König, Melanie

[["dc.bibliographiccitation.firstpage","2858"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","2863"],["dc.bibliographiccitation.volume","101"],["dc.contributor.author","Schuette, C. G."],["dc.contributor.author","Hatsuzawa, K."],["dc.contributor.author","Margittai, M."],["dc.contributor.author","Stein, A."],["dc.contributor.author","Riedel, D."],["dc.contributor.author","Kuster, P."],["dc.contributor.author","Konig, M."],["dc.contributor.author","Seidel, C."],["dc.contributor.author","Jahn, R."],["dc.date.accessioned","2021-06-01T10:51:03Z"],["dc.date.available","2021-06-01T10:51:03Z"],["dc.date.issued","2004"],["dc.identifier.doi","10.1073/pnas.0400044101"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86875"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.title","Determinants of liposome fusion mediated by synaptic SNARE proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","143"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Developmental and comparative immunology"],["dc.bibliographiccitation.lastpage","150"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Gamil, A. A. A."],["dc.contributor.author","Guo, T.-C."],["dc.contributor.author","König, M."],["dc.contributor.author","Evensen, O."],["dc.date.accessioned","2019-07-09T11:40:44Z"],["dc.date.available","2019-07-09T11:40:44Z"],["dc.date.issued","2015"],["dc.description.abstract","Prostaglandin E2 (PGE2) is an important lipid mediator that plays diverse functions in mammals. Four receptor subtypes of PGE2, designated EP1-4, have been identified to mediate its signaling pathways. Extensive studies of PGE2 and its receptors have been carried out in mammals, but little is known in fish, including Atlantic salmon. In the current study, the distribution of Atlantic salmon EP4 receptor in different tissues was investigated using RT- and real-time PCR. A custom made antibody was used to investigate the distribution of this receptor in different tissues. Quantitative analysis by real-time PCR revealed that the expression was more abundant in the spleen followed by head kidney, skin and fin while it was least expressed in heart, muscles and brain. The staining intensity obtained by immunohistochemistry correlated with the RT-PCR results. EP4 expression was strongly associated with the immune cells in different tissues. To our knowledge, this is the first study to describe the distribution of EP4 receptor in Atlantic salmon tissues. Our findings suggest that EP4 may play a role in mediating immune responses as observed in mammals."],["dc.identifier.doi","10.1016/j.dci.2014.09.013"],["dc.identifier.pmid","25307202"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11232"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58237"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1879-0089"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/3.0"],["dc.title","Distribution of EP4 receptor in different Atlantic salmon (Salmo salar L.) tissues."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0120483"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PloS one"],["dc.bibliographiccitation.lastpage","e0120483"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Guo, Tz Chun"],["dc.contributor.author","Gamil, Amr Ahmed Abdelrahim"],["dc.contributor.author","Koenig, Melanie"],["dc.contributor.author","Evensen, Øystein"],["dc.date.accessioned","2019-07-09T11:41:10Z"],["dc.date.available","2019-07-09T11:41:10Z"],["dc.date.issued","2015"],["dc.description.abstract","PGE2 plays an important role in a broad spectrum of physiological and pathological processes mediated through a membrane-bound G protein-coupled receptor (GPCR) called EP receptor. In mammals, four subtypes of EP receptor (EP 1-4) are identified and each of them functions through different signal transduction pathways. Orthologous EP receptors have also been identified in other non-mammalian species, such as chicken and zebrafish. EP4 is the only identified PGE2 receptor to date in Atlantic salmon but its tissue distribution and function have not been studied in any detail. In this study, we first sequenced EP4 receptor in different tissues and found that the presence of the 3nt deletion in the 5' untranslated region was accompanied by silent mutation at nt 668. While attempting to amplify the same sequence in TO cells (an Atlantic salmon macrophage-like cell line), we failed to obtain the full-length product. Further investigation revealed different isoform of EP4 receptor in TO cells and we subsequently documented its presence in different Atlantic salmon tissues. These two isoforms of EP4 receptor share high homology in their first half of sequence but differ in the second half part with several deletion segments though the final length of coding sequence is the same for two isoforms. We further studied the immunomodulation effect of PGE2 in TO cells and found that PGE2 inhibited the induction of CXCL-10, CCL-4, IL-8 and IL-1β genes expression in a time dependent manner and without cAMP upregulation."],["dc.identifier.doi","10.1371/journal.pone.0120483"],["dc.identifier.pmid","25837516"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11759"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58364"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Sequence Analysis and Identification of New Isoform of EP4 Receptors in Different Atlantic Salmon Tissues (Salmo salar L.) and Its Role in PGE2 Induced Immunomodulation In Vitro."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2564"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Molecular biology of the cell"],["dc.bibliographiccitation.lastpage","2578"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Luo, L."],["dc.contributor.author","Hannemann, M."],["dc.contributor.author","Koenig, S."],["dc.contributor.author","Hegermann, J."],["dc.contributor.author","Ailion, M."],["dc.contributor.author","Cho, M.-K."],["dc.contributor.author","Sasidharan, N."],["dc.contributor.author","Zweckstetter, M."],["dc.contributor.author","Rensing, S. A."],["dc.contributor.author","Eimer, S."],["dc.date.accessioned","2012-10-22T14:47:20Z"],["dc.date.accessioned","2021-10-27T13:11:00Z"],["dc.date.available","2012-10-22T14:47:20Z"],["dc.date.available","2021-10-27T13:11:00Z"],["dc.date.issued","2011-07-15"],["dc.description.abstract","In yeast the Golgi-associated retrograde protein (GARP) complex is required for tethering of endosome-derived transport vesicles to the late Golgi. It consists of four subunits--Vps51p, Vps52p, Vps53p, and Vps54p--and shares similarities with other multimeric tethering complexes, such as the conserved oligomeric Golgi (COG) and the exocyst complex. Here we report the functional characterization of the GARP complex in the nematode Caenorhabditis elegans. Furthermore, we identified the C. elegans Vps51 subunit, which is conserved in all eukaryotes. GARP mutants are viable but show lysosomal defects. We show that GARP subunits bind specific sets of Golgi SNAREs within the yeast two-hybrid system. This suggests that the C. elegans GARP complex also facilitates tethering as well as SNARE complex assembly at the Golgi. The GARP and COG tethering complexes may have overlapping functions for retrograde endosome-to-Golgi retrieval, since loss of both complexes leads to a synthetic lethal phenotype."],["dc.identifier.doi","10.1091/mbc.E10-06-0493"],["dc.identifier.fs","580298"],["dc.identifier.pmid","21613545"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8148"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91551"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","1939-4586"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.mesh","Amino Acid Sequence"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Caenorhabditis elegans"],["dc.subject.mesh","Caenorhabditis elegans Proteins"],["dc.subject.mesh","Conserved Sequence"],["dc.subject.mesh","Endosomes"],["dc.subject.mesh","Golgi Apparatus"],["dc.subject.mesh","Lysosomes"],["dc.subject.mesh","Molecular Sequence Data"],["dc.subject.mesh","Multiprotein Complexes"],["dc.subject.mesh","Phylogeny"],["dc.subject.mesh","SNARE Proteins"],["dc.subject.mesh","Transport Vesicles"],["dc.subject.mesh","Two-Hybrid System Techniques"],["dc.subject.mesh","Vesicular Transport Proteins"],["dc.title","The Caenorhabditis elegans GARP complex contains the conserved Vps51 subunit and is required to maintain lysosomal morphology."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","2149"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific reports"],["dc.bibliographiccitation.lastpage","19"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Burk, Katja"],["dc.contributor.author","Fischer, André"],["dc.contributor.author","Murdoch, John D"],["dc.contributor.author","Koenig, Melanie"],["dc.contributor.author","Bharat, Vinita"],["dc.contributor.author","Markworth, Ronja"],["dc.contributor.author","Burkhardt, Susanne"],["dc.contributor.author","Dean, Camin"],["dc.date.accessioned","2018-01-09T14:36:50Z"],["dc.date.available","2018-01-09T14:36:50Z"],["dc.date.issued","2017-05-19"],["dc.description.abstract","The sorting of activated receptors into distinct endosomal compartments is essential to activate specific signaling cascades and cellular events including growth and survival. However, the proteins involved in this sorting are not well understood. We discovered a novel role of EndophilinAs in sorting of activated BDNF-TrkB receptors into late endosomal compartments. Mice lacking all three EndophilinAs accumulate Rab7-positive late endosomes. Moreover, EndophilinAs are differentially localized to, co-traffic with, and tubulate, distinct endosomal compartments: In response to BDNF, EndophilinA2 is recruited to both early and late endosomes, EndophilinA3 is recruited to Lamp1-positive late endosomes, and co-trafficks with Rab5 and Rab7 in both the presence and absence of BDNF, while EndophilinA1 colocalizes at lower levels with endosomes. The absence of all three EndophilinAs caused TrkB to accumulate in EEA1 and Rab7-positive endosomes, and impaired BDNF-TrkB-dependent survival signaling cascades. In addition, EndophilinA triple knockout neurons exhibited increased cell death which could not be rescued by exogenous BDNF, in a neurotrophin-dependent survival assay. Thus, EndophilinAs differentially regulate activated receptor sorting via distinct endosomal compartments to promote BDNF-dependent cell survival."],["dc.identifier.doi","10.1038/s41598-017-02202-4"],["dc.identifier.pmid","28526875"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14709"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11603"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","EndophilinAs regulate endosomal sorting of BDNF-TrkB to mediate survival signaling in hippocampal neurons"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3463"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Immunology (Baltimore, Md. : 1950)"],["dc.bibliographiccitation.lastpage","3469"],["dc.bibliographiccitation.volume","193"],["dc.contributor.author","Aas, Ida Bergva"],["dc.contributor.author","Austbø, Lars"],["dc.contributor.author","König, Melanie"],["dc.contributor.author","Syed, Mohasina"],["dc.contributor.author","Falk, Knut"],["dc.contributor.author","Hordvik, Ivar"],["dc.contributor.author","Koppang, Erling O."],["dc.date.accessioned","2019-02-27T13:14:38Z"],["dc.date.available","2019-02-27T13:14:38Z"],["dc.date.issued","2014"],["dc.description.abstract","Previously, our group has shown that the interbranchial lymphoid tissue (ILT) is a distinct structure largely consisting of T cells embedded in a meshwork of epithelial cells, with no direct resemblance to previously described lymphoid tissues. In this study, we aim to focus on the T cell population and the possibility of the ILT being a thymus analog. By characterizing structural responsiveness to Ag challenge, the presence of recombination activating genes, and different T cell-related transcripts, we attempt to further approach the immunological function of the ILT in salmonid gills. In addition to eight healthy individuals, a group of eight infectious salmon anemia virus-challenged fish were included to observe T cell responses related to infection. The results showed reduced size of ILT in the infected group, no expression of RAG-1 and -2, and a high degree of T cell diversity within the ILT. Taking into account that the ILT can be regarded as a strategically located T cell reservoir and possibly an evolutionary forerunner of mammalian MALTs right at the border to the external environment, the alteration in transcription observed may likely represent a shift in the T cell population to optimize local gill defense mechanisms."],["dc.identifier.doi","10.4049/jimmunol.1400797"],["dc.identifier.eissn","1550-6606"],["dc.identifier.pmid","25172486"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/57644"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Transcriptional characterization of the T cell population within the salmonid interbranchial lymphoid tissue"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]