Search results for "NITRIC OXIDE SYNTHASE"

Purification of isoforms of nitric oxide synthase

1996

Nitric Oxide Synthase(s)

2007

NO synthases (NOS) represent a family of enzymes that catalyze the formation of nitric oxide (NO) from the amino acid L-arginine. In mammals, three isoforms of NOS have been identified …

Evidence for a possible NOS back-up system in the organ of Corti of the guinea pig

2003

Recently, the two Ca(2+)/calmodulin-regulated nitric oxide synthase isoforms, nNOS and eNOS, and NO itself have been identified in the cochlea of vertebrates using specific antibodies and a new fluorescence indicator. In order to acquire more information about the quantitative and spatial distribution of these two constitutively expressed NOS isoforms (cNOS) in the organ of Corti at the cellular and subcelluar levels, ultrathin sections of London resin (LR) White-embedded cochleae of the guinea pig were incubated with various concentrations of commercially available antibodies to nNOS and eNOS. The immunoreactivity was visualized by a gold-labeled secondary antibody and the amount of the im…

Potential Functional Significance of Brain-Type and Muscle-Type Nitric Oxide Synthase I Expressed in Adventitia and Media of Rat Aorta

1999

Abstract —Skeletal muscle and myocardium express μNOS I, an elongated splice variant of neuronal-type nitric oxide (NO) synthase (NOS I), and NOS III, endothelial-type NO synthase, respectively. This study was designed to elucidate whether vascular smooth muscle also contains a constitutively expressed NO synthase isoform. In the rat, μNOS I contains an insert of 102 nucleotides after nucleotide 2865 of the cDNA, yielding a protein of 164 kd. Reverse transcription-polymerase chain reaction with primers flanking this insert and with insert-specific primers indicated that endothelium-denuded rat aorta expresses both brain-type NOS I and μNOS I. RNase protection analyses with an antisense RNA…

Regulation of the expression of inducible nitric oxide synthase

2010

Nitric oxide (NO) generated by the inducible isoform of nitric oxide synthase (iNOS) is involved in complex immunomodulatory and antitumoral mechanisms and has been described to have multiple beneficial microbicidal, antiviral and antiparasital effects. However, dysfunctional induction of iNOS expression seems to be involved in the pathophysiology of several human diseases. Therefore iNOS has to be regulated very tightly. Modulation of expression, on both the transcriptional and post-transcriptional level, is the major regulation mechanism for iNOS. Pathways resulting in the induction of iNOS expression vary in different cells or species. Activation of the transcription factors NF-kappaB an…

Regulation of the expression of inducible nitric oxide synthase

2004

The role of nitric oxide (NO) generated by the inducible isoform of nitric oxide synthase (iNOS) is very complex. Induction of iNOS expression and hence NO production has been described to have beneficial antiviral, antiparasital, microbicidal, immunomodulatory, and antitumoral effects. However, induced at the wrong place or at the wrong time, iNOS has detrimental consequences and seems to be involved in the pathophysiology of different human diseases. The pathways regulating iNOS expression seem to vary in different cells or different species. In general, activation of the transcription factors nuclear factor (NF)-kappaB and signal transducer and activator of transcription (STAT)-1alpha an…

Nitric oxide synthase isozymes. Characterization, purification, molecular cloning, and functions.

1994

Three isozymes of nitric oxide (NO) synthase (EC 1.14.13.39) have been identified and the cDNAs for these enzymes isolated. In humans, isozymes I (in neuronal and epithelial cells), II (in cytokine-induced cells), and III (in endothelial cells) are encoded for by three different genes located on chromosomes 12, 17, and 7, respectively. The deduced amino acid sequences of the human isozymes show less than 59% identity. Across species, amino acid sequences for each isoform are well conserved (> 90% for isoforms I and III, > 80% for isoform II). All isoforms use L-arginine and molecular oxygen as substrates and require the cofactors NADPH, 6(R)-5,6,7,8-tetrahydrobiopterin, flavin adenine…

Regulation of the Expression of Nitric Oxide Synthase Isoforms

2000

Publisher Summary There is a large array of regulatory mechanisms for the expression of different nitric oxide synthases (NOS) isoforms. The high-output NOS II is not only turned on transcriptionally, but the stability of the transcripts and their translation can be regulated dynamically. In addition, the expressional levels of the servoregulatory, low-output enzymes, NOS I and NOS III, can also be adjusted to meet local demand. The original paradigm that nitrogen oxide (NO) is synthesized either by constitutive NO synthases or by inducible NOS II is no longer valid. This adds to the diversity of mechanisms controlling NO production in different cells and tissues. Whereas transcriptional re…

Nitric oxide synthase isozymes antibodies

1995

Three isozymes of nitric oxide synthase (NOS) have been identified, cDNAs isolated and sequenced, and antibodies produced against each isozyme. Isozyme I (found primarily in central and peripheral neuronal cells), II (in cytokine-induced cells), and III (in endothelial cells) show less than 58% identity in the deduced amino acid sequences from humans. Many investigators have produced isozyme-specific antibodies and used these antibodies to locate these proteins in various cells and tissues. NOS-I is constitutively expressed, and the enzymatic activity is regulated by Ca2+ and calmodulin. The anti-NOS-I antibodies have allowed investigators to characterize non-adrenergic non-cholinergic neur…

Prenatal low-level exposure to CO alters postnatal development of hippocampal nitric oxide synthase and haem-oxygenase activities in rats.

2001

The effects of prenatal CO exposure (150 ppm from days 0 to 20 of pregnancy) on the postnatal development of hippocampal neuronal NO synthase (nNOS) and haem-oxygenase (HO-2) isoform activities in 15-, 30- and 90-d-old rats were investigated. Unlike HO-2, hippocampal nNOS activity increased from postnatal days 15-90 in controls. Prenatal CO produced a long-lasting decrease in either nNOS or HO-2. The results suggest that the altered developmental profile of hippocampal nNOS and HO-2 activities could be involved in cognitive deficits and long-term potentiation dysfunction exhibited by rats prenatally exposed to CO levels resulting in carboxyhaemoglobin (HbCO) levels equivalent to those obser…