Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1994-3-22
pubmed:abstractText
Zymogen granules of the exocrine pancreas are the secretory organelles responsible for the regulated secretion of digestive enzymes. Several proteins are associated with or are integral components of the lipid bilayer that forms the zymogen granule membrane. These proteins likely represent important components in the regulated secretion of digestive enzymes. VAMPs (vesicle-associated membrane proteins)/synaptobrevins are a family of 18-kDa integral membrane proteins originally characterized in synaptic vesicles. Polyclonal antisera raised against either a VAMP/glutathione S-transferase (GST) fusion protein or rat brain synaptic vesicles, detected an 18-kDa immunoreactive protein in zymogen granule membranes that co-migrates electrophorectically with rat brain synaptic vesicle VAMP. Rat brain synaptic vesicle VAMP was detected by both antisera. Botulinum-B toxin treatment of zymogen granule membranes did not result in cleavage of zymogen granule membrane VAMP, indicating that exocrine pancreatic VAMP is either VAMP1 or a novel VAMP-isoform. Immunofluorescent studies demonstrated that exocrine pancreatic VAMP localized with GP2, a zymogen granule membrane protein, to the apical region of pancreatic acinar cells. No significant labeling was observed in basolateral regions of pancreatic acinar cells. These results establish the presence of a VAMP protein in the zymogen granule of the rat pancreas and suggest that VAMPs have a role in exocrine secretion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5328-35
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8106518-Animals, pubmed-meshheading:8106518-Brain, pubmed-meshheading:8106518-Cytoplasmic Granules, pubmed-meshheading:8106518-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8106518-Endopeptidases, pubmed-meshheading:8106518-Enzyme Precursors, pubmed-meshheading:8106518-Fluorescent Antibody Technique, pubmed-meshheading:8106518-Immunohistochemistry, pubmed-meshheading:8106518-Intracellular Membranes, pubmed-meshheading:8106518-Islets of Langerhans, pubmed-meshheading:8106518-Male, pubmed-meshheading:8106518-Membrane Proteins, pubmed-meshheading:8106518-Molecular Weight, pubmed-meshheading:8106518-Nerve Tissue Proteins, pubmed-meshheading:8106518-Pancreas, pubmed-meshheading:8106518-Peptide Fragments, pubmed-meshheading:8106518-R-SNARE Proteins, pubmed-meshheading:8106518-Rats, pubmed-meshheading:8106518-Rats, Sprague-Dawley, pubmed-meshheading:8106518-Synaptic Vesicles
pubmed:year
1994
pubmed:articleTitle
Identification of a vesicle-associated membrane protein (VAMP)-like membrane protein in zymogen granules of the rat exocrine pancreas.
pubmed:affiliation
Department of Medicine, Stanford University, California 94305-5487.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.