rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
24
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pubmed:dateCreated |
1996-8-20
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pubmed:abstractText |
Protein kinase C-mediated phosphorylation of a 25-kDa synaptosome-associated protein (SNAP-25) was examined in living PC12 cells. Phorbol 12-myristate 13-acetate treatment enhanced high potassium-induced [3H]-norepinephrine release, and a 28-kDa protein recognized by an anti-SNAP-25 antibody was phosphorylated on Ser residues. The molecular size of the phosphorylated band decreased slightly following treatment with Clostridium botulinum type A neurotoxin, whereas the band disappeared after treatment with botulinum type E neurotoxin, indicating that the 28-kDa protein was SNAP-25. A phosphorylation is likely to occur at Ser187, as this is the only Ser residue located between the cleavage sites of botulinum type A and E neurotoxins. SNAP-25 of PC12 cells was phosphorylated by purified protein kinase C in vitro, and the amount of syntaxin co-immunoprecipitated with SNAP-25 was decreased by phosphorylation. These results suggest that the phosphorylation of SNAP-25 may be involved in protein kinase C-mediated regulation of catecholamine release from PC12 cells.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Botulinum Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Norepinephrine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Snap25 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptosomal-Associated Protein 25,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14548-53
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8662851-Animals,
pubmed-meshheading:8662851-Antibodies, Monoclonal,
pubmed-meshheading:8662851-Antigens,
pubmed-meshheading:8662851-Botulinum Toxins,
pubmed-meshheading:8662851-Membrane Proteins,
pubmed-meshheading:8662851-Nerve Tissue Proteins,
pubmed-meshheading:8662851-Neurotoxins,
pubmed-meshheading:8662851-Norepinephrine,
pubmed-meshheading:8662851-PC12 Cells,
pubmed-meshheading:8662851-Phosphorylation,
pubmed-meshheading:8662851-Phosphoserine,
pubmed-meshheading:8662851-Potassium,
pubmed-meshheading:8662851-Protein Kinase C,
pubmed-meshheading:8662851-Qa-SNARE Proteins,
pubmed-meshheading:8662851-Rats,
pubmed-meshheading:8662851-SNARE Proteins,
pubmed-meshheading:8662851-Synaptosomal-Associated Protein 25,
pubmed-meshheading:8662851-Tetradecanoylphorbol Acetate,
pubmed-meshheading:8662851-Vesicular Transport Proteins
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pubmed:year |
1996
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pubmed:articleTitle |
Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release.
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pubmed:affiliation |
Mitsubishi Kasei Institute of Life Sciences, Machida, Tokyo 194, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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