P107. Cobalamins and cobinamides directly inhibit nitric oxide synthase enzymatic activity

Nitric Oxide ◽  
2006 ◽  
Vol 14 (4) ◽  
pp. 51-52
Author(s):  
J. Brice Weinberg ◽  
Youwei Chen ◽  
Bethany E. Beasley ◽  
Dipak K. Ghosh
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Enzymatic Activity ◽  
Oxide Synthase

Nitric oxide synthase expression and enzymatic activity in multiple sclerosis

2004 ◽  
Vol 109 (4) ◽  
pp. 261-269 ◽  
Author(s):  
H. Broholm ◽  
B. Andersen ◽  
B. Wanscher ◽  
J. L. Frederiksen ◽  
I. Rubin ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Multiple Sclerosis ◽  
Nitric Oxide Synthase ◽  
Enzymatic Activity ◽  
Oxide Synthase

scholarly journals A specific method for measurement of nitric oxide synthase enzymatic activity in peritoneal biopsies

2000 ◽  
Vol 57 (1) ◽  
pp. 332-338 ◽  
Author(s):  
Sophie Combet ◽  
Jean-Luc Balligand ◽  
Norbert Lameire ◽  
Eric Goffin ◽  
Olivier Devuyst
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Enzymatic Activity ◽  
Specific Method ◽  
Oxide Synthase

Cell growth modulates nitric oxide synthase expression in fetal pulmonary artery endothelial cells

2000 ◽  
Vol 278 (1) ◽  
pp. L131-L138 ◽  
Author(s):  
Jeannette A. Whitney ◽  
Zohre German ◽  
Todd S. Sherman ◽  
Ivan S. Yuhanna ◽  
Philip W. Shaul
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Cell Growth ◽  
Nitric Oxide Synthase ◽  
Pulmonary Artery ◽  
Enzymatic Activity ◽  
Vascular Function ◽  
Enos Gene ◽  
Enos Expression ◽  
Oxide Synthase

Nitric oxide (NO), produced by endothelial (e) nitric oxide synthase (NOS), is a critical mediator of vascular function and growth in the developing lung. Pulmonary eNOS expression is diminished in conditions associated with altered pulmonary vascular development, suggesting that eNOS may be modulated by changes in pulmonary artery endothelial cell (PAEC) growth. We determined the effects of cell growth on eNOS expression in cultured ovine fetal PAEC studied at varying levels of confluence. NOS enzymatic activity was sixfold greater in quiescent PAEC at 100% confluence compared with more rapidly replicating cells at 50% confluence. To determine if there is a reciprocal effect of NO on PAEC growth, studies of NOS inhibition or the provision of exogenous NO from spermine NONOate were performed. Neither intervention had a discernable effect on PAEC growth. The influence of cell growth on NOS activity was unique to pulmonary endothelium, because varying confluence did not alter NOS activity in fetal systemic endothelial cells. The effects of cell growth induced by serum stimulation were also evaluated, and NOS enzymatic activity was threefold greater in quiescent, serum-deprived cells compared with that in serum-stimulated cells. The increase in NOS activity observed at full confluence was accompanied by parallel increases in eNOS protein and mRNA expression. These findings indicate that eNOS gene expression in fetal PAEC is upregulated during cell quiescence and downregulated during rapid cell growth. Furthermore, the interaction between cell growth and NO in the PAEC is unidirectional.

Endothelial cell nitric oxide production in acute chest syndrome

1999 ◽  
Vol 277 (4) ◽  
pp. H1579-H1592 ◽  
Author(s):  
Samuel I. Hammerman ◽  
Elizabeth S. Klings ◽  
Katherine P. Hendra ◽  
Gilbert R. Upchurch ◽  
David C. Rishikof ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cell ◽  
Nitric Oxide Synthase ◽  
Enzymatic Activity ◽  
Sickle Cell ◽  
Fold Increase ◽  
Acute Chest Syndrome ◽  
No Production ◽  
Dependent Manner ◽  
Oxide Synthase

Acute chest syndrome (ACS) is the most common form of acute pulmonary disease associated with sickle cell disease. To investigate the possibility that alterations in endothelial cell (EC) production and metabolism of nitric oxide (NO) products might be contributory, we measured NO products from cultured pulmonary EC exposed to red blood cells and/or plasma from sickle cell patients during crisis. Exposure to plasma from patients with ACS caused a 5- to 10-fold increase in S-nitrosothiol (RSNO) and a 7- to 14-fold increase in total nitrogen oxide (NOx) production by both pulmonary arterial and microvascular EC. Increases occurred within 2 h of exposure to plasma in a concentration-dependent manner and were associated with increases in endothelial nitric oxide synthase (eNOS) protein and eNOS enzymatic activity, but not with changes in nitric oxide synthase (NOS) III or NOS II transcripts, inducible NOS (iNOS) protein nor iNOS enzymatic activity. RSNO and NOxincreased whether plasma was obtained from patients with ACS or other forms of vasoocclusive crisis. Furthermore, an oxidative state occurred and oxidative metabolites of NO, particularly peroxynitrite, were produced. These findings suggest that altered NO production and metabolism to damaging oxidative molecules contribute to the pathogenesis of ACS.

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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