Prolonged in vivo hypoxia enhances nitric oxide synthase type I and type III gene expression in adult rat lung.

1995 ◽  
Vol 13 (2) ◽  
pp. 167-174 ◽  
Author(s):  
P W Shaul ◽  
A J North ◽  
T S Brannon ◽  
K Ujiie ◽  
L B Wells ◽  
...  
Keyword(s):  
Gene Expression ◽  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Type I ◽  
Rat Lung ◽  
Type Iii ◽  
Adult Rat ◽  
Oxide Synthase

Nitric oxide synthase type I and type III gene expression are developmentally regulated in rat lung

1994 ◽  
Vol 266 (6) ◽  
pp. L635-L641 ◽  
Author(s):  
A. J. North ◽  
R. A. Star ◽  
T. S. Brannon ◽  
K. Ujiie ◽  
L. B. Wells ◽  
...  
Keyword(s):  
Gene Expression ◽  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Fetal Lung ◽  
Mrna Abundance ◽  
Type I ◽  
Fetal Life ◽  
Rat Lung ◽  
Developmentally Regulated ◽  
Oxide Synthase

The successful transition from fetal to neonatal life involves a marked decline in pulmonary vascular resistance which is modulated in part by endothelium-derived nitric oxide. To define the molecular processes which prepare the pulmonary circulation for nitric oxide mediation of vasodilatation at the time of birth, we determined the ontogeny of endothelial nitric oxide synthase (NOS-III) gene expression in lungs from fetal and newborn rats. Maturational changes in lung neuronal NOS (NOS-I) expression were also investigated; the latter isoform has been localized to rat bronchiolar epithelium. NOS proteins were examined by immunoblot analysis, and mRNA abundance was assessed in reverse transcription-polymerase chain reaction assays. Both NOS-III and NOS-I protein were detectable in 16-day fetal lung, they increased 3.8- and 3.1-fold, respectively, to maximal levels at 20 days of gestation (term = 22 day), and they fell postnatally (1-5 days). In parallel with the findings for NOS-III protein, NOS-III mRNA increased from 16 to 20 days gestation and fell after birth. In contrast, NOS-I mRNA abundance declined during late fetal life and rose postnatally. These findings were confirmed by Northern analyses. Thus NOS-III and NOS-I gene expression are developmentally regulated in rat lung, with maximal NOS-III and NOS-I protein present near term. The regulation of pulmonary NOS-III may primarily involve alterations in transcription or mRNA stability, whereas NOS-I expression in the maturing lung may also be mediated by additional posttranscriptional processes.

Expression of nitric oxide synthase isoforms (NOS II and NOS III) in adult rat lung in hyperoxic pulmonary hypertension

1999 ◽  
Vol 295 (2) ◽  
pp. 317-329 ◽  
Author(s):  
Wolfgang Steudel ◽  
Masazumi Watanabe ◽  
Krikor Dikranian ◽  
Margaretha Jacobson ◽  
R. C. Jones
Keyword(s):  
Nitric Oxide ◽  
Pulmonary Hypertension ◽  
Nitric Oxide Synthase ◽  
Rat Lung ◽  
Adult Rat ◽  
Oxide Synthase

scholarly journals Regulation of Endothelial Constitutive Nitric Oxide Synthase Gene Expression in Endothelial Cells and In Vivo

Circulation ◽  
2000 ◽  
Vol 101 (6) ◽  
pp. 676-681 ◽  
Author(s):  
Koji Kuboki ◽  
Zhen Y. Jiang ◽  
Noriko Takahara ◽  
Sung Woo Ha ◽  
Masahiko Igarashi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Nitric Oxide ◽  
Endothelial Cells ◽  
Nitric Oxide Synthase ◽  
Constitutive Nitric Oxide Synthase ◽  
Oxide Synthase

scholarly journals Proteomic analysis of endogenous nitrotryptophan-containing proteins in rat hippocampus and cerebellum

2012 ◽  
Vol 32 (6) ◽  
pp. 521-530 ◽  
Author(s):  
Munehiro Uda ◽  
Hiroaki Kawasaki ◽  
Ayako Shigenaga ◽  
Takeshi Baba ◽  
Fumiyuki Yamakura
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Cytoskeletal Proteins ◽  
Post Translational Modification ◽  
Physiological Conditions ◽  
Adult Rat ◽  
Aldolase C ◽  
Tryptophan Residues ◽  
Oxide Synthase

Nitration of tryptophan residues is a novel post-translational modification. In the present study, we examined whether NO2Trp (nitrotryptophan)-containing proteins are produced in the hippocampus and cerebellum of the adult rat under physiological conditions in vivo. Using Western blot analysis with anti-6-NO2Trp-specific antibody, we found many similar immunoreactive spots in the protein extracts from both regions. These spots were subsequently subjected to trypsin digestion and LC-ESI-MS/MS (LC-electrospray ionization-tandem MS) analysis. We identified several cytoskeletal proteins and glycolytic enzymes as NO2Trp-containing proteins and determined the position of nitrated tryptophan residues with significant ion score levels (P<0.05) in several proteins in both regions. We also observed that the total amount of NO2Trp-containing proteins in the cerebellum was significantly greater than that in the hippocampus (P<0.05). Moreover, IP (immunoprecipitation) assays using anti-aldolase C antibody showed that the relative intensity of immunostaining for NO2Trp over aldolase C was much higher in cerebellum than in hippocampus. The amounts of nNOS (neuronal nitric oxide synthase) and eNOS (endothelial nitric oxide synthase) were much greater in cerebellum than in hippocampus. This is the first evidence of several specific sites of nitrated tryptophan in proteins under physiological conditions in vivo.

Attenuation of nitric oxide synthase gene expression in rat lung induced by hypoxia

1996 ◽  
Vol 16 (3) ◽  
pp. 148-151
Author(s):  
Dai Aiguo ◽  
Zhahg Zhenxiang ◽  
Niu Ruji ◽  
Xu Yongjian ◽  
Duan Shengfu
Keyword(s):  
Gene Expression ◽  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Rat Lung ◽  
Oxide Synthase

In Vivo and in Vitro Effects of Lysine Clonixinate on Nitric Oxide Synthase in LPS-Treated and Untreated Rat Lung Preparations

Nitric Oxide ◽  
2001 ◽  
Vol 5 (2) ◽  
pp. 150-157 ◽  
Author(s):  
A.M. Franchi ◽  
G. Di Girolamo ◽  
M. Farina ◽  
A.R. de los Santos ◽  
M.L. Martı́ ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Rat Lung ◽  
Lysine Clonixinate ◽  
In Vitro Effects ◽  
Oxide Synthase
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