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152. The class I scavenger receptor CD163 promotes internalization of ADAMTS13 by macrophages

Author

Verbij, Fabian C, Sorvillo, Nicoletta, Kaijen, Paul H P, Hrdinova, Johana, Peyron, Ivan, Fijnheer, Rob, Ten Brinke, Anja, Meijer, Sander, van Alphen, Floris P.J., van den Berg, Timo K, Graversen, Jonas J H, Moestrup, Soren K, Voorberg, Jan, Verbij, Fabian C, Sorvillo, Nicoletta, Kaijen, Paul H P, Hrdinova, Johana, Peyron, Ivan, Fijnheer, Rob, Ten Brinke, Anja, Meijer, Sander, van Alphen, Floris P.J., van den Berg, Timo K, Graversen, Jonas J H, Moestrup, Soren K, and Voorberg, Jan

Abstract

Internalization of ADAMTS13 by macrophages may contribute to its clearance from the circulation. Here we investigated endocytic mechanisms that contribute to the uptake of ADAMTS13 by macrophages. Human monocyte-derived macrophages were used to monitor the uptake of fluorescently labeled recombinant ADAMTS13 by flow cytometry. Internalization of ADAMTS13 was blocked upon addition of the cell-permeable dynamin inhibitor dynasore. Partial blocking of ADAMTS13 uptake was observed by using mannan; however, uptake was not affected by an antibody that blocked binding to the macrophage mannose receptor CD206, which suggests that other endocytic receptors contribute to the internalization of ADAMTS13 by macrophages. A pull-down with ADAMTS13 and subsequent mass spectrometric analysis identified the class I scavenger receptor CD163 as a candidate receptor for ADAMTS13. Blocking experiments with monoclonal anti-CD163 antibody EDHu-1 resulted in decreased ADAMTS13 internalization by macrophages. Pronounced inhibition of ADAMTS13 uptake by EDHu-1 was observed in CD163 high-expressing macrophages. In agreement with these findings, CD163-expressing Chinese hamster ovary cells were capable of rapidly internalizing ADAMTS13. Surface plasmon resonance revealed binding of ADAMTS13 to scavenger receptor cysteine-rich domains 1-9 and 1-5 of CD163. Taken together, our data identify CD163 as a major endocytic receptor for ADAMTS13 on macrophages.

Published
2017

153. Analysis of the HLA-DR peptidome from human dendritic cells reveals high affinity repertoires and nonconventional pathways of peptide generation

Author

Ciudad, M Teresa, Sorvillo, Nicoletta, van Alphen, Floris P.J., Catalán, Diego, Meijer, Sander, Voorberg, Jan, Jaraquemada, Dolores, Ciudad, M Teresa, Sorvillo, Nicoletta, van Alphen, Floris P.J., Catalán, Diego, Meijer, Sander, Voorberg, Jan, and Jaraquemada, Dolores

Abstract

Dendritic cells (DCs) are the major professional APCs of the immune system; however, their MHC-II-associated peptide repertoires have been hard to analyze, mostly because of their scarce presence in blood and tissues. In vitro matured human monocyte-derived DCs (MoDCs) are widely used as professional APCs in experimental systems. In this work, we have applied mass spectrometry to identify the HLA-DR-associated self-peptide repertoires from small numbers of mature MoDCs (∼5 × 106cells), derived from 7 different donors. Repertoires of 9 different HLA-DR alleles were defined from analysis of 1319 peptides, showing the expected characteristics of MHC-II-associated peptides. Most peptides identified were predicted high binders for their respective allele, formed nested sets, and belonged to endo-lysosomal pathway-degraded proteins. Approximately 20% of the peptides were derived from cytosolic and nuclear proteins, a recurrent finding in HLA-DR peptide repertoires. Of interest, most of these peptides corresponded to single sequences, did not form nested sets, and were located at the C terminus of the parental protein, which suggested alternative processing. Analysis of cleavage patterns for terminal peptides predominantly showed aspartic acid before the cleavage site of both C- and N-terminal peptides and proline immediately after the cleavage site in C-terminal peptides. Proline was also frequent next to the cut sites of internal peptides. These data provide new insights into the Ag processing capabilities of DCs. The relevance of these processing pathways and their contribution to response to infection, tolerance induction, or autoimmunity deserve further analysis.

Published
2017

154. Factor VIII/V C-domain swaps reveal discrete C-domain roles in factor VIII function and intracellular trafficking

Author

Ebberink, Eduard H T M, Bouwens, Eveline A M, Bloem, Esther, Boon-Spijker, Mariëtte, Van den Biggelaar, Maartje, Voorberg, Jan, Meijer, Sander, Mertens, Koen, Ebberink, Eduard H T M, Bouwens, Eveline A M, Bloem, Esther, Boon-Spijker, Mariëtte, Van den Biggelaar, Maartje, Voorberg, Jan, Meijer, Sander, and Mertens, Koen

Abstract

Factor VIII C-domains are believed to contain specific function in co-factor activity and in interaction with von Willebrand factor. We have previously shown that factor VIII is co-targeted with von Willebrand factor to the Weibel-Palade bodies in blood outgrowth endothelial cells, even when factor VIII carries mutations in the light chain that are associated with defective von Willebrand factor binding. In this study we furthermore addressed the contribution of individual factor VIII C-domains in intracellular targeting, von Willebrand factor binding and co-factor activity by factor VIII/V C-domain swapping. Blood outgrowth endothelial cells were transduced with lentivirus encoding factor V, VIII and YFP-tagged C-domain chimeras, and examined by confocal microscopy. The same chimeras were produced in HEK293-cells for in vitro characterization and chemical foot-printing by mass spectrometry. In contrast to factor VIII, V did not target to Weibel-Palade bodies. The chimeras showed reduced Weibel-Palade body targeting, suggesting that this requires the factor VIII C1-C2 region. The factor VIII/V-C1 chimera did not bind von Willebrand Factor and had reduced affinity for factor IXa whereas the factor VIII/V-C2 chimera showed a small reduction in von Willebrand factor binding and normal interaction with factor IXa. This suggests that mainly the C1-domain carries factor VIII-specific features in assembly with von Willebrand Factor and factor IXa. Foot-printing analysis of the chimeras revealed increased exposure of lysine residues in the A1/C2- and C1/C2-domain interface, suggesting increased C2-domain mobility, which disrupts the natural C-domain tandem pair orientation. This affects intracellular trafficking more than extracellular function.

Published
2017

155. The class I scavenger receptor CD163 promotes internalization of ADAMTS13 by macrophages

Author

Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Verbij, Fabian C, Sorvillo, Nicoletta, Kaijen, Paul H P, Hrdinova, Johana, Peyron, Ivan, Fijnheer, Rob, Ten Brinke, Anja, Meijer, Sander, van Alphen, Floris P.J., van den Berg, Timo K, Graversen, Jonas J H, Moestrup, Soren K, Voorberg, Jan, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Verbij, Fabian C, Sorvillo, Nicoletta, Kaijen, Paul H P, Hrdinova, Johana, Peyron, Ivan, Fijnheer, Rob, Ten Brinke, Anja, Meijer, Sander, van Alphen, Floris P.J., van den Berg, Timo K, Graversen, Jonas J H, Moestrup, Soren K, and Voorberg, Jan

Published
2017

156. Factor VIII/V C-domain swaps reveal discrete C-domain roles in factor VIII function and intracellular trafficking

Author

Pharmaceutics, Afd Biomol.Mass Spect. and Proteomics, Afd Pharmaceutics, Biomolecular Mass Spectrometry and Proteomics, Ebberink, Eduard H T M, Bouwens, Eveline A M, Bloem, Esther, Boon-Spijker, Mariëtte, Van den Biggelaar, Maartje, Voorberg, Jan, Meijer, Sander, Mertens, Koen, Pharmaceutics, Afd Biomol.Mass Spect. and Proteomics, Afd Pharmaceutics, Biomolecular Mass Spectrometry and Proteomics, Ebberink, Eduard H T M, Bouwens, Eveline A M, Bloem, Esther, Boon-Spijker, Mariëtte, Van den Biggelaar, Maartje, Voorberg, Jan, Meijer, Sander, and Mertens, Koen

Published
2017

157. Monitoring storage induced changes in the platelet proteome employing label free quantitative mass spectrometry

Author

Biomolecular Mass Spectrometry and Proteomics, Rijkers, Maaike, van den Eshof, Bart L, van der Meer, Pieter F, van Alphen, Floris P.J., de Korte, Dirk, Leebeek, Frank W G, Meijer, Alexander B, Voorberg, Jan, Jansen, A J Gerard, Biomolecular Mass Spectrometry and Proteomics, Rijkers, Maaike, van den Eshof, Bart L, van der Meer, Pieter F, van Alphen, Floris P.J., de Korte, Dirk, Leebeek, Frank W G, Meijer, Alexander B, Voorberg, Jan, and Jansen, A J Gerard

Published
2017

158. Analysis of the HLA-DR peptidome from human dendritic cells reveals high affinity repertoires and nonconventional pathways of peptide generation

Author

Biomolecular Mass Spectrometry and Proteomics, Afd Biomol.Mass Spect. and Proteomics, Ciudad, M Teresa, Sorvillo, Nicoletta, van Alphen, Floris P.J., Catalán, Diego, Meijer, Sander, Voorberg, Jan, Jaraquemada, Dolores, Biomolecular Mass Spectrometry and Proteomics, Afd Biomol.Mass Spect. and Proteomics, Ciudad, M Teresa, Sorvillo, Nicoletta, van Alphen, Floris P.J., Catalán, Diego, Meijer, Sander, Voorberg, Jan, and Jaraquemada, Dolores

Published
2017

159. Sorting out the Weibel-Palade body

Author

Bierings, Ruben, Voorberg, Jan J., Mertens, Koen, van Mourik, Jan A., Voorberg, Jan J., Experimental Vascular Medicine, Landsteiner Laboratory, ACS - Microcirculation, and AII - Inflammatory diseases

Published
2007

160. Immune tolerance induction in hemophilia A

Author

van Helden, P.M.W., Voorberg, Jan J., Mertens, Koen, van den Berg, H. Marijke, Voorberg, Jan J., Experimental Vascular Medicine, Landsteiner Laboratory, ACS - Microcirculation, and AII - Inflammatory diseases

Published
2007

165. The Macrophage-Specific CD163 Is an Endocytic Receptor for Von Willebrand Factor (VWF) Cleaving Protease ADAMTS13

Author

Verbij, Fabian, primary, Sorvillo, Nicoletta, additional, Kaijen, Paul, additional, Hrdinova, Johana, additional, Fijnheer, Rob, additional, ten Brinke, Anja, additional, Meijer, Alexander B., additional, van Alphen, Floris P., additional, van der Berg, Timo K., additional, Graversen, Jonas H., additional, Moestrup, Soren K., additional, and Voorberg, Jan, additional

Published
2016
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168. Factor VIII inhibitors in mild hemophilia A

Author

Bril, Wendy S., Voorberg, Jan J., Mertens, Koen, van Lier, Rene A. W., Voorberg, Jan J., Experimental Vascular Medicine, Landsteiner Laboratory, ACS - Microcirculation, and AII - Inflammatory diseases

Published
2003

169. The severe von Willebrand Disease variant p.M771V leads to impaired anterograde trafficking of Von Willebrand factor in patient-derived and base-edited ECFCs

Author

Bär, Isabel, Barraclough, Alastair, Bürgisser, Petra E., van Kwawegen, Calvin, Fijnvandraat, Karin, Eikenboom, Jeroen C.J., Leebeek, Frank W.G., Voorberg, Jan, and Bierings, Ruben

Abstract

Von Willebrand disease (VWD) is the most common inherited bleeding disorder caused by quantitative or qualitative defects of VWF. The p.M771V VWF variant leads to a severe bleeding phenotype in homozygous patients. However, the exact molecular mechanism remains unclear, which prevents personalized treatment of those VWD patients.

Published
2024
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170. Molecular analysis of Factor VIII inhibitors using phage display

Author

van den Brink, Edward N., Voorberg, Jan J., Aalberse, Rob C., van Aken, W. G., Peters, Marjolein, Voorberg, Jan J., Experimental Vascular Medicine, Landsteiner Laboratory, ACS - Microcirculation, and AII - Inflammatory diseases

Published
2000

174. Sorting out the Weibel-Palade body

Author

Voorberg, Jan J., Experimental Vascular Medicine, Landsteiner Laboratory, ACS - Microcirculation, and AII - Inflammatory diseases

Published
2007

180. STXBP1 promotes Weibel-Palade body exocytosis through its interaction with the Rab27A effector Slp4-a

Author

van Breevoort, Dorothee, primary, Snijders, Ambrosius P., additional, Hellen, Nicola, additional, Weckhuysen, Sarah, additional, van Hooren, Kathinka W. E. M., additional, Eikenboom, Jeroen, additional, Valentijn, Karine, additional, Fernandez-Borja, Mar, additional, Ceulemans, Berten, additional, De Jonghe, Peter, additional, Voorberg, Jan, additional, Hannah, Matthew, additional, Carter, Tom, additional, and Bierings, Ruben, additional

Published
2014
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183. FVIII inhibitors in mild hemophilia A

Author

Voorberg, Jan J., Mertens, Koen, van Lier, Rene A. W., Experimental Vascular Medicine, Landsteiner Laboratory, ACS - Microcirculation, and AII - Inflammatory diseases

Published
2003

184. Weibel-Palade Body Localized Syntaxin-3 Modulates Von Willebrand Factor Secretion From Endothelial Cells

Author

Schillemans, Maaike, Karampini, Ellie, van den Eshof, Bart L., Gangaev, Anastasia, Hofman, Menno, van Breevoort, Dorothee, Meems, Henriët, Janssen, Hans, Mulder, Aat A., Jost, Carolina R., Escher, Johanna C., Adam, Rüdiger, Carter, Tom, Koster, Abraham J., van den Biggelaar, Maartje, Voorberg, Jan, and Bierings, Ruben

Abstract

Supplemental Digital Content is available in the text.

Published
2018
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185. Factor VIII inhibitor in a patient with mild haemophilia A and an Asn618-->Ser mutation responsive to immune tolerance induction and cyclophosphamide

Author

Vlot, André J., Wittebol, Shulamiet, Strengers, Paul F. W., Turenhout, Ellen A. M., Voorberg, Jan, van den Berg, H. Marijke, Mauser-Bunschoten, Eveline P., and Landsteiner Laboratory

Subjects
hemic and lymphatic diseases
Abstract

We describe a patient with mild haemophilia A (original value of factor VIII activity 0.30 U/ml) who developed an inhibitor (36.1 Bethesda U/ml) which cross-reacted with his endogenous factor VIII. This caused a decline in basal factor VIII level ( Ser in the A2 domain of factor VIII. Immunoprecipitation analysis showed that the antibodies present in the patient's plasma reacted with metabolically labelled A2 domain and, to a lesser extent, with factor VIII light chain. Inhibitory antibodies were completely neutralized by recombinant A2 domain, whereas no neutralization was observed after the addition of factor VIII light chain (A3-C1-C2) and C2 domain. More detailed analysis showed that the majority of inhibitory antibodies were directed against residues Arg484-Ile508, a previously identified binding site for factor VIII inhibitors. Our findings suggest that immune tolerance therapy and cyclophosphamide were successful in eradicating inhibitory antibodies against a common epitope on factor VIII

Published
2002

186. Analysis of factor VIII inhibitors in a haemophilia A patient with an Arg(593)-> Cys mutation using phage display

Author

Bril, Wendy S., Turenhout, Ellen A. M., Kaijen, Paul H. P., van den Brink, Edward N., Koopman, Maria M. W., Peters, Marjolein, Voorberg, Jan, Paediatric Infectious Diseases / Rheumatology / Immunology, and Landsteiner Laboratory

Abstract

We characterized anti-factor VIII antibodies in a mild haemophilia A patient with an Arg(593)-->Cys mutation in the A2 domain, using V gene phage-display technology. All isolated single-chain variable-domain antibody fragments were directed against residues Arg(484)-Ile(508), a binding site for factor VIII inhibitors in the A2 domain. After a further period of replacement therapy, a transient rise in inhibitor titre was observed. These antibodies were directed against the A2 domain. Activation of a pre-existing pool of B cells, which express antibodies against residues Arg(484)-Ile(508), could explain the rapid anamnestic response

Published
2002

194. Analysis of the storage and secretion of von Willebrand factor in blood outgrowth endothelial cells derived from patients with von Willebrand disease

Author

Wang, Jiong-Wei, primary, Bouwens, Eveline A. M., additional, Pintao, Maria Carolina, additional, Voorberg, Jan, additional, Safdar, Huma, additional, Valentijn, Karine M., additional, de Boer, Hetty C., additional, Mertens, Koen, additional, Reitsma, Pieter H., additional, and Eikenboom, Jeroen, additional

Published
2013
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