187: Nitric oxide inhibition enhances cyclooxygenase-2 induction in smooth muscle cells through modulation of phosphorylation signalling events

2008 ◽  
Vol 2 (5) ◽  
pp. S87
2001 ◽  
Vol 34 (1) ◽  
pp. 76-83 ◽  
Author(s):  
Gilbert R. Upchurch ◽  
John W. Ford ◽  
Steven J. Weiss ◽  
Brian S. Knipp ◽  
David A. Peterson ◽  
...  

2000 ◽  
Vol 191 (4) ◽  
pp. S73
Author(s):  
Gilbert R Upchurch ◽  
John W Ford ◽  
Steven J Weiss ◽  
James J Mule ◽  
Michael A Marletta ◽  
...  

1995 ◽  
Vol 74 (03) ◽  
pp. 980-986 ◽  
Author(s):  
Valérie B Schini-Kerth ◽  
Beate Fißithaler ◽  
Thomas T Andersen ◽  
John W Fenton ◽  
Paul M Vanhoutte ◽  
...  

SummaryProteolytically active forms of thrombin (α- and γ-thrombin) and thrombin receptor peptides inhibited the release of nitrite, a stable endproduct of nitric oxide, evoked by interleukin-1 β(IL-1 β) in cultured vascular smooth muscle cells while proteolytically inactive forms [D-Phe-Pro-Arg chloromethyl ketone-α-thrombin (PPACK-α- thrombin) and diisopropylphosphoryl-α-thrombin (DIP-α-thrombin)] had either no or only minimal inhibitory effects. Under bioassay conditions, perfusates from columns containing IL-1 β-activated vascular smooth muscle cells or cells treated with IL-1βplus PPACK-α-thrombin relaxed detector blood vessels. These relaxations were abolished by the inhibitor of nitric oxide synthesis, NG-nitro-L arginine. No relaxations were obtained with untreated cells or IL-1 β-treated cells in the presence of α-thrombin. The expression of inducible nitric oxide synthase mRNA and protein in vascular smooth muscle cells by IL-1 β was impaired by α-thrombin. These results demonstrate that thrombin regulates the expression of the inducible nitric oxide synthase at a transcriptional level via the proteolytic activation of the thrombin receptor in vascular smooth muscle cells


2000 ◽  
Vol 191 (4) ◽  
pp. S25-S26
Author(s):  
Nicholas J Zyromski ◽  
Judith A Duenes ◽  
Michael L Kendrick ◽  
Gianrico Farrugia ◽  
Michael G Sarr

Sign in / Sign up

Export Citation Format

Share Document