scholarly journals Nitric Oxide Regulation of MMP-9 Activation and Its Relationship to Modifications of the Cysteine Switch†

Biochemistry ◽  
2008 ◽  
Vol 47 (21) ◽  
pp. 5832-5840 ◽  
Author(s):  
Sean M. McCarthy ◽  
Peter F. Bove ◽  
Dwight E. Matthews ◽  
Takaaki Akaike ◽  
Albert van der Vliet
Keyword(s):  
Nitric Oxide ◽  
Cysteine Switch

Effects of reactive metabolites of oxygen and nitrogen on gelatinase A activity

1997 ◽  
Vol 273 (2) ◽  
pp. L445-L450 ◽  
Author(s):  
M. W. Owens ◽  
S. A. Milligan ◽  
D. Jourd'heuil ◽  
M. B. Grisham
Keyword(s):  
Nitric Oxide ◽  
Matrix Protein ◽  
Gelatinase A ◽  
Simultaneous Generation ◽  
Zinc Thiolate ◽  
Switch Mechanism ◽  
Increased Activity ◽  
Metalloproteinase Activity ◽  
Cysteine Switch ◽  
Proper Balance

The regulation of matrix metalloproteinase activity is crucial for maintaining the proper balance of tissue remodeling vs. injury. Metalloproteinase proenzymes are activated when the active site zinc is exposed via a cysteine switch mechanism. Peroxynitrite, the product generated from the interaction between nitric oxide and superoxide, has been shown to release zinc from zinc-thiolate groups, suggesting that it might alter metalloproteinase activity. This study examined the effects of nitric oxide and superoxide generators on gelatinase A activity. Results showed that nitric oxide alone had no effect on gelatinase A activity relative to control, whereas superoxide-derived metabolites increased activity. The simultaneous generation of both nitric oxide and superoxide caused an inhibition of gelatinase A activity. This inhibition was reversed by the addition of hemoglobin, superoxide dismutase, or sodium urate, suggesting that peroxynitrite and/or peroxynitrous acid caused the inhibition. Authentic peroxynitrite also inhibited gelatinase A activity. We postulate that the relative fluxes of nitric oxide and superoxide at sites of inflammation may modulate metalloproteinase activity and thus affect matrix protein metabolism.

Localization of endothelial nitric oxide synthase in the normal and failing human atrial myocardium

1996 ◽  
Vol 54 ◽  
pp. 786-787
Author(s):  
Chi-Ming Wei ◽  
Margarita Bracamonte ◽  
Shi-Wen Jiang ◽  
Richard C. Daly ◽  
Christopher G.A. McGregor ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Heart Failure ◽  
Nitric Oxide Synthase ◽  
Endothelial Nitric Oxide Synthase ◽  
Cardiac Tissues ◽  
Mammalian Tissues ◽  
End Stage Heart Failure ◽  
End Stage ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Nitric oxide (NO) is a potent endothelium-derived relaxing factor which also may modulate cardiomyocyte inotropism and growth via increasing cGMP. While endothelial nitric oxide synthase (eNOS) isoforms have been detected in non-human mammalian tissues, expression and localization of eNOS in the normal and failing human myocardium are poorly defined. Therefore, the present study was designed to investigate eNOS in human cardiac tissues in the presence and absence of congestive heart failure (CHF).Normal and failing atrial tissue were obtained from six cardiac donors and six end-stage heart failure patients undergoing primary cardiac transplantation. ENOS protein expression and localization was investigated utilizing Western blot analysis and immunohistochemical staining with the polyclonal rabbit antibody to eNOS (Transduction Laboratories, Lexington, Kentucky).

Nitric Oxide Reduces Pressor Responsiveness During Ovine Hypoadrenocorticism

2001 ◽  
Vol 28 (5-6) ◽  
pp. 459-462
Author(s):  
Pini Orbach ◽  
Charles E Wood ◽  
Maureen Keller-Wood
Keyword(s):  
Nitric Oxide

Nitric oxide synthase and cellac disease

2001 ◽  
Vol 120 (5) ◽  
pp. A684-A684
Author(s):  
I DANIELS ◽  
I MURRAY ◽  
W GODDARD ◽  
R LONG
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Oxide Synthase

Intralipid-induced gastric relaxation in humans is mediated by nitric oxide

2001 ◽  
Vol 120 (5) ◽  
pp. A461-A461
Author(s):  
S KUIKEN ◽  
G TYTGAT ◽  
G BOEKXSTAENS
Keyword(s):  
Nitric Oxide
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