Plasmin as a previously unknown powerful inducer of the endothelium-dependent vasodilatation

Sergeev, I. Yu.; Bashkov, G.V.

doi:10.1016/0268-9499(94)90557-6

Fibrinolysis

1994

DOI: 10.1016/0268-9499(94)90557-6

|View full text |Cite

Plasmin as a previously unknown powerful inducer of the endothelium-dependent vasodilatation

I. Yu. Sergeev¹,

G.V. Bashkov²

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2007

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The NO-dependent relaxant effect of plasmin has been reported in rat arteries. 18 However, the precise mechanism for the plasmin-induced relaxation and the receptors involved still remain to be elucidated.In the present study, we aimed to determine the role of plasmin in the regulation of vascular tone and investigated the mechanism of plasmin-induced vasorelaxation in the porcine coronary artery. The effects of plasmin on [Ca 2ϩ ] i and the production of NO were also determined in the cultured …”

mentioning

confidence: 99%

Plasmin Induces Endothelium-Dependent Nitric Oxide–Mediated Relaxation in the Porcine Coronary Artery

Fujiyoshi

Hirano

Hirano³

et al. 2007

ATVB

View full text Add to dashboard Cite

Objective-Plasmin is a key enzyme in fibrinolysis. We attempted to determine the possible role of plasmin in the regulation of vascular tone, while also investigating the mechanism of plasmin-induced vasorelaxation. Methods and Results-In porcine coronary artery, plasmin induced an endothelium-dependent relaxation. This relaxing effect was mostly abolished by a proteinase inhibitor, a plasmin inhibitor, or a nitric oxide (NO) synthase inhibitor. The preceding stimulation with plasmin significantly inhibited the subsequent relaxation induced by thrombin but not that induced by proteinase-activated receptor-1-activating peptide. The relaxation induced by trypsin and substance P remained unaffected by the preceding plasmin stimulation. The pretreatment with plasmin, thrombin, or trypsin significantly attenuated the plasmin-induced relaxation. In porcine coronary artery endothelial cells ( Key Words: plasmin Ⅲ proteinase-activated receptor Ⅲ vasorelaxation Ⅲ nitric oxide Ⅲ endothelium P roteinases involved in the blood coagulation cascade not only play an important role in hemostasis but also exert various vascular effects such as the regulation of the vascular tone, tissue remodeling, and angiogenesis. 1,2 Proteinase-activated receptors (PARs) play a major role in mediating such cellular effects of proteinases. [3][4][5][6] PARs belong to a unique family of G protein-coupled receptor. 3 Four members of PARs have been cloned. PAR1, PAR3, and PAR4 serve as receptors for thrombin, whereas PAR1, PAR2, and PAR4 serve as receptors for trypsin. 3 The activation of PAR is initiated by the proteolytic cleavage at the specific site of the extracellular domain. 3 Under physiological conditions, thrombin and trypsin mainly have been reported to induce an endothelium-dependent vasorelaxation in various type of blood vessel. [5][6][7] We have previously reported that thrombin and trypsin induced a transient elevation of cytosolic Ca 2ϩ concentration ([Ca 2ϩ ] i ) in vascular and aortic valve endothelial cells 8 -10 and an endothelium-dependent relaxation in the porcine coronary artery. 8,9,10,11 Plasmin, as a key enzyme in fibrinolysis, has been reported to induce the cell migration in Chinese hamster ovary cells, 12 the cell proliferation in the murine thoracic aorta smooth muscle cells, 13 and an increase in the expression of Cyr61, a growth factor-like gene, in fibroblast. 14 These reports suggested PAR1 to mediate the cellular effects of plasmin. However, the roles of plasmin in the regulation of vascular tone still remain to be determined. Plasmin has been reported to cleave PAR1 at the C-terminal side of the tethered ligand region, thus inactivating the responsiveness of PAR1. 15,16 Plasmin has been shown to cleave the extracellular region of PAR2 at the N-terminal side of the trypsin cleavage site as well as the trypsin site, 16 although it was also shown to attenuate the subsequent PAR2-mediated [Ca 2ϩ ] i elevation in the rat brain capillary endothelial cell. 17 Therefore, the receptor(s) that mediate the cellular...

show abstract

mentioning

confidence: 99%

Plasmin Induces Endothelium-Dependent Nitric Oxide–Mediated Relaxation in the Porcine Coronary Artery

Fujiyoshi

Hirano

Hirano³

et al. 2007

ATVB

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Plasmin as a previously unknown powerful inducer of the endothelium-dependent vasodilatation

Cited by 1 publication

References 0 publications

Plasmin Induces Endothelium-Dependent Nitric Oxide–Mediated Relaxation in the Porcine Coronary Artery

Plasmin Induces Endothelium-Dependent Nitric Oxide–Mediated Relaxation in the Porcine Coronary Artery

Contact Info

Product

Resources

About