| pubmed-article:9130775 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C0039062 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C0084697 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C0021547 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C1511359 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C0598964 | lld:lifeskim |
| pubmed-article:9130775 | lifeskim:mentions | umls-concept:C0599668 | lld:lifeskim |
| pubmed-article:9130775 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9130775 | pubmed:dateCreated | 1997-7-1 | lld:pubmed |
| pubmed-article:9130775 | 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. | lld:pubmed |
| pubmed-article:9130775 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9130775 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9130775 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9130775 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9130775 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9130775 | pubmed:issn | 0306-4522 | lld:pubmed |
| pubmed-article:9130775 | pubmed:author | pubmed-author:KobayashiHH | lld:pubmed |
| pubmed-article:9130775 | pubmed:author | pubmed-author:MikoshibaKK | lld:pubmed |
| pubmed-article:9130775 | pubmed:author | pubmed-author:FukudaMM | lld:pubmed |
| pubmed-article:9130775 | pubmed:author | pubmed-author:NiinobeMM | lld:pubmed |
| pubmed-article:9130775 | pubmed:author | pubmed-author:MochidaSS | lld:pubmed |
| pubmed-article:9130775 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9130775 | pubmed:volume | 77 | lld:pubmed |
| pubmed-article:9130775 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9130775 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9130775 | pubmed:pagination | 937-43 | lld:pubmed |
| pubmed-article:9130775 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9130775 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9130775 | pubmed:articleTitle | Roles of synaptotagmin C2 domains in neurotransmitter secretion and inositol high-polyphosphate binding at mammalian cholinergic synapses. | lld:pubmed |
| pubmed-article:9130775 | pubmed:affiliation | Department of Physiology, Tokyo Medical College, Japan. | lld:pubmed |
| pubmed-article:9130775 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9130775 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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