Transient expression of neuronal nitric oxide synthase by neurons of the submucous plexus of the mouse small intestine

1998 ◽  
Vol 291 (3) ◽  
pp. 395-401 ◽  
Author(s):  
H. M. Young ◽  
D. Ciampoli
Keyword(s):  
Nitric Oxide ◽  
Small Intestine ◽  
Nitric Oxide Synthase ◽  
Transient Expression ◽  
Neuronal Nitric Oxide Synthase ◽  
Submucous Plexus ◽  
Mouse Small Intestine ◽  
Oxide Synthase

Phenotypic characterization of taste cells of the mouse small intestine

2007 ◽  
Vol 292 (5) ◽  
pp. G1420-G1428 ◽  
Author(s):  
Kate Sutherland ◽  
Richard L. Young ◽  
Nicole J. Cooper ◽  
Michael Horowitz ◽  
L. Ashley Blackshaw
Keyword(s):  
Nitric Oxide ◽  
Small Intestine ◽  
Nitric Oxide Synthase ◽  
Epithelial Cells ◽  
Neuronal Nitric Oxide Synthase ◽  
Enteroendocrine Cells ◽  
Brush Cells ◽  
Cell Markers ◽  
Mouse Small Intestine ◽  
Oxide Synthase

Nutrient-evoked gastrointestinal reflexes are likely initiated by specialized epithelial cells located in the small intestine that detect luminal stimuli and release mediators that activate vagal endings. The G-protein α-gustducin, a key signal molecule in lingual taste detection, has been identified in mouse small intestine, where it may also subserve nutrient detection; however, the phenotype of α-gustducin cells is unknown. Immunohistochemistry was performed throughout the mouse small intestine for α-gustducin, enteroendocrine cell markers 5-HT and glucagon-like peptide-1 (GLP-1), and brush cell markers neuronal nitric oxide synthase and Ulex europaeus agglutinin-1 (UEA-1) lectin binding, singly, and in combination. α-Gustducin was expressed in solitary epithelial cells of the mid to upper villus, which were distributed in a regional manner with most occurring within the midjejunum. Here, 27% of α-gustducin cells colabeled for 5-HT and 15% for GLP-1; 57% of α-gustducin cells colabeled UEA-1, with no triple labeling. α-Gustducin cells that colabeled for 5-HT or GLP-1 were of distinct morphology and exhibited a different α-gustducin immunolabeling pattern to those colabeled with UEA-1. Neuronal nitric oxide synthase was absent from intestinal epithelium despite strong labeling in the myenteric plexus. We conclude that subsets of enteroendocrine cells in the midjejunum and brush cells (more generally distributed) are equipped to utilize α-gustducin signaling in mice. Intestinal taste modalities may be signaled by these enteroendocrine cells via the release of 5-HT, GLP-1, or coexpressed mediators or by brush cells via a nonnitrergic mediator in distinct regions of the intestine.

Smooth muscle nitric oxide synthase, co‐localized with caveolin‐1, modulates contraction in mouse small intestine

2007 ◽  
Vol 21 (6) ◽  
Author(s):  
Ahmed El‐Yazbi ◽  
Woo Jung Cho ◽  
Johnathan Cena ◽  
Richard Schulz ◽  
Edwin Daniel
Keyword(s):  
Nitric Oxide ◽  
Smooth Muscle ◽  
Small Intestine ◽  
Nitric Oxide Synthase ◽  
Caveolin 1 ◽  
Mouse Small Intestine ◽  
Oxide Synthase

Characterization and splice variants of neuronal nitric oxide synthase in rat small intestine

1998 ◽  
Vol 275 (5) ◽  
pp. G1146-G1156 ◽  
Author(s):  
Andrea Huber ◽  
Dieter Saur ◽  
Manfred Kurjak ◽  
Volker Schusdziarra ◽  
Hans-Dieter Allescher
Keyword(s):  
Nitric Oxide ◽  
Small Intestine ◽  
Nitric Oxide Synthase ◽  
Splice Variants ◽  
Neuronal Nitric Oxide Synthase ◽  
Membrane Association ◽  
Nerve Terminals ◽  
Rat Small Intestine ◽  
Longitudinal Muscle Layer ◽  
Oxide Synthase

The aim of this study was to characterize neuronal nitric oxide synthase (nNOS) activity and 5′-end splice variants in rat small intestine. nNOS was predominantly expressed in the longitudinal muscle layer, with attached myenteric plexus (LM-MP). The biochemical properties of NOS activity in enriched nerve terminals resemble those of nNOS isolated from the brain. Western blot analysis of purified NOS protein with an nNOS antibody showed a single band in the particulate fraction and three bands in the soluble fraction. Rapid amplification of 5′ cDNA ends-PCR revealed the presence of three different 5′-end splice variants of nNOS. Two variants encode for nNOSα, which has a specific domain for membrane association. The third variant encodes for nNOSβ, which lacks the domain for membrane association and should therefore be soluble. nNOS is predominantly expressed in LM-MP and can be enriched in enteric nerve terminals. We present the first evidence that three 5′-end splice variants of nNOS encoding two different proteins are expressed in rat small intestine. These two nNOS enzymes exhibit different subcellular locations and might be implicated in different biological functions.

Further characterisation of particulate neuronal nitric oxide synthase in rat small intestine

2004 ◽  
Vol 110 (1) ◽  
pp. 8-18 ◽  
Author(s):  
Lieve A Van Geldre ◽  
Norbert H Fraeyman ◽  
Theo L Peeters ◽  
Jean-Pierre Timmermans ◽  
Romain A Lefebvre
Keyword(s):  
Nitric Oxide ◽  
Small Intestine ◽  
Nitric Oxide Synthase ◽  
Neuronal Nitric Oxide Synthase ◽  
Rat Small Intestine ◽  
Oxide Synthase
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