Abstract
The exocytosis of salivary proteins is mainly regulated by cAMP, although soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), which mediate cAMP-dependent exocytic membrane fusion, have remained unidentified. Here we examined the effect of isoproterenol (ISO) and cytochalasin D (CyD) on the level of SNARE complexes in rat parotid glands. When SNARE complexes were immunoprecipitated by anti-SNAP23, the coprecipitation of VAMP2 was significantly increased in response to ISO and/or CyD, although the coprecipitation of VAMP8 or syntaxin 4 was scarcely augmented. These results suggest that the SNAP23-VAMP2 interaction plays a key role in cAMP-mediated exocytosis from parotid glands.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adrenergic beta-Agonists / pharmacology*
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Animals
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Cyclic AMP / metabolism*
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Cytochalasin D / pharmacology
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Dithiothreitol
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Ethylmaleimide
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Exocytosis / drug effects
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Exocytosis / physiology
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Gene Expression Regulation / drug effects
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Immunoprecipitation
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Isoproterenol / pharmacology*
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Male
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Nucleic Acid Synthesis Inhibitors / pharmacology
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Parotid Gland / drug effects*
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Parotid Gland / physiology
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Protein Binding
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Qa-SNARE Proteins / genetics
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Qa-SNARE Proteins / metabolism
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Rats
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Rats, Wistar
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Signal Transduction / drug effects
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Tissue Culture Techniques
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Vesicle-Associated Membrane Protein 2 / genetics
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Vesicle-Associated Membrane Protein 2 / metabolism*
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Vesicular Transport Proteins / genetics
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Vesicular Transport Proteins / metabolism*
Substances
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Adrenergic beta-Agonists
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Nucleic Acid Synthesis Inhibitors
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Qa-SNARE Proteins
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Snap23 protein, rat
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Vamp2 protein, rat
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Vesicle-Associated Membrane Protein 2
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Vesicular Transport Proteins
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Cytochalasin D
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Cyclic AMP
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Isoproterenol
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Ethylmaleimide
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Dithiothreitol