Molecular cloning and expression of a cDNA encoding endothelial cell nitric oxide synthase.

Sessa, William C.; Harrison, Jeffrey K.; Barber, Cynthia M.; Zeng, Dewan; Durieux, Marcel E.; D'Angelo, Drew D.; Lynch, Kevin R.; Peach, Michael J.

doi:10.1016/s0021-9258(19)49528-8

Cited by 436 publications

(32 citation statements)

References 34 publications

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“…NADPH-d reactivity in vessels of uninflamed pulp was consistent with that in other tissues. Molecular cloning has been used to demonstrate a constitutive isoform of NOS in endothelium (Janssens et al, 1992;Lamas et al, 1992;Sessa et al, 1992), and NADPH-d activity has been shown to be distributed in blood vessels in rat brain vasculature (Poeggel et al, 1992;Gabbott and Bacon, 1993). In blood vessels, NO is believed to cause vasodilatation by increasing binding to the L V-i, (Ignarro et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Localization and Changes in NADPH-Diaphorase Reactivity and Nitric Oxide Synthase Immunoreactivity in Rat Pulp Following Tooth Preparation

et al. 1999

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Inflammatory changes in the dental pulp are accompanied by release of a wide variety of chemical mediators. Nitric oxide, an oxidative free radical produced by the enzyme nitric oxide synthase (NOS), has been implicated in multiple inflammatory processes, which makes it a suitable marker for changes which likely occur following tooth pulp insult. Since limited information on nitric oxide in the pulp is available, it is necessary first to examine relative distributions of NOS in uninflamed and inflamed rat pulp. We accomplished this by characterizing regions of nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-d) activity and the distribution of both macrophage NOS (macNOS) and neuronal NOS (nNOS) immunoreactivity in normal and inflamed rat molar pulp at multiple time points. The results showed that: (1) deep cavity preparation on the mesial surface of the molar produced a time-dependent inflammation, with acute inflammation early progressing to chronic, granulomatous inflammation with necrosis later that spread preferentially down the mesial root; (2) control (non-prepared) teeth showed a relatively faint and homogeneous distribution of NADPH-d and macNOS reactivity but no discernible nNOS reactivity; (3) inflamed teeth displayed localized increased intensity of NADPH-d and macNOS reactivity surrounding the inflamed area of pulp, but no increased nNOS activity; (4) pulp vessels supplying the inflamed area showed increased NADPH-d reactivity, but no increased macNOS or nNOS reactivity; and (5) neither NADPH-d, macNOS, nor nNOS reactivity was observed in pulpal nerves. Therefore, nitric oxide may mediate the pulpal inflammatory response through its effects on the paralesional pulp tissue and surrounding endothelial/vascular structures.

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Section: Discussionmentioning

confidence: 99%

Localization and Changes in NADPH-Diaphorase Reactivity and Nitric Oxide Synthase Immunoreactivity in Rat Pulp Following Tooth Preparation

et al. 1999

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“…Therefore, eNOS needs to be tightly regulated (for reviews on eNOS regulation see Govers and Rabelink 2001). Proteins that activate eNOS are calmodulin (Sessa et al 1992), Hsp90 (Garcia-Cardena et al 1998, Akt kinase (Dimmeler et al 1999), and dy-namin-2 (Cao et al 2000). The negative regulators known thus far are caveolin-1 and NOSIP (Dedio et al 2001).…”

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confidence: 99%

Endothelial Nitric Oxide Synthase and Its Negative Regulator Caveolin-1 Localize to Distinct Perinuclear Organelles

Govers

Sluijs

Donselaar

et al. 2002

J Histochem Cytochem.

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S U M M A R YCaveolin-1 is a member of a subset of intracellular proteins that regulate endothelial nitric oxide synthase (eNOS) activity. In caveolae, caveolin-1 inhibits eNOS activity via a direct interaction with the enzyme. Previous work has indicated that both eNOS and caveolin-1 are also localized at the perinuclear Golgi complex. Whether caveolin-1 is involved in eNOS regulation in this cell compartment is unknown. Here we studied the localization of eNOS and caveolin-1 in the perinuclear region of primary bovine aortic endothelial cells. By immunofluorescence microscopy we show that both eNOS and caveolin-1 co-localize with Golgi markers. On treatment of the cells with the microtubule-depolymerizing drug nocodazole, the Golgi complex is scattered and caveolin-1 is found in vesicles at the periphery of the cell, while eNOS is localized at large structures near the nucleus. The nocodazole-induced redistribution of eNOS is similar to that of cis -, medial-, and transGolgi markers, while the caveolin-1 redistribution resembles that of sec22, a marker for the intermediate compartment. The localization of eNOS and caveolin-1 at distinct perinuclear compartments that behave differently in the presence of nocodazole indicates that eNOS activity is not regulated by caveolin-1 in the Golgi complex.

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“…ent protein molecular weights: eNOS, 135 kD (Sessa et al 1992); iNOS, 130-135 kD (Xie et al 1992;Sessa 1994); and nNOS, 160 kD (Sessa 1994;Lopez-Figueroa et al 1996). Generation of NO from l -arginine requires, in addition, NOS cofactors: NADPH, flavin mononucleotide (FMN), and flavin adenine dinucleotide (FAD; Knowles and Moncada 1994).…”

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confidence: 99%

Distribution of NADPH-diaphorase and Nitric Oxide Synthase (NOS) in Different Regions of Porcine Oviduct During the Estrous Cycle

Gawrońska

Bodek

Ziȩcik

2000

J Histochem Cytochem.

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S U M M A R YNitric oxide synthase (NOS) is responsible for the biological production of nitric oxide (NO) in several organs, including those of the reproductive tract. We investigated potential changes in NADPH-diaphorase (NADPH-d) activity (marker for NOS activity) and the presence and distribution of NOS in the porcine oviduct. Tissues were obtained from gilts ( n ϭ 16) on different days of the estrous cycle. One fallopian tube was used for histoand immunohistochemistry and the other for Western blotting analysis. NADPH-d activity was much higher in the epithelium of the mucosa than in the myosalpinx. The highest activity of NADPH-d was always found in the epithelium of the isthmus. The intensity of the reaction (arbitrary units Ϯ SEM) in isthmus epithelium increased from the postovulatory period until early proestrus (96.2 Ϯ 11.2) and then gradually decreased. The lowest intensity of NADPH-d reaction in the epithelium of the isthmus was seen at estrus (58.4 Ϯ 7.7). The most intense NADPH-d activity in myosalpinx of all parts of the oviduct was observed at the postovulatory stage of the estrous cycle (isthmus 38.3 Ϯ 2.5; ampulla 35.6 Ϯ 4.2; infundibulum 24.7 Ϯ 0.8) and then decreased during the remaining stages of the estrous cycle ( p Ͻ 0.001). The presence of endothelial NOS (eNOS) was detected in epithelial cells of mucosa and in endothelium of vascular tissues and myosalpinx during all studied days of the estrous cycle. The positive reaction for inducible NOS (iNOS) was restricted only to the endothelium of lymph vessels and some blood vessels. Because our Western blotting analysis revealed that porcine oviduct contains eNOS but not iNOS, we suggest that eNOS is the main isoform of NOS expressed in the porcine oviduct. We concluded that the different activity of NADPH-d in the various regions of the oviduct, accompanied by changes in its activity during the course of the estrous cycle, could indicate an important role of NO in regulation of tubal function.

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Molecular cloning and expression of a cDNA encoding endothelial cell nitric oxide synthase.

Cited by 436 publications

References 34 publications

Localization and Changes in NADPH-Diaphorase Reactivity and Nitric Oxide Synthase Immunoreactivity in Rat Pulp Following Tooth Preparation

Localization and Changes in NADPH-Diaphorase Reactivity and Nitric Oxide Synthase Immunoreactivity in Rat Pulp Following Tooth Preparation

Endothelial Nitric Oxide Synthase and Its Negative Regulator Caveolin-1 Localize to Distinct Perinuclear Organelles

Distribution of NADPH-diaphorase and Nitric Oxide Synthase (NOS) in Different Regions of Porcine Oviduct During the Estrous Cycle

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