors, the MHC class I chain-related (MIC) A and B molecules were found to be expressed. Interestingly, a counter selection was observed against the expression of MICA/B in HSP70-overexpressing tumors compared with control tumors in SCID, but not in SCID/beige mice, suggesting a functional relevance of MICA/B expression. The melanoma cells were found to release exosomes. HSP70-positive exosomes from the HSP70-overexpressing cells, in contrast to HSP70-negative exosomes from the control cells, were able to activate mouse NK cells in vitro to kill YAC-1 cells, which express NKG2D ligands constitutively, or the human melanoma cells, in which MICA/B expression was induced. Thus, HSP70 and inducible NKG2D ligands synergistically promote the activation of mouse NK cells resulting in a reduced tumor growth and suppression of metastatic disease."],["dc.identifier.doi","10.4049/jimmunol.179.8.5523"],["dc.identifier.isi","000250099400061"],["dc.identifier.pmid","17911639"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/110150"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.eissn","1550-6606"],["dc.relation.issn","0022-1767"],["dc.title","The Heat Shock Protein HSP70 Promotes Mouse NK Cell Activity against Tumors That Express Inducible NKG2D Ligands"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","497"],["dc.bibliographiccitation.lastpage","512"],["dc.bibliographiccitation.seriesnr","631"],["dc.contributor.author","Elsner, Leslie"],["dc.contributor.author","Dressel, Ralf"],["dc.date.accessioned","2021-04-21T11:15:34Z"],["dc.date.available","2021-04-21T11:15:34Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1016/bs.mie.2019.05.037"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84259"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/335"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | C05: Bedeutung von zellulären Immunreaktionen für das kardiale Remodeling und die Therapie der Herzinsuffizienz durch Stammzelltransplantation"],["dc.relation.crisseries","Methods in Enzymology"],["dc.relation.isbn","9780128186732"],["dc.relation.ispartof","Tumor Immunology and Immunotherapy – Cellular Methods Part A"],["dc.relation.ispartofseries","Methods in Enzymology; 631"],["dc.relation.workinggroup","RG Dressel"],["dc.title","51Cr-release to monitor NK cell cytotoxicity"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Immunology"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Dressel, Ralf"],["dc.contributor.author","Greinix, Hildegard T."],["dc.contributor.author","Holler, Ernst"],["dc.contributor.author","Dickinson, Anne M."],["dc.date.accessioned","2020-12-10T18:44:24Z"],["dc.date.available","2020-12-10T18:44:24Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.3389/fimmu.2018.01966"],["dc.identifier.eissn","1664-3224"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78441"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Editorial: Cellular Therapies: Past, Present and Future"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","editorial_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20200"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","20210"],["dc.bibliographiccitation.volume","279"],["dc.contributor.author","Dressel, Ralf"],["dc.contributor.author","Raja, S. M."],["dc.contributor.author","Honing, S."],["dc.contributor.author","Seidler, Tim"],["dc.contributor.author","Froelich, C. J."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Gunther, E."],["dc.date.accessioned","2018-11-07T10:49:00Z"],["dc.date.available","2018-11-07T10:49:00Z"],["dc.date.issued","2004"],["dc.description.abstract","Cytotoxic T lymphocytes (CTL) and natural killer cells secrete granzymes to kill infected or transformed cells. The mannose 6-phosphate receptor (Mpr) 300 on target cells has been reported to function as receptor for secreted granzyme B. Using lymphoblasts and mouse embryonal fibroblast lines from Mpr300 and Mpr46 knockout mice, we show here that both receptors are not essential for CTL-induced apoptosis. Similarly, cells exposed to either monomeric granzyme B or granzyme B-serglycin complexes readily internalize the granzyme and undergo apoptosis in the absence of Mpr300 and Mpr46. Further, no colocalization of granzyme B and Mpr300 could be observed in target cells after internalization. In conclusion, these results strongly argue against an Mpr300- or Mpr46-dependent pathway of granzyme-mediated killing and provide new insight in the internalization of monomeric and complexed granzyme B."],["dc.identifier.doi","10.1074/jbc.M313108200"],["dc.identifier.isi","000221164500097"],["dc.identifier.pmid","14985351"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48328"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Granzyme-mediated cytotoxicity does not involve the mannose 6-phosphate receptors on target cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]