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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1997-7-1
|
| pubmed:abstractText |
To determine the functional role of synaptotagmin (Syt) regulatory domains, affinity-purified antibodies specific for C2A or C2B domains were injected into presynaptic neurons of cholinergic synapses formed between rat sympathetic neurons in culture. Following injection of anti-C2A antibody, postsynaptic responses evoked by presynaptic action potentials at a frequency of 0.05 Hz decreased rapidly, while anti-C2B antibody slowly decreased synaptic transmitter release. The inhibitory effect of anti-C2B antibody depended on the amount of synaptic activity. Asynchronous release induced by hypertonic solution was also affected by the antibodies. Anti-C2A antibody showed a dual action on miniature excitatory postsynaptic potentials, a decrease and following increase in the frequency, while synapses loaded with anti-C2B antibody showed a decrease in the frequency after long repetitive stimulation (0.05 Hz for more than 60 min). Anti-C2B antibody prevented the inhibition of acetylcholine release induced by injection of inositol 1,3,4,5-tetrakisphosphate (IP4), indicating that C2B domain may down-regulate transmitter release by IP4 binding. These results confirm similar experiments in the glutamatergic squid giant synapses and suggest a model in which Syt C2A and C2B domains differentially control synaptic vesicle trafficking in mammalian cholinergic terminals; C2A domain may act on the fusion step as a calcium sensor in synaptic vesicle exocytosis evoked by action potentials in addition to controlling spontaneous transmitter release, while C2B domain is involved in exo- and endocytosis.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phytic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins,
http://linkedlifedata.com/resource/pubmed/chemical/inositol pentaphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/inositol-1,3,4,5-tetrakisphosphate
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0306-4522
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
77
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
937-43
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9130775-Acetylcholine,
pubmed-meshheading:9130775-Animals,
pubmed-meshheading:9130775-Antibody Specificity,
pubmed-meshheading:9130775-Calcium-Binding Proteins,
pubmed-meshheading:9130775-Cells, Cultured,
pubmed-meshheading:9130775-Cholinergic Fibers,
pubmed-meshheading:9130775-Electrophysiology,
pubmed-meshheading:9130775-Immunoblotting,
pubmed-meshheading:9130775-Inositol Phosphates,
pubmed-meshheading:9130775-Membrane Glycoproteins,
pubmed-meshheading:9130775-Membrane Potentials,
pubmed-meshheading:9130775-Nerve Tissue Proteins,
pubmed-meshheading:9130775-Neurons,
pubmed-meshheading:9130775-Phytic Acid,
pubmed-meshheading:9130775-Protein Structure, Tertiary,
pubmed-meshheading:9130775-Rats,
pubmed-meshheading:9130775-Synapses,
pubmed-meshheading:9130775-Synaptotagmins
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Roles of synaptotagmin C2 domains in neurotransmitter secretion and inositol high-polyphosphate binding at mammalian cholinergic synapses.
|
| pubmed:affiliation |
Department of Physiology, Tokyo Medical College, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|