B2 kinin receptor activation is the predominant mechanism by which trypsin mediates endothelium-dependent relaxation in bovine coronary arteries-Reference-Cited by-同舟云学术

B2 kinin receptor activation is the predominant mechanism by which trypsin mediates endothelium-dependent relaxation in bovine coronary arteries

Published:2008-05-06 Issue:1 Volume:378 Page:33-41
ISSN:0028-1298
Container-title:Naunyn-Schmiedeberg's Archives of Pharmacology
language:en
Short-container-title:Naunyn-Schmied Arch Pharmacol

Author:

Drummond Grant R.,Selemidis Stavros,Cocks Thomas M.

Publisher

Springer Science and Business Media LLC

Subject

Pharmacology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/s00210-008-0291-x.pdf

Reference40 articles.

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2. Blackhart BD, Emilsson K, Nguyen D, Teng W, Martelli AJ, Nystedt S, Sundelin J, Scarborough RM (1996) Ligand cross-reactivity within the protease-activated receptor family. J Biol Chem 271:16466–16471

3. Cocks TM, Moffatt JD (2000) Protease-activated receptors: sentries for inflammation? Trends Pharmacol Sci 21:103–108

4. Colman RW, Pixley RA, Najamunnisa S, Yan W, Wang J, Mazar A, McCrae KR (1997) Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor. J Clin Invest 100:1481–1487

5. De Mey JG, Vanhoutte PM (1981) Role of the intima in the relaxation of the canine femoral artery caused by thrombin. Arch Int Pharmacodyn Ther 250:314–315

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