β-arrestin-2 in PAR-1-biased signaling has a crucial role in endothelial function via PDGF-β in stroke.


Journal

Cell death & disease
ISSN: 2041-4889
Titre abrégé: Cell Death Dis
Pays: England
ID NLM: 101524092

Informations de publication

Date de publication:
04 02 2019
Historique:
received: 14 05 2018
accepted: 15 01 2019
revised: 07 01 2019
entrez: 6 2 2019
pubmed: 6 2 2019
medline: 9 4 2020
Statut: epublish

Résumé

Thrombin aggravates ischemic stroke and activated protein C (APC) has a neuroprotective effect. Both proteases interact with protease-activated receptor 1, which exhibits functional selectivity and leads to G-protein- and β-arrestin-mediated-biased signal transduction. We focused on the effect of β-arrestin in PAR-1-biased signaling on endothelial function after stroke or high-fat diet (HFD). Thrombin had a rapid disruptive effect on endothelial function, but APC had a slow protective effect. Paralleled by prolonged MAPK 42/44 signaling activation by APC via β-arrestin-2, a lower cleavage rate of PAR-1 for APC than thrombin was quantitatively visualized by bioluminescence video imaging. HFD-fed mice showed lower β-arrestin-2 levels and more severe ischemic injury. The expression of β-arrestin-2 in capillaries and PDGF-β secretion in HFD-fed mice were reduced in penumbra lesions. These results suggested that β-arrestin-2-MAPK-PDGF-β signaling enhanced protection of endothelial function and barrier integrity after stroke.

Identifiants

pubmed: 30718498
doi: 10.1038/s41419-019-1375-x
pii: 10.1038/s41419-019-1375-x
pmc: PMC6361911
doi:

Substances chimiques

Protein C 0
Proto-Oncogene Proteins c-sis 0
Receptor, PAR-1 0
Recombinant Proteins 0
beta-Arrestin 2 0
MAP Kinase Kinase 2 EC 2.7.12.2
Thrombin EC 3.4.21.5
drotrecogin alfa activated JGH8MYC891

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

100

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Auteurs

Hideaki Kanki (H)

Department of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.

Tsutomu Sasaki (T)

Department of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan. sasaki@neurol.med.osaka-u.ac.jp.

Shigenobu Matsumura (S)

Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, 611-0011, Kyoto, Japan.

Satoru Yokawa (S)

School of Pharmacy, Aichi Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku, Nagoya, 464-8650, Japan.

Toshiro Yukami (T)

Department of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.

Munehisa Shimamura (M)

Department of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Department of Health, Development and Medicine, Osaka University Graduate School of Medicine, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.

Manabu Sakaguchi (M)

Department of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.

Tadahide Furuno (T)

School of Pharmacy, Aichi Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku, Nagoya, 464-8650, Japan.

Takahiro Suzuki (T)

School of Dentistry, Aichi Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku, Nagoya, 464-8650, Japan.

Hideki Mochizuki (H)

Department of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.

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Classifications MeSH