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


Journal

Journal of thrombosis and haemostasis : JTH
ISSN: 1538-7836
Titre abrégé: J Thromb Haemost
Pays: England
ID NLM: 101170508

Informations de publication

Date de publication:
02 2023
Historique:
received: 10 05 2022
revised: 30 09 2022
accepted: 25 10 2022
pubmed: 27 1 2023
medline: 15 2 2023
entrez: 26 1 2023
Statut: ppublish

Résumé

Sickle cell disease (SCD) is an inherited red blood cell disorder with a causative substitution in the beta-globin gene that encodes beta-globin in hemoglobin. Furthermore, the ensuing vasculopathy in the microvasculature involves heightened endothelial cell adhesion, inflammation, and coagulopathy, all of which contribute to vaso-occlusive crisis (VOC) and the sequelae of SCD. In particular, dysregulation of the von Willebrand factor (VWF) and a disintegrin and metalloproteinase with thrombospondin type 1 motif, member 13 (ADAMTS13) axis has been implicated in human SCD pathology. To investigate the beneficial potential of treatment with recombinant ADAMTS13 (rADAMTS13) to alleviate VOC. Pharmacologic treatment with rADAMTS13 in vitro or in vivo was performed in a humanized mouse model of SCD that was exposed to hypoxia/reoxygenation stress as a model of VOC. Then, pharmacokinetic, pharmacodynamic, and behavioral analyses were performed. Administration of rADAMTS13 to SCD mice dose-dependently increased plasma ADAMTS13 activity, reduced VWF activity/antigen ratios, and reduced baseline hemolysis (free hemoglobin and total bilirubin) within 24 hours. rADAMTS13 was administered in SCD mice, followed by hypoxia/reoxygenation stress, and reduced VWF activity/antigen ratios in parallel to significantly (p < .01) improved recovery during the reoxygenation phase. Consistent with the results in SCD mice, we demonstrate in a human in vitro system that treatment with rADAMTS13 counteracts the inhibitory activity of hemoglobin on the VWF/ADAMTS13-axis. Collectively, our data provide evidence that relative ADAMTS13 insufficiency in SCD mice is corrected by pharmacologic treatment with rADAMTS13 and provides an effective disease-modifying approach in a human SCD mouse model.

Sections du résumé

BACKGROUND
Sickle cell disease (SCD) is an inherited red blood cell disorder with a causative substitution in the beta-globin gene that encodes beta-globin in hemoglobin. Furthermore, the ensuing vasculopathy in the microvasculature involves heightened endothelial cell adhesion, inflammation, and coagulopathy, all of which contribute to vaso-occlusive crisis (VOC) and the sequelae of SCD. In particular, dysregulation of the von Willebrand factor (VWF) and a disintegrin and metalloproteinase with thrombospondin type 1 motif, member 13 (ADAMTS13) axis has been implicated in human SCD pathology.
OBJECTIVES
To investigate the beneficial potential of treatment with recombinant ADAMTS13 (rADAMTS13) to alleviate VOC.
METHODS
Pharmacologic treatment with rADAMTS13 in vitro or in vivo was performed in a humanized mouse model of SCD that was exposed to hypoxia/reoxygenation stress as a model of VOC. Then, pharmacokinetic, pharmacodynamic, and behavioral analyses were performed.
RESULTS
Administration of rADAMTS13 to SCD mice dose-dependently increased plasma ADAMTS13 activity, reduced VWF activity/antigen ratios, and reduced baseline hemolysis (free hemoglobin and total bilirubin) within 24 hours. rADAMTS13 was administered in SCD mice, followed by hypoxia/reoxygenation stress, and reduced VWF activity/antigen ratios in parallel to significantly (p < .01) improved recovery during the reoxygenation phase. Consistent with the results in SCD mice, we demonstrate in a human in vitro system that treatment with rADAMTS13 counteracts the inhibitory activity of hemoglobin on the VWF/ADAMTS13-axis.
CONCLUSION
Collectively, our data provide evidence that relative ADAMTS13 insufficiency in SCD mice is corrected by pharmacologic treatment with rADAMTS13 and provides an effective disease-modifying approach in a human SCD mouse model.

Identifiants

pubmed: 36700507
pii: S1538-7836(22)07185-9
doi: 10.1016/j.jtha.2022.10.016
pii:
doi:

Substances chimiques

von Willebrand Factor 0
Volatile Organic Compounds 0
ADAMTS13 Protein EC 3.4.24.87
ADAMTS13 protein, human EC 3.4.24.87
ADAMTS13 protein, mouse EC 3.4.24.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

269-275

Informations de copyright

Copyright © 2022 International Society on Thrombosis and Haemostasis. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest S.C., G.S., and H. Gritsch are employees of Baxalta Innovations GmbH, a member of the Takeda group of companies, and are Takeda stock owners. P.R., H. Glantschnig, F.C., M.S., D.V., M.D., B.P., H.R., F.S., and W.H. were employees of Baxalta Innovations GmbH, a member of the Takeda group of companies, at the time of the study. L.D.F. has received grant/research support from Baxalta Innovations GmbH, a Takeda company; Roche; and Agios. E.F. and A.M. have no competing interests to declare.

Auteurs

Paolo Rossato (P)

Baxalta Innovations GmbH, Vienna, Austria.

Helmut Glantschnig (H)

Baxalta Innovations GmbH, Vienna, Austria.

Fabio Canneva (F)

Baxalta Innovations GmbH, Vienna, Austria.

Maria Schuster (M)

Baxalta Innovations GmbH, Vienna, Austria.

Sogue Coulibaly (S)

Baxalta Innovations GmbH, Vienna, Austria.

Gerald Schrenk (G)

Baxalta Innovations GmbH, Vienna, Austria. Electronic address: gerald.schrenk@takeda.com.

Dirk Voelkel (D)

Baxalta Innovations GmbH, Vienna, Austria.

Michael Dockal (M)

Baxalta Innovations GmbH, Vienna, Austria.

Barbara Plaimauer (B)

Baxalta Innovations GmbH, Vienna, Austria.

Hanspeter Rottensteiner (H)

Baxalta Innovations GmbH, Vienna, Austria.

Herbert Gritsch (H)

Baxalta Innovations GmbH, Vienna, Austria.

Enrica Federti (E)

Department of Medicine, University of Verona, Verona, Italy; Azienda Ospedaliera Universitaria Integrata di Verona, Policlinico GB Rossi, Verona, Italy.

Alessandro Matte (A)

Department of Medicine, University of Verona, Verona, Italy; Azienda Ospedaliera Universitaria Integrata di Verona, Policlinico GB Rossi, Verona, Italy.

Lucia De Franceschi (L)

Department of Medicine, University of Verona, Verona, Italy; Azienda Ospedaliera Universitaria Integrata di Verona, Policlinico GB Rossi, Verona, Italy.

Friedrich Scheiflinger (F)

Baxalta Innovations GmbH, Vienna, Austria.

Werner Hoellriegl (W)

Baxalta Innovations GmbH, Vienna, Austria.

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Classifications MeSH