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17 results on '"Goebeler, Verena"'

6. Development of Novel Monoamine Oxidase-B (MAO-B) Inhibitors with Reduced Blood–Brain Barrier Permeability for the Potential Management of Noncentral Nervous System (CNS) Diseases

Author

Gealageas, Ronan, primary, Devineau, Alice, additional, So, Pauline P. L., additional, Kim, Catrina M. J., additional, Surendradoss, Jayakumar, additional, Buchwalder, Christian, additional, Heller, Markus, additional, Goebeler, Verena, additional, Dullaghan, Edith M., additional, Grierson, David S., additional, and Putnins, Edward E., additional

Published
2018
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7. Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14

Author

Eckhard, Ulrich, primary, Huesgen, Pitter F., additional, Schilling, Oliver, additional, Bellac, Caroline L., additional, Butler, Georgina S., additional, Cox, Jennifer H., additional, Dufour, Antoine, additional, Goebeler, Verena, additional, Kappelhoff, Reinhild, additional, auf dem Keller, Ulrich, additional, Klein, Theo, additional, Lange, Philipp F., additional, Marino, Giada, additional, Morrison, Charlotte J., additional, Prudova, Anna, additional, Rodriguez, David, additional, Starr, Amanda E., additional, Wang, Yili, additional, and Overall, Christopher M., additional

Published
2016
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8. Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses

Author

Eckhard, Ulrich, primary, Huesgen, Pitter F., additional, Schilling, Oliver, additional, Bellac, Caroline L., additional, Butler, Georgina S., additional, Cox, Jennifer H., additional, Dufour, Antoine, additional, Goebeler, Verena, additional, Kappelhoff, Reinhild, additional, Keller, Ulrich auf dem, additional, Klein, Theo, additional, Lange, Philipp F., additional, Marino, Giada, additional, Morrison, Charlotte J., additional, Prudova, Anna, additional, Rodriguez, David, additional, Starr, Amanda E., additional, Wang, Yili, additional, and Overall, Christopher M., additional

Published
2016
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9. Macrophage Matrix Metalloproteinase-12 Dampens Inflammation and Neutrophil Influx in Arthritis

Author

Bellac, Caroline L., primary, Dufour, Antoine, additional, Krisinger, Michael J., additional, Loonchanta, Anantasak, additional, Starr, Amanda E., additional, auf dem Keller, Ulrich, additional, Lange, Philipp F., additional, Goebeler, Verena, additional, Kappelhoff, Reinhild, additional, Butler, Georgina S., additional, Burtnick, Leslie D., additional, Conway, Edward M., additional, Roberts, Clive R., additional, and Overall, Christopher M., additional

Published
2014
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16. Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca2+ and lipid binding proteins

Author

Goebeler, Verena, Ruhe, Daniela, Gerke, Volker, and Rescher, Ursula

Subjects
*BIOLOGICAL membranes, *ANNEXINS
Abstract

Annexin A9 is a novel member of the annexin family of Ca2+ and phospholipid binding proteins which has so far only been identified in EST data bases and whose deduced protein sequence shows mutations in residues considered crucial for Ca2+ coordination in other annexins. To elucidate whether the annexin A9 protein is expressed as such and to characterize its biochemical properties we probed cell extracts with specific anti-annexin A9 antibodies and developed a recombinant expression system. We show that the protein is found in HepG2 hepatoma cell lysates and that a green fluorescent protein-tagged form is abundantly expressed in the cytosol of HeLa cells. Recombinant expression in bacteria yields a soluble protein that can be enriched by conventional chromatographic procedures. The protein is capable of binding phosphatidylserine containing liposomes albeit only at Ca2+ concentrations exceeding 2 mM. Moreover and in contrast to other annexins this binding appears to be irreversible as the liposome-bound annexin A9 cannot be released by Ca2+ chelation. These results indicate that annexin A9 is a unique member of the annexin family whose intracellular activity is not subject to Ca2+ regulation. [Copyright &y& Elsevier]

Published
2003
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17. Macrophage matrix metalloproteinase-12 dampens inflammation and neutrophil influx in arthritis

Author

Bellac, Caroline L., Dufour, Antoine, Krisinger, Michael J., Loonchanta, Anantasak, Starr, Amanda E., auf dem Keller, Ulrich, Lange, Philipp F., Goebeler, Verena, Kappelhoff, Reinhild, Butler, Georgina S., Burtnick, Leslie D., Conway, Edward M., Roberts, Clive R., and Overall, Christopher M.

Subjects
3. Good health
Abstract

Resolution of inflammation reduces pathological tissue destruction and restores tissue homeostasis. Here, we used a proteomic protease substrate discovery approach, terminal amine isotopic labeling of substrates (TAILS), to analyze the role of the macrophage-specific matrix metalloproteinase-12 (MMP12) in inflammation. In murine peritonitis, MMP12 inactivates antithrombin and activates prothrombin, prolonging the activated partial thromboplastin time. Furthermore, MMP12 inactivates complement C3 to reduce complement activation and inactivates the chemoattractant anaphylatoxins C3a and C5a, whereas iC3b and C3b opsonin cleavage increases phagocytosis. Loss of these anti-inflammatory activities in collagen-induced arthritis in Mmp12−/− mice leads to unresolved synovitis and extensive articular inflammation. Deep articular cartilage loss is associated with massive neutrophil infiltration and abnormal DNA neutrophil extracellular traps (NETs). The NETs are rich in fibrin and extracellular actin, which TAILS identified as MMP12 substrates. Thus, macrophage MMP12 in arthritis has multiple protective roles in countering neutrophil infiltration, clearing NETs, and dampening inflammatory pathways to prepare for the resolution of inflammation., Cell Reports, 9 (2), ISSN:2666-3864, ISSN:2211-1247

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