Abstract
The SNARE hypothesis proposes that specificity of exocytosis is regulated by the appropriate interactions between the vesicle (v-) SNARE and the target membrane (t-) SNAREs. We show here that pancreatic acinar cells express the SNAP-25 t-SNARE homolog SNAP-23, and find that this t-SNARE is most highly concentrated on the basolateral plasma membrane while being expressed below detectable levels in endocrine islets within the same tissue. This is the first localization of SNAP-23 within a polarized tissue and suggests that this t-SNAREs may interact with syntaxin-4 to mediate basolateral secretion.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3 Cells
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Animals
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Carrier Proteins / analysis*
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Carrier Proteins / metabolism
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Cell Fractionation
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Cell Membrane / chemistry
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Cell Membrane / metabolism
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Cell Membrane / ultrastructure*
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Cytoplasmic Granules / chemistry
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Cytoplasmic Granules / ultrastructure
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Diabetes Mellitus, Experimental / metabolism
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Intracellular Membranes / chemistry
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Intracellular Membranes / ultrastructure
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Mice
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Microscopy, Confocal
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Pancreas / chemistry*
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Pancreas / cytology*
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Pancreas / metabolism
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Qb-SNARE Proteins
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Qc-SNARE Proteins
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Rats
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Rats, Sprague-Dawley
Substances
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Carrier Proteins
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Qb-SNARE Proteins
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Qc-SNARE Proteins
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SNAP23 protein, human
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Snap23 protein, mouse