Oppermann, Martin

[["dc.bibliographiccitation.journal","Naunyn-Schmiedeberg s Archives of Pharmacology"],["dc.bibliographiccitation.volume","365"],["dc.contributor.author","Pollok-Kopp, B."],["dc.contributor.author","Kraft, K."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:31:35Z"],["dc.date.available","2018-11-07T10:31:35Z"],["dc.date.issued","2002"],["dc.format.extent","R18"],["dc.identifier.isi","000175030900068"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44148"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.issn","0028-1298"],["dc.title","Kinetic analysis of PKC- and GRK-mediated phosphorylation of chemokine receptor CCR5 by phosphosite-specific antibodies"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Molecular Immunology"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Pollok-Kopp, B."],["dc.contributor.author","Rethorn, S."],["dc.contributor.author","Schwarze, Katrin"],["dc.contributor.author","Huttenrauch, F."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:38:44Z"],["dc.date.available","2018-11-07T10:38:44Z"],["dc.date.issued","2006"],["dc.format.extent","149"],["dc.identifier.isi","000232021600087"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45879"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.publisher.place","Oxford"],["dc.relation.conference","10th Meeting on Complement in Human Disease"],["dc.relation.eventlocation","Heidelberg, GERMANY"],["dc.relation.issn","0161-5890"],["dc.title","Protein kinase C beta-mediated phosphorylation of Serine-334 of the human C5a anaphylatoxin receptor (C5aR): Modulation by the adapter protein beta-arrestin"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","37503"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","37515"],["dc.bibliographiccitation.volume","280"],["dc.contributor.author","Huttenrach, F."],["dc.contributor.author","Pollok-Kopp, B."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:54:21Z"],["dc.date.available","2018-11-07T10:54:21Z"],["dc.date.issued","2005"],["dc.description.abstract","Expression levels of the chemokine receptor, CC chemokine receptor 5 (CCR5), at the cell surface determine cell susceptibility to HIV entry and infection. Cellular activation by CCR5 itself, but also by unrelated receptors leads to cross-phosphorylation and cross-internalization of CCR5. This study addresses the underlying molecular mechanisms of homologous and heterologous CCR5 regulation. As shown by bioluminescence resonance energy transfer experiments, CCR5 formed constitutive homo- as well as heterooligomeric complexes together with C5aR but not with the unrelated AT(1a)R in living cells. Stimulation with CCL5 of RBL cells, which co-expressed CCR5 together with an N-terminally truncated CCR5-Delta NT mutant, resulted in both protein kinase C(PKC)- and G protein-coupled receptor (GPCR) kinase (GRK)-mediated cross-phosphorylation of the mutant unligated receptor, as determined by phosphosite-specific monoclonal antibody. Similarly, both PKC and GRK cross-phosphorylated CCR5 in a heterologous manner after C5a stimulation of RBL-CCR5/ C5aR cells, whereas AT(1a)R stimulation resulted only in classical PKC-mediated CCR5 phosphorylation. Co-expression of CCR5-Delta NT together with a phosphorylation-deficient CCR5 mutant that neither binds beta-arrestin nor undergoes internalization partially restored the CCL5-induced association of beta-arrestin with the homo- oligomeric receptor complex and augmented cellular uptake of I-125-CCL5. Co-expression of C5aR, but not of AT1aR, promoted CCR5 co-internalization upon agonist stimulation by a mechanism independent of CCR5 phosphorylation. Co-internalization of phosphorylated CCR5 was also observed in C5a-stimulated macrophages. Finally, co-expression of a constitutively internalized C5aR-US28(CT) mutant led to intracellular accumulation of CCR5 in the absence of ligand stimulation. These results show that GRKs and beta-arrestin are involved in heterologous receptor regulation by cross-phosphorylating and co-internalizing unligated receptors within homo- or hetero-oligomeric protein complexes."],["dc.identifier.doi","10.1074/jbc.M500535200"],["dc.identifier.isi","000233044500027"],["dc.identifier.pmid","16144840"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49545"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","G protein-coupled receptor kinases promote phosphorylation and beta-arrestin-mediated internalization of CCR5 homo- and hetero-oligomers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The FASEB Journal"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Oppermann, Martin"],["dc.contributor.author","Herfarth, H."],["dc.contributor.author","Goke, M."],["dc.contributor.author","Press, A."],["dc.contributor.author","Pollok-Kopp, B."],["dc.date.accessioned","2018-11-07T09:17:14Z"],["dc.date.available","2018-11-07T09:17:14Z"],["dc.date.issued","2001"],["dc.format.extent","A358"],["dc.identifier.isi","000167438102047"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28115"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Federation Amer Soc Exp Biol"],["dc.publisher.place","Bethesda"],["dc.relation.issn","0892-6638"],["dc.title","Polymorphism of CC chemokine receptors CCR5 and CCR2 in Crohn's disease"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","113"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Immunology Letters"],["dc.bibliographiccitation.lastpage","117"],["dc.bibliographiccitation.volume","77"],["dc.contributor.author","Herfarth, H."],["dc.contributor.author","Pollok-Kopp, B."],["dc.contributor.author","Goke, M."],["dc.contributor.author","Press, A."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T09:00:31Z"],["dc.date.available","2018-11-07T09:00:31Z"],["dc.date.issued","2001"],["dc.description.abstract","Crohn's disease (CD) is a chronic inflammatory disease of the intestine that is characterized by mononuclear cell infiltration and a predominant Th1 lymphocyte response. We tested the hypothesis that CC chemokine receptors CCR2 and CCR5 might be important in the regulation of the intestinal immune response in this disease, and we speculated that carriers of a defective 32 base pair deletion mutant of CCR5, CCR5 Delta 32, which results in a non-functional receptor, might be protected from CD. Using polymerase chain reaction (PCR) and PCR restriction fragment length polymorphism (PCR-RFLP) gene frequencies of CCR5 Delta 32 and of CCR2-641 (replacement of valine-64 by isoleucine in the CCR2 gene) in healthy controls (n = 346) and in CD patients (n = 235) were determined. In CD patients, subgroup phenotypic analyses were performed according to the Vienna classification. The overall gene frequency of CCR5 Delta 32 (9.8%) and CCR2-641 (7.6%) in CD patients did not deviate significantly from healthy controls (9.2 and 8.2%, respectively), nor did we observe a significant deviation from the predicted Hardy-Weinberg distribution. No significant differences in the CD phenotype classification for the different CCR5 and CCR2 alleles were observed, except for a trend to disease sparing of the upper gastrointestinal tract (carrier frequency 0 versus 19.6%, Delta = 1 9.6%, P = 0.079) as well as a more stricturing disease behaviour (23.5 versus 16.2%, Delta = 7.3%, P = 0.136) in carriers of the mutant CCR5 Delta 32 allele. These results indicate that the different CCR5 but not CCR2 alleles may influence disease behaviour and thereby contribute to the observed heterogeneity of CD. However, the associations observed are limited and await replication in other datasets. CCR2 and CCR5 polymorphisms are unlikely to be important determinants of overall disease susceptibility. (C) 2001 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0165-2478(01)00199-7"],["dc.identifier.isi","000169218100007"],["dc.identifier.pmid","11377705"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24183"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0165-2478"],["dc.title","Polymorphism of CC chemokine receptors CCR2 and CCR5 in Crohn's disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2190"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","2198"],["dc.bibliographiccitation.volume","278"],["dc.contributor.author","Pollok-Kopp, B."],["dc.contributor.author","Schwarze, Katrin"],["dc.contributor.author","Baradari, V. K."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:41:37Z"],["dc.date.available","2018-11-07T10:41:37Z"],["dc.date.issued","2003"],["dc.description.abstract","Human CC chemokine receptor 5 (CCR5), a member of the superfamily of G protein-coupled receptors, regulates the activation and directed migration of leukocytes and serves as the main coreceptor for the entry of R5 tropic strains of human immunodeficiency viruses. We have previously shown that RANTES/CCL5 binding to CCR5 induces GPCR kinase (GRK)- and protein kinase C (PKC)-mediated phosphorylation of four distinct C-terminal serine residues. To study these phosphorylation events in vivo, we have generated monoclonal antibodies, which specifically react only with either phosphorylated or nonphosphorylated CCR5. These phosphosite-specific antibodies reveal that following ligand stimulation of the receptor serine 337 is exclusively phosphorylated by a PKC-mediated mechanism, while GRKs phosphorylate serine 349. GRK-mediated receptor phosphorylation proceeds in a regular time-dependent manner (t(1/2),similar to2 min) with an apparent EC50 of 5 nm. In contrast, PKC phosphorylates serine 337 at 50-fold lower concentrations and in a very rapid, albeit transient manner. Protein phosphatases that are active at neutral pH and are inhibited by okadaic acid rapidly dephosphorylate phosphoserine 337, but less efficiently phosphoserine 349, in intact cells and in an in vitro assay. Immunofluorescence microscopy demonstrates that phosphorylated receptors accumulate in a perinuclear compartment, which resembles recycling endosomes. This study is the first to analyze in detail the spatial and temporal dynamics of GRK- versus PKC-mediated phosphorylation of a G protein-coupled receptor and its subsequent dephosphorylation on the level of individual phosphorylation sites."],["dc.identifier.doi","10.1074/jbc.M209844200"],["dc.identifier.isi","000180562000017"],["dc.identifier.pmid","12403770"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46583"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Analysis of ligand-stimulated CC chemokine receptor 5 (CCR5) phosphorylation in intact cells using phosphosite-specific antibodies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]