scholarly journals Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor

FEBS Letters ◽  
2005 ◽  
Vol 579 (14) ◽  
pp. 3159-3163 ◽  
Author(s):  
Mónica Martínez-Moreno ◽  
Alberto Álvarez-Barrientos ◽  
Fernando Roncal ◽  
Juan Pablo Albar ◽  
Francisco Gavilanes ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Ryanodine Receptor ◽  
Endothelial Nitric Oxide Synthase ◽  
Direct Interaction ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide ◽  
Reductase Domain

scholarly journals Direct Interaction between Endothelial Nitric-oxide Synthase and Dynamin-2

2000 ◽  
Vol 276 (17) ◽  
pp. 14249-14256 ◽  
Author(s):  
Sheng Cao ◽  
Janet Yao ◽  
Timothy J. McCabe ◽  
Qing Yao ◽  
Zvonimir S. Katusic ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Endothelial Nitric Oxide Synthase ◽  
Direct Interaction ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide ◽  
Dynamin 2

scholarly journals Endothelial Nitric Oxide Synthase and Its Negative Regulator Caveolin-1 Localize to Distinct Perinuclear Organelles

2002 ◽  
Vol 50 (6) ◽  
pp. 779-788 ◽  
Author(s):  
Roland Govers ◽  
Peter van der Sluijs ◽  
Elly van Donselaar ◽  
Jan-Willem Slot ◽  
Ton J. Rabelink
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Golgi Complex ◽  
Endothelial Nitric Oxide Synthase ◽  
Direct Interaction ◽  
Negative Regulator ◽  
Caveolin 1 ◽  
Enos Activity ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Caveolin-1 is a member of a subset of intracellular proteins that regulate endothelial nitric oxide synthase (eNOS) activity. In caveolae, caveolin-1 inhibits eNOS activity via a direct interaction with the enzyme. Previous work has indicated that both eNOS and caveolin-1 are also localized at the perinuclear Golgi complex. Whether caveolin-1 is involved in eNOS regulation in this cell compartment is unknown. Here we studied the localization of eNOS and caveolin-1 in the perinuclear region of primary bovine aortic endothelial cells. By immunofluorescence microscopy we show that both eNOS and caveolin-1 co-localize with Golgi markers. On treatment of the cells with the microtubule-depolymerizing drug nocodazole, the Golgi complex is scattered and caveolin-1 is found in vesicles at the periphery of the cell, while eNOS is localized at large structures near the nucleus. The nocodazole-induced redistribution of eNOS is similar to that of cis-, medial-, and trans-Golgi markers, while the caveolin-1 redistribution resembles that of sec22, a marker for the intermediate compartment. The localization of eNOS and caveolin-1 at distinct perinuclear compartments that behave differently in the presence of nocodazole indicates that eNOS activity is not regulated by caveolin-1 in the Golgi complex.

scholarly journals Interaction between Caveolin-1 and the Reductase Domain of Endothelial Nitric-oxide Synthase

1998 ◽  
Vol 273 (35) ◽  
pp. 22267-22271 ◽  
Author(s):  
Sanjay Ghosh ◽  
Ratan Gachhui ◽  
Carol Crooks ◽  
Chaoqun Wu ◽  
Michael P. Lisanti ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Endothelial Nitric Oxide Synthase ◽  
Caveolin 1 ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide ◽  
Reductase Domain

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).

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