The impact of intrarenal nitric oxide synthase inhibition on renal blood flow and function in mild and severe hyperdynamic sepsis*

2011 ◽  
Vol 39 (4) ◽  
pp. 770-776 ◽  
Author(s):  
Ken Ishikawa ◽  
Rinaldo Bellomo ◽  
Clive N. May
Keyword(s):  
Nitric Oxide ◽  
Blood Flow ◽  
Nitric Oxide Synthase ◽  
Renal Blood Flow ◽  
And Function ◽  
Oxide Synthase ◽  
The Impact ◽  
Hyperdynamic Sepsis

scholarly journals Effects of chronic nitric oxide synthase (NOS) inhibition on renal blood flow

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Richard Murray McAllister ◽  
Robert L Johnson ◽  
Sean C Newcomer ◽  
Maurice Harold Laughlin
Keyword(s):  
Nitric Oxide ◽  
Blood Flow ◽  
Nitric Oxide Synthase ◽  
Renal Blood Flow ◽  
Oxide Synthase

Nitric oxide synthase and cGMP-mediated stimulation of renin secretion

2001 ◽  
Vol 281 (4) ◽  
pp. R1146-R1151 ◽  
Author(s):  
Cecilia M. Sayago ◽  
William H. Beierwaltes
Keyword(s):  
Nitric Oxide ◽  
Blood Pressure ◽  
Blood Flow ◽  
Nitric Oxide Synthase ◽  
Renal Blood Flow ◽  
No Synthase ◽  
Renin Secretion ◽  
Hemodynamic Changes ◽  
Oxide Synthase ◽  
Stimulation Of

The interaction between nitric oxide (NO) and renin is controversial. cAMP is a stimulating messenger for renin, which is degraded by phosphodiesterase (PDE)-3. PDE-3 is inhibited by cGMP, whereas PDE-5 degrades cGMP. We hypothesized that if endogenous cGMP was increased by inhibiting PDE-5, it could inhibit PDE-3, increasing endogenous cAMP, and thereby stimulate renin. We used the selective PDE-5 inhibitor zaprinast at 20 mg/kg body wt ip, which we determined would not change blood pressure (BP) or renal blood flow (RBF). In thiobutabarbital (Inactin)-anesthetized rats, renin secretion rate (RSR) was determined before and 75 min after administration of zaprinast or vehicle. Zaprinast increased cGMP excretion from 12.75 ± 1.57 to 18.67 ± 1.87 pmol/min ( P < 0.003), whereas vehicle had no effect. Zaprinast increased RSR sixfold (from 2.95 ± 1.74 to 17.62 ± 5.46 ng ANG I · h−1 · min−1, P< 0.024), while vehicle had no effect (from 4.08 ± 2.02 to 3.87 ± 1.53 ng ANG I · h−1 · min−1). There were no changes in BP or RBF. We then tested whether the increase in cGMP could be partially due to the activity of the neuronal isoform of NO synthase (nNOS). Pretreatment with the nNOS inhibitor 7-nitroindazole (7-NI; 50 mg/kg body wt) did not change BP or RBF but attenuated the renin-stimulating effect of zaprinast by 40% compared with vehicle. In 7-NI-treated animals, zaprinast-stimulated cGMP excretion was attenuated by 48%, from 9.17 ± 1.85 to 13.60 ± 2.15 pmol/min, compared with an increase from 10.94 ± 1.90 to 26.38 ± 3.61 pmol/min with zaprinast without 7-NI ( P < 0.04). This suggests that changes in endogenous cGMP production at levels not associated with renal hemodynamic changes are involved in a renin-stimulatory pathway. One source of this cGMP may be nNOS generation of NO in the kidney.

Nitric Oxide Synthase Inhibition Restores Vasopressor Effects of Norepinephrine in Ovine Hyperdynamic Sepsis

1996 ◽  
Vol 83 (5) ◽  
pp. 1009-1013 ◽  
Author(s):  
Jorg Meyer ◽  
Michael Booke ◽  
Rene Waurick ◽  
Thomas Prien ◽  
Hugo Van Aken
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Oxide Synthase ◽  
Hyperdynamic Sepsis

scholarly journals Cloning, Expression, and Purification of a Nitric Oxide Synthase-Like Protein fromBacillus cereus

2010 ◽  
Vol 2010 ◽  
pp. 1-4 ◽  
Author(s):  
Heather J. Montgomery ◽  
Andrea L. Dupont ◽  
Hilary E. Leivo ◽  
J. Guy Guillemette
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Peroxide ◽  
Nitric Oxide Synthase ◽  
Expression And Purification ◽  
Spectral Shifts ◽  
Reconstituted System ◽  
Low Levels ◽  
And Function ◽  
Oxide Synthase ◽  
Reductase Domain

The nitric oxide synthase-like protein fromBacillus cereus(bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer. The recombinant protein showed similar spectral shifts to the mammalian NOS proteins and could bind the substrates L-arginine andNG-hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation ofNG-hydroxy-L-arginine and L-arginine by bcNOS, while a reconstituted system with the rat neuronal NOS reductase domain showed no activity. The recombinant bcNOS protein adds to the complement of bacterial NOS-like proteins that are used for the investigation of the mechanism and function of NO in microorganisms.

scholarly journals Temporal patterns of blood flow and nitric oxide synthase expression affect macrophage accumulation and proliferation during collateral growth

2010 ◽  
Vol 2 (1) ◽  
pp. 18 ◽  
Author(s):  
Hendrik B Sager ◽  
Ralf Middendorff ◽  
Kim Rauche ◽  
Joachim Weil ◽  
Wolfgang Lieb ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Blood Flow ◽  
Nitric Oxide Synthase ◽  
Temporal Patterns ◽  
Collateral Growth ◽  
Oxide Synthase ◽  
Macrophage Accumulation
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