Defective Flow-Migration Coupling Causes Arteriovenous Malformations in Hereditary Hemorrhagic Telangiectasia.


Journal

Circulation
ISSN: 1524-4539
Titre abrégé: Circulation
Pays: United States
ID NLM: 0147763

Informations de publication

Date de publication:
07 09 2021
Historique:
pubmed: 30 6 2021
medline: 30 12 2021
entrez: 29 6 2021
Statut: ppublish

Résumé

Activin receptor-like kinase 1 (ALK1) is an endothelial transmembrane serine threonine kinase receptor for BMP family ligands that plays a critical role in cardiovascular development and pathology. Loss-of-function mutations in the Using Cre lines that recombine in different subsets of arterial, capillary-venous, or endothelial tip cells, we show that capillary-venous ALK1 deletion impaired capillary-venous endothelial cell polarization against the direction of blood flow in vivo and in vitro. Mechanistically, ALK1-deficient cells exhibited increased integrin signaling interaction with vascular endothelial growth factor receptor 2, which enhanced downstream YAP/TAZ nuclear translocation. Pharmacologic inhibition of integrin or YAP/TAZ signaling rescued flow migration coupling and prevented vascular malformations in Our study reveals ALK1 as an essential driver of flow-induced endothelial cell migration and identifies loss of flow-migration coupling as a driver of arteriovenous malformation formation in hereditary hemorrhagic telangiectasia disease. Integrin-YAP/TAZ signaling blockers are new potential targets to prevent vascular malformations in patients with hereditary hemorrhagic telangiectasia.

Sections du résumé

BACKGROUND
Activin receptor-like kinase 1 (ALK1) is an endothelial transmembrane serine threonine kinase receptor for BMP family ligands that plays a critical role in cardiovascular development and pathology. Loss-of-function mutations in the
METHODS
Using Cre lines that recombine in different subsets of arterial, capillary-venous, or endothelial tip cells, we show that capillary-venous
RESULTS
ALK1 deletion impaired capillary-venous endothelial cell polarization against the direction of blood flow in vivo and in vitro. Mechanistically, ALK1-deficient cells exhibited increased integrin signaling interaction with vascular endothelial growth factor receptor 2, which enhanced downstream YAP/TAZ nuclear translocation. Pharmacologic inhibition of integrin or YAP/TAZ signaling rescued flow migration coupling and prevented vascular malformations in
CONCLUSIONS
Our study reveals ALK1 as an essential driver of flow-induced endothelial cell migration and identifies loss of flow-migration coupling as a driver of arteriovenous malformation formation in hereditary hemorrhagic telangiectasia disease. Integrin-YAP/TAZ signaling blockers are new potential targets to prevent vascular malformations in patients with hereditary hemorrhagic telangiectasia.

Identifiants

pubmed: 34182767
doi: 10.1161/CIRCULATIONAHA.120.053047
pmc: PMC8429266
mid: NIHMS1727528
doi:

Substances chimiques

KDR protein, human EC 2.7.10.1
Vascular Endothelial Growth Factor A 0
Vascular Endothelial Growth Factor Receptor-2 EC 2.7.10.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

805-822

Subventions

Organisme : NEI NIH HHS
ID : P30 EY026878
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY025979
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL135582
Pays : United States

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Auteurs

Hyojin Park (H)

Cardiovascular Research Center, Department of Internal Medicine (H.P., J.F., M.P., M.C., S.Y., M.A.S., A.E.), Yale University School of Medicine, New Haven, CT.

Jessica Furtado (J)

Cardiovascular Research Center, Department of Internal Medicine (H.P., J.F., M.P., M.C., S.Y., M.A.S., A.E.), Yale University School of Medicine, New Haven, CT.

Mathilde Poulet (M)

Cardiovascular Research Center, Department of Internal Medicine (H.P., J.F., M.P., M.C., S.Y., M.A.S., A.E.), Yale University School of Medicine, New Haven, CT.

Minhwan Chung (M)

Cardiovascular Research Center, Department of Internal Medicine (H.P., J.F., M.P., M.C., S.Y., M.A.S., A.E.), Yale University School of Medicine, New Haven, CT.

Sanguk Yun (S)

Cardiovascular Research Center, Department of Internal Medicine (H.P., J.F., M.P., M.C., S.Y., M.A.S., A.E.), Yale University School of Medicine, New Haven, CT.

Sungwoon Lee (S)

Department of Pharmacology (S.L., W.C.S.), Yale University School of Medicine, New Haven, CT.

William C Sessa (WC)

Department of Pharmacology (S.L., W.C.S.), Yale University School of Medicine, New Haven, CT.

Claudio A Franco (CA)

Instituto de Medicina Molecular João Lobo Antunes and Instituto de Histologia e Biologia do Desenvolvimento, Faculdade de Medicina, Universidade de Lisboa, Portugal (C.A.F.).

Martin A Schwartz (MA)

Cardiovascular Research Center, Department of Internal Medicine (H.P., J.F., M.P., M.C., S.Y., M.A.S., A.E.), Yale University School of Medicine, New Haven, CT.
Department of Cell Biology (M.A.S.), Yale University School of Medicine, New Haven, CT.
Department of Biomedical Engineering (M.A.S.), Yale University School of Medicine, New Haven, CT.

Anne Eichmann (A)

Cardiovascular Research Center, Department of Internal Medicine (H.P., J.F., M.P., M.C., S.Y., M.A.S., A.E.), Yale University School of Medicine, New Haven, CT.
Department of Molecular and Cellular Physiology (A.E.), Yale University School of Medicine, New Haven, CT.
Université de Paris, PARCC, INSERM, Paris, France (A.E.).

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Classifications MeSH