Distinct regional expression of SNARE proteins in the feline oesophagus

Soluble N‐ethylmaleimide‐sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown to also bind and regulate a number of membrane ion channels in neurones and neuroendocrine cells. We recently reported that the SNARE protein SNAP‐25 regu...

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Published inNeurogastroenterology and motility Vol. 14; no. 4; pp. 383 - 394
Main Authors Ji, J., Lau, H., Sheu, L., Diamant, N. E., Gaisano, H. Y.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Science Ltd 01.08.2002
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Abstract Soluble N‐ethylmaleimide‐sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown to also bind and regulate a number of membrane ion channels in neurones and neuroendocrine cells. We recently reported that the SNARE protein SNAP‐25 regulates Ca2+‐ activated (KCa) and delays rectifier K+channels (KV) in oesophageal smooth muscle cells. This raised the possibility that cognate and other SNARE proteins could also be present in the oesophageal smooth muscle cell to regulate these and other functions. Circular muscle tissue sections and single freshly isolated muscle cells from the oesophageal body circular and longitudinal layers, and from lower oesophageal sphincter clasp and sling regions were studied. The subcellular location of SNAP‐23, SNAP‐25, syntaxins 1 to 4, and vesicle‐associated membrane protein (VAMP)‐2 were explored using a laser scanning confocal imaging system. Feline oesophageal smooth muscle of all regions examined demonstrated the presence of SNAP‐23, SNAP‐25, syntaxins 1 to 4, and VAMP‐2 on the plasma membrane. The intensity of these syntaxins and SNAP‐25/‐23 proteins varied between the different muscle groups of the oesophagus. In some regions, some SNARE proteins were also noted in the muscle cell cytoplasm. No differential expression was found for VAMP‐2. The differential expression of SNAP‐25 and its regulation of K+channels indicate the important role of SNAP‐25 in regulating the distinct membrane excitability and contractility along the smooth muscle of the oesophagus. This is further contributed by its interactions with the cognate syntaxins, which are also differentially expressed in the muscle groups of the oesophageal body and lower oesophageal sphincter (LOS). These SNARE proteins probably have other functions in the smooth muscle cell, such as regulating vesicular transport processes.
AbstractList Abstract Soluble N-ethylmaleimide-sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown to also bind and regulate a number of membrane ion channels in neurones and neuroendocrine cells. We recently reported that the SNARE protein SNAP-25 regulates Ca(2+)- activated (K(Ca)) and delays rectifier K(+) channels (K(V)) in oesophageal smooth muscle cells. This raised the possibility that cognate and other SNARE proteins could also be present in the oesophageal smooth muscle cell to regulate these and other functions. Circular muscle tissue sections and single freshly isolated muscle cells from the oesophageal body circular and longitudinal layers, and from lower oesophageal sphincter clasp and sling regions were studied. The subcellular location of SNAP-23, SNAP-25, syntaxins 1 to 4, and vesicle-associated membrane protein (VAMP)-2 were explored using a laser scanning confocal imaging system. Feline oesophageal smooth muscle of all regions examined demonstrated the presence of SNAP-23, SNAP-25, syntaxins 1 to 4, and VAMP-2 on the plasma membrane. The intensity of these syntaxins and SNAP-25/-23 proteins varied between the different muscle groups of the oesophagus. In some regions, some SNARE proteins were also noted in the muscle cell cytoplasm. No differential expression was found for VAMP-2. The differential expression of SNAP-25 and its regulation of K(+) channels indicate the important role of SNAP-25 in regulating the distinct membrane excitability and contractility along the smooth muscle of the oesophagus. This is further contributed by its interactions with the cognate syntaxins, which are also differentially expressed in the muscle groups of the oesophageal body and lower oesophageal sphincter (LOS). These SNARE proteins probably have other functions in the smooth muscle cell, such as regulating vesicular transport processes.
Abstract   Soluble N ‐ ethylmaleimide‐sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown to also bind and regulate a number of membrane ion channels in neurones and neuroendocrine cells. We recently reported that the SNARE protein SNAP‐25 regulates Ca 2+ ‐ activated (K Ca ) and delays rectifier K + channels (K V ) in oesophageal smooth muscle cells. This raised the possibility that cognate and other SNARE proteins could also be present in the oesophageal smooth muscle cell to regulate these and other functions. Circular muscle tissue sections and single freshly isolated muscle cells from the oesophageal body circular and longitudinal layers, and from lower oesophageal sphincter clasp and sling regions were studied. The subcellular location of SNAP‐23, SNAP‐25, syntaxins 1 to 4, and vesicle‐associated membrane protein (VAMP)‐2 were explored using a laser scanning confocal imaging system. Feline oesophageal smooth muscle of all regions examined demonstrated the presence of SNAP‐23, SNAP‐25, syntaxins 1 to 4, and VAMP‐2 on the plasma membrane. The intensity of these syntaxins and SNAP‐25/‐23 proteins varied between the different muscle groups of the oesophagus. In some regions, some SNARE proteins were also noted in the muscle cell cytoplasm. No differential expression was found for VAMP‐2. The differential expression of SNAP‐25 and its regulation of K + channels indicate the important role of SNAP‐25 in regulating the distinct membrane excitability and contractility along the smooth muscle of the oesophagus. This is further contributed by its interactions with the cognate syntaxins, which are also differentially expressed in the muscle groups of the oesophageal body and lower oesophageal sphincter (LOS). These SNARE proteins probably have other functions in the smooth muscle cell, such as regulating vesicular transport processes.
Soluble N‐ethylmaleimide‐sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown to also bind and regulate a number of membrane ion channels in neurones and neuroendocrine cells. We recently reported that the SNARE protein SNAP‐25 regulates Ca2+‐ activated (KCa) and delays rectifier K+channels (KV) in oesophageal smooth muscle cells. This raised the possibility that cognate and other SNARE proteins could also be present in the oesophageal smooth muscle cell to regulate these and other functions. Circular muscle tissue sections and single freshly isolated muscle cells from the oesophageal body circular and longitudinal layers, and from lower oesophageal sphincter clasp and sling regions were studied. The subcellular location of SNAP‐23, SNAP‐25, syntaxins 1 to 4, and vesicle‐associated membrane protein (VAMP)‐2 were explored using a laser scanning confocal imaging system. Feline oesophageal smooth muscle of all regions examined demonstrated the presence of SNAP‐23, SNAP‐25, syntaxins 1 to 4, and VAMP‐2 on the plasma membrane. The intensity of these syntaxins and SNAP‐25/‐23 proteins varied between the different muscle groups of the oesophagus. In some regions, some SNARE proteins were also noted in the muscle cell cytoplasm. No differential expression was found for VAMP‐2. The differential expression of SNAP‐25 and its regulation of K+channels indicate the important role of SNAP‐25 in regulating the distinct membrane excitability and contractility along the smooth muscle of the oesophagus. This is further contributed by its interactions with the cognate syntaxins, which are also differentially expressed in the muscle groups of the oesophageal body and lower oesophageal sphincter (LOS). These SNARE proteins probably have other functions in the smooth muscle cell, such as regulating vesicular transport processes.
Author Sheu, L.
Ji, J.
Gaisano, H. Y.
Lau, H.
Diamant, N. E.
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Notes Part of this work was presented at the American Gastroenterology Association Meeting in 1998.
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Snippet Soluble N‐ethylmaleimide‐sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown to also bind...
Abstract Soluble N-ethylmaleimide-sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown to...
Abstract   Soluble N ‐ ethylmaleimide‐sensitive factors attachment protein receptors (SNAREs), initially found to mediate membrane fusion, have now been shown...
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wiley
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StartPage 383
SubjectTerms Animals
Carrier Proteins - metabolism
Cats
confocal microscopy
Esophagus - cytology
Esophagus - metabolism
Female
Male
Membrane Proteins - biosynthesis
Membrane Proteins - metabolism
Mice
Muscle, Smooth - cytology
Muscle, Smooth - metabolism
Nerve Tissue Proteins - metabolism
oesophagus
Qb-SNARE Proteins
Qc-SNARE Proteins
R-SNARE Proteins
smooth muscle cells
SNARE Proteins
SNAREs
Subcellular Fractions - metabolism
Synaptosomal-Associated Protein 25
Vesicular Transport Proteins
Title Distinct regional expression of SNARE proteins in the feline oesophagus
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https://www.ncbi.nlm.nih.gov/pubmed/12213106
https://search.proquest.com/docview/72065559
Volume 14
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