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Vesicle-associated membrane protein (VAMP), also known as synaptobrevin, is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle (2). VAMP consists of a proline-rich amino-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a carboxylterminal tail (3). Two VAMP homologs, VAMP1 and VAMP2, are differentially expressed in the nervous system (3). VAMP1 expression is localized to neurons involved in modulating overlapping patterns, whereas VAMP2 is found in neurons ssociated with autonomic, sensory and integrative functions. In non-neuronal tissues, VAMP1 is restricted to pancreas and kidney tubular cells, whereas VAMP2 is predominantly expressed in Langerhans islets and glomerular cells (4). Evidences for VAMP