| pubmed-article:10594896 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10594896 | lifeskim:mentions | umls-concept:C0027934 | lld:lifeskim |
| pubmed-article:10594896 | lifeskim:mentions | umls-concept:C1420270 | lld:lifeskim |
| pubmed-article:10594896 | lifeskim:mentions | umls-concept:C1817242 | lld:lifeskim |
| pubmed-article:10594896 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:10594896 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:10594896 | pubmed:dateCreated | 2000-3-21 | lld:pubmed |
| pubmed-article:10594896 | pubmed:abstractText | The vesicular neuroexocytosis process consists of two important steps: fusion of transmitter-loaded vesicles at release sites on the presynaptic nerve terminal membrane; followed by the release of transmitter molecules into the synaptic cleft. We previously reported that in nerve growth factor (NGF)-differentiated PC12 cells, arachidonic acid (AA) release is associated with acetylcholine (ACh) release, botulinum neurotoxin A (BoNT/A) inhibits both processes and AA itself or a phospholipase A(2) (PLA(2)) activator can cause ACh release in BoNT/A-poisoned cells in which SNAP-25 has supposedly been hydrolyzed. In the present study, we examined the roles of two endogenous intraterminal components in neuroexocytosis: the membrane fusogenic agent AA; and the vesicle fusion protein SNAP-25. A PLA(2) activator, mastoparan, was used to induce the release of AA and ACh from NGF-differentiated PC12 cells. Release depended upon the mastoparan concentration, as well as Ca(2+) influx via the neuronal-type voltage-sensitive Ca(2+) channels. Release of ACh followed a rise in intracellular free Ca(2+) concentration; the increased Ca(2+) activated PLA(2) and, thereby, increased the AA level. Scanning and transmission electron microscopy confirmed that mastoparan-induced ACh and AA release were not due to simple diffusion through damaged plasma membranes. Treatment of PC12 cells with appropriate antisense oligonucleotides blocked SNAP-25 expression, as judged by Western blot protein analysis with a specific monoclonal antibody. Despite apparent elimination of SNAP-25, treatment of differentiated PC12 cells with mastoparan and high (80 mM) K(+) induced ACh exocytosis. The results support the conclusion that PLA(2) and AA have important roles in neuroexocytosis that are independent of SNAP-25. Both PLA(2) and AA have been shown to be involved in actin cytoskeletal organization related to vesicle fusion and exocytosis. This mechanism may be an alternative target of BoNT/A other than SNAP-25. | lld:pubmed |
| pubmed-article:10594896 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10594896 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594896 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10594896 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:10594896 | pubmed:issn | 0260-437X | lld:pubmed |
| pubmed-article:10594896 | pubmed:author | pubmed-author:IshidaHH | lld:pubmed |
| pubmed-article:10594896 | pubmed:author | pubmed-author:RazSS | lld:pubmed |
| pubmed-article:10594896 | pubmed:author | pubmed-author:PetraliJ PJP | lld:pubmed |
| pubmed-article:10594896 | pubmed:author | pubmed-author:RayPP | lld:pubmed |
| pubmed-article:10594896 | pubmed:author | pubmed-author:MillardC BCB | lld:pubmed |
| pubmed-article:10594896 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10594896 | pubmed:volume | 19 Suppl 1 | lld:pubmed |
| pubmed-article:10594896 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10594896 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10594896 | pubmed:pagination | S27-8 | lld:pubmed |
| pubmed-article:10594896 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:10594896 | pubmed:meshHeading | pubmed-meshheading:10594896... | lld:pubmed |
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| pubmed-article:10594896 | pubmed:meshHeading | pubmed-meshheading:10594896... | lld:pubmed |
| pubmed-article:10594896 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10594896 | pubmed:articleTitle | Phospholipaise A2 and arachidonic acid-mediated mechanism of neuroexocytosis: a possible target of botidinum neurotoxin A other then SNAP-25. | lld:pubmed |
| pubmed-article:10594896 | pubmed:affiliation | Biology Department, Division of Experimental Therapeutics, Walter Reed Army Institute of Research, Washington, DC 20307-5100, USA. ray@wrsmtp-ccmail.army.mil | lld:pubmed |
| pubmed-article:10594896 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10594896 | lld:pubmed |
