Heat Stress-Activated, Calcium-Dependent Nitric Oxide Synthase in Sponges

Nitric Oxide ◽  
2001 ◽  
Vol 5 (5) ◽  
pp. 427-431 ◽  
Author(s):  
Marco Giovine ◽  
Marina Pozzolini ◽  
Anna Favre ◽  
Giorgio Bavestrello ◽  
Carlo Cerrano ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Heat Stress ◽  
Nitric Oxide Synthase ◽  
Calcium Dependent ◽  
Oxide Synthase

Inhibition of calcium-dependent nitric oxide synthase causes ileitis and leukocytosis in guinea pigs

1994 ◽  
Vol 39 (6) ◽  
pp. 1185-1192 ◽  
Author(s):  
Mark J. S. Miller ◽  
Upender K. Munshi ◽  
Halina Sadowska-Krowicka ◽  
Jane L. Kakkis ◽  
Xiao-Jing Zhang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Guinea Pigs ◽  
Calcium Dependent ◽  
Oxide Synthase

scholarly journals Relations between nitric oxide synthase DNOS1, Hsp70 and apoptosis regulatory gene grim in Drosophila melanogaster after heat stress induction

2010 ◽  
Vol 26 (3) ◽  
pp. 194-199
Author(s):  
E. M. Khussainova ◽  
Z. A. Bulentayeva ◽  
B. O. Bekmanov ◽  
L. B. Djansugurova ◽  
R. I. Bersimbayev
Keyword(s):  
Nitric Oxide ◽  
Drosophila Melanogaster ◽  
Heat Stress ◽  
Nitric Oxide Synthase ◽  
Regulatory Gene ◽  
Stress Induction ◽  
Oxide Synthase

Estrogen Does Not Induce the Calcium-Dependent Nitric Oxide Synthase in Cultured Human Uterine Endothelial and Myometrial Smooth Muscle Cells

1997 ◽  
Vol 34 (4) ◽  
pp. 281-288 ◽  
Author(s):  
Walter Tschugguel ◽  
Zydi Zhegu ◽  
Christian Schneeberger ◽  
Eva Tantscher ◽  
Klaus Czerwenka ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Smooth Muscle ◽  
Nitric Oxide Synthase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Calcium Dependent ◽  
Oxide Synthase

scholarly journals Tyrosine nitration on calmodulin enhances calcium-dependent association and activation of nitric-oxide synthase

2019 ◽  
Vol 295 (8) ◽  
pp. 2203-2211 ◽  
Author(s):  
Joseph J. Porter ◽  
Hyo Sang Jang ◽  
Mohammad Mahfuzul Haque ◽  
Dennis J. Stuehr ◽  
Ryan A. Mehl
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Calcium Binding ◽  
Vascular Dysfunction ◽  
Post Translational Modification ◽  
Calcium Dependent ◽  
Genetic Code Expansion ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Production of reactive oxygen species caused by dysregulated endothelial nitric-oxide synthase (eNOS) activity is linked to vascular dysfunction. eNOS is a major target protein of the primary calcium-sensing protein calmodulin. Calmodulin is often modified by the main biomarker of nitroxidative stress, 3-nitrotyrosine (nitroTyr). Despite nitroTyr being an abundant post-translational modification on calmodulin, the mechanistic role of this modification in altering calmodulin function and eNOS activation has not been investigated. Here, using genetic code expansion to site-specifically nitrate calmodulin at its two tyrosine residues, we assessed the effects of these alterations on calcium binding by calmodulin and on binding and activation of eNOS. We found that nitroTyr–calmodulin retains affinity for eNOS under resting physiological calcium concentrations. Results from in vitro eNOS assays with calmodulin nitrated at Tyr-99 revealed that this nitration reduces nitric-oxide production and increases eNOS decoupling compared with WT calmodulin. In contrast, calmodulin nitrated at Tyr-138 produced more nitric oxide and did so more efficiently than WT calmodulin. These results indicate that the nitroTyr post-translational modification, like tyrosine phosphorylation, can impact calmodulin sensitivity for calcium and reveal Tyr site-specific gain or loss of functions for calmodulin-induced eNOS activation.

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