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27 results on '"Gritsch, Herbert"'

1. Treatment with recombinant ADAMTS13, alleviates hypoxia/reoxygenation-induced pathologies in a mouse model of human sickle cell disease

Author

Rossato, Paolo, primary, Glantschnig, Helmut, additional, Canneva, Fabio, additional, Schuster, Maria, additional, Coulibaly, Sogue, additional, Schrenk, Gerald, additional, Voelkel, Dirk, additional, Dockal, Michael, additional, Plaimauer, Barbara, additional, Rottensteiner, Hanspeter, additional, Gritsch, Herbert, additional, Federti, Enrica, additional, Matte, Alessandro, additional, De Franceschi, Lucia, additional, Scheiflinger, Friedrich, additional, and Hoellriegl, Werner, additional

Published
2023
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4. Structure and Function of Recombinant versus Plasma-Derived von Willebrand Factor and Impact on Multimer Pharmacokinetics in von Willebrand Disease

Author

Gritsch,Herbert, Schrenk,Gerald, Weinhappl,Nina, Mellgård,Björn, Ewenstein,Bruce, Turecek,Peter L, Gritsch,Herbert, Schrenk,Gerald, Weinhappl,Nina, Mellgård,Björn, Ewenstein,Bruce, and Turecek,Peter L

Abstract

Herbert Gritsch,1 Gerald Schrenk,1 Nina Weinhappl,1 Björn Mellgård,2 Bruce Ewenstein,2 Peter L Turecek3,4 1Pharmaceutical Sciences, Baxalta Innovations GmbH, a Takeda Company, Vienna, Austria; 2Rare Genetics and Hematology, Research & Development, Takeda Development Center Americas, Inc, Cambridge, MA, USA; 3Department of Pharmaceutical Sciences, Division of Pharmacology, University of Vienna, Vienna, Austria; 4Plasma Derived Therapies, Research & Development, Baxalta Innovations GmbH, a Takeda Company, Vienna, AustriaCorrespondence: Peter L Turecek, Baxalta Innovations GmbH, a Takeda company, DC-Tower, Donau-City-Straße 7, Vienna, A-1220, Austria, Tel +43 1 20 100 247 2520, Fax +43 1 20 100 247 5733, Email peter.turecek@takeda.comAbstract: Background: Recombinant von Willebrand factor (rVWF, vonicog alfa) is a purified VWF concentrate produced from Chinese hamster ovary cells. rVWF is not exposed to the VWF-cleaving protease ADAMTS13 and so is not subject to proteolytic degradation of large (L) and ultra-large (UL) VWF multimers by that enzyme.Purpose: To compare the structure and function of rVWF with the human plasma-derived VWF [pdVWF] concentrates Haemate P®/Humate-P®, Voncento®, Wilate®/Eqwilate®, and Wilfactin®/Willfact®; to investigate the relationship between VWF multimeric pattern and VWF:ristocetin cofactor (VWF:RCo) activity through population pharmacokinetic (PK) modeling in patients with severe von Willebrand disease (VWD) treated with rVWF.Methods: Analyses included VWF:RCo activity, VWF:collagen-binding activity, VWF:platelet glycoprotein Ib receptor binding, factor VIII (FVIII) binding capacity, and VWF-mediated platelet adhesion under flow conditions. VWF multimeric structure was determined by agarose gel electrophoresis. Population PK models describing the activity-time profile of small, medium, and L/UL multimers following intravenous administration of rVWF in patients with severe VWD were developed.Results: Findings demonstrate

Published
2022

5. Evidence of protective effects of recombinant ADAMTS13 in a humanized model of sickle cell disease

Author

Rossato, Paolo, primary, Federti, Enrica, additional, Matte, Alessandro, additional, Glantschnig, Helmut, additional, Canneva, Fabio, additional, Schuster, Maria, additional, Coulibaly, Sogue, additional, Schrenk, Gerald, additional, Voelkel, Dirk, additional, Dockal, Michael, additional, Plaimauer, Barbara, additional, Andolfo, Immacolata, additional, Iolascon, Achille, additional, Rottensteiner, Hanspeter, additional, Gritsch, Herbert, additional, Scheiflinger, Friedrich, additional, Hoellriegl, Werner, additional, and Franceschi, Lucia De, additional

Published
2022
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7. Evaluation of Factor VIII Polysialylation: Identification of a Longer-Acting Experimental Therapy in Mice and Monkeys

Author

Glantschnig, Helmut, primary, Bauer, Alexander, additional, Benamara, Karima, additional, Dockal, Michael, additional, Ehrlich, Veronika, additional, Gritsch, Herbert, additional, Höbarth, Gerald, additional, Horling, Frank M., additional, Kopic, Alexandra, additional, Leidenmühler, Peter, additional, Reipert, Birgit M., additional, Rottensteiner, Hanspeter, additional, Ruthsatz, Tanja, additional, Schrenk, Gerald, additional, Schuster, Maria, additional, Turecek, Peter L., additional, Weber, Alfred, additional, Wolfsegger, Martin, additional, Scheiflinger, Friedrich, additional, and Höllriegl, Werner, additional

Published
2019
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8. Nonclinical Safety of SHP 826 (BAX 826), a Next Generation Extended Half-Life Recombinant Factor VIII Product

Author

Ehrlich, Veronika, primary, Leidenmuehler, Peter, additional, Dietrich, Barbara, additional, Hoebarth, Gerald, additional, Ruthsatz, Tanja, additional, Turecek, Peter L., additional, Wolfsegger, Martin, additional, Weber, Alfred, additional, Gritsch, Herbert, additional, Hoellriegl, Werner, additional, and Turecek, Marietta, additional

Published
2016
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9. Pharmacokinetics of BAX 826, a Polysialylated Full-Length rFVIII, in Hemophilia a Mice, Rats, and Cynomolgus Monkeys

Author

Schiviz, Alexandra, primary, Hoebarth, Gerald, additional, Wolfsegger, Martin, additional, Rossato, Paolo, additional, Weber, Alfred, additional, Gritsch, Herbert, additional, Rottensteiner, Hanspeter, additional, Turecek, Peter L., additional, Scheiflinger, Friedrich, additional, Hoellriegl, Werner, additional, and Putz, Marietta, additional

Published
2015
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14. Pharmacokinetics of Baxter’s Longer Acting rFVIII (BAX 855) in Factor VIII Ko Mice, Rats and Cynomolgus Monkeys

Author

Hoebarth, Gerald, primary, Kubik, Susan, additional, Wolfsegger, Martin, additional, Lawo, John-Philip, additional, Weber, Alfred, additional, Gritsch, Herbert, additional, Hoellriegl, Werner, additional, Schiviz, Alexandra, additional, Ehrlich, Hartmut J., additional, Scheiflinger, Friedrich, additional, Turecek, Peter L, additional, Schwarz, Hans Peter, additional, and Muchitsch, Eva-Maria, additional

Published
2011
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22. Biochemical and Functional Characterization of PEGylated rVWF.

Author

Turecek, Peter L., primary, Scheiflinger, Friedrich, primary, Siekmann, Juergen, primary, Váradi, Katalin, primary, Matthiessen, H. Peter, primary, Weber, Alfred, primary, Gritsch, Herbert, primary, Muchitsch, Eva-Maria, primary, Baumgartner, Bernhard, primary, and Schwarz, Hans Peter, primary

Published
2006
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25. In Vivo Characterization of Recombinant von Willebrand Factor in Dogs With von Willebrand Disease

Author

Turecek, Peter L., primary, Gritsch, Herbert, additional, Pichler, Ludwig, additional, Auer, Wilfried, additional, Fischer, Bernhard, additional, Mitterer, Artur, additional, Mundt, Wolfgang, additional, Schlokat, Uwe, additional, Dorner, Friedrich, additional, Brinkman, Herm Jan M., additional, van Mourik, Jan A., additional, and Schwarz, Hans Peter, additional

Published
1997
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27. An Automated pre-Dilution Setup for Von Willebrand Factor Activity Assays.

Author

Schachinger T, Holik AK, Schrenk G, Gritsch H, Hofbauer S, Furtmüller PG, and Turecek PL

Abstract

Accurate quantification of von Willebrand factor ristocetin cofactor activity (VWF:RCo) is critical for the diagnosis and classification of von Willebrand disease, the most common hereditary and acquired bleeding disorder in humans. Moreover, it is important to accurately assess the function of von Willebrand factor (VWF) concentrates within the pharmaceutical industry to provide consistent and high-quality biopharmaceuticals. Although the performance of VWF:RCo assay has been improved by using coagulation analyzers, which are specialized devices for blood and blood plasma samples, scientists still report a high degree of intra- and inter-assay variation in clinical laboratories. Moreover, high, manual sample dilutions are required for VWF:RCo determination of VWF concentrates within the pharmaceutical industry, which are a major source for assay imprecision. For the first time, we present a precise and accurate method to determine VWF:RCo, where all critical pipetting and mixing steps are automated. A pre-dilution setup was established on CyBio FeliX (Analytik-Jena) liquid handling system, and an adapted VWF:RCo method on BCS-XP analyzer (Siemens) is used. The automated pre-dilution method was executed on three different, most frequently used coagulation analyzers and compared to manual pre-dilutions performed by an experienced operator. Comparative sample testing revealed a similar assay precision (coefficient of variation = 5.9% automated, 3.1% manual pre-dilution) and no significant differences between the automated approach and manual dilutions of an expert in this method. While no outliers were generated with the automated procedure, the manual pre-dilution resulted in an error rate of 8.3%. Overall, this operator-independent protocol enables standardization and offers an efficient way of fully automating VWF activity assays, while maintaining the precision and accuracy of an expert analyst. Key features • Automated pre-dilution setup for von Willebrand factor concentrates of various natures. • Combination of a liquid handling system (CyBio FeliX) with a coagulation analyzer (BCS-XP). • Simplifies method transfer to other laboratories. • Basic training for CyBio FeliX and BCS-XP is required. Graphical overview VWF:RCo assay principle and measurement setup. Platelets (yellow ellipsoids) with negative surface charge (- - -) are treated with formaldehyde, which partly denatures the cell surface and thus stabilizes platelets for use as assay reagents. Stabilized platelets (dark-yellow-framed yellow ellipsoids) are then brought in contact with ristocetin A (chemical structure shown; black dots), which binds to the platelet surface and facilitates binding of VWF (green circles). The graphs show an example of quantitative determination of platelet agglutination by measurement of light transmission, where increasing amounts of VWF increase light transmission over time. The photo in the left-bottom corner shows the CyBio FeliX setup for VWF sample dilution and the photo in the right-bottom corner displays the BCS-XP system, which is used for VWF:RCo measurements., Competing Interests: Competing interestsBaxalta Innovations GmbH (part of Takeda) provided funding for this research. Authors Tobias Schachinger, Ann-Katrin Holik, Gerald Schrenk, Herbert Gritsch, and Peter L. Turecek are employed at Baxalta Innovations GmbH, part of Takeda. Gerald Schrenk, Herbert Gritsch, and Peter L. Turecek hold stocks of Takeda. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (©Copyright : © 2024 The Authors; This is an open access article under the CC BY-NC license.)

Published
2024
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