Endothelial Protease Nexin-1 Is a Novel Regulator of A Disintegrin and Metalloproteinase 17 Maturation and Endothelial Protein C Receptor Shedding via Furin Inhibition | Zendy

Yacine Boulaftali | Zendy; Déborah François | Zendy; Laurence Vénisse | Zendy; Martine JandrotPerrus | Zendy; Véronique Arocas | Zendy; MarieChristine Bouton | Zendy

Open Access

Endothelial Protease Nexin-1 Is a Novel Regulator of A Disintegrin and Metalloproteinase 17 Maturation and Endothelial Protein C Receptor Shedding via Furin Inhibition

Author(s) -

Yacine Boulaftali,

Déborah François,

Laurence Vénisse,

Martine JandrotPerrus,

Véronique Arocas,

MarieChristine Bouton

Publication year - 2013

Publication title -

arteriosclerosis thrombosis and vascular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.007

H-Index - 270

eISSN - 1524-4636

pISSN - 1079-5642

DOI - 10.1161/atvbaha.113.301494

Subject(s) - disintegrin , furin , microbiology and biotechnology , vascular endothelial growth inhibitor , metalloproteinase , endothelial stem cell , biology , serine protease , receptor , proteases , protease , chemistry , vascular endothelial growth factor a , matrix metalloproteinase , cancer research , biochemistry , in vitro , vascular endothelial growth factor , enzyme , vegf receptors

Human protein C is a plasma serine protease that plays a key role in hemostasis, and activated protein C (aPC) is known to elicit protective responses in vascular endothelial cells. This cytoprotective activity requires the interaction of the protease with its cell membrane receptor, endothelial protein C receptor. However, the mechanisms regulating the beneficial cellular effects of aPC are not well known. We aimed to determine whether a serine protease inhibitor called protease nexin-1 (PN-1) or serpinE2, expressed by vascular cells, can modulate the effect of aPC on endothelial cells.

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