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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0027895,
umls-concept:C0030685,
umls-concept:C0033634,
umls-concept:C0035820,
umls-concept:C0039067,
umls-concept:C0068563,
umls-concept:C0205263,
umls-concept:C0332120,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1414967,
umls-concept:C1710236,
umls-concept:C1963578
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pubmed:issue |
2
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pubmed:dateCreated |
1993-8-24
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pubmed:abstractText |
To study the involvement of the protein kinase C (PKC) substrate B-50 [also known as growth-associated protein-43 (GAP-43), neuromodulin, and F1] in presynaptic cholecystokinin-8 (CCK-8) release, highly purified synaptosomes from rat cerebral cortex were permeated with the bacterial toxin streptolysin O (SL-O). CCK-8 release from permeated synaptosomes, determined quantitatively by radioimmunoassay, could be induced by Ca2+ in a concentration-dependent manner (EC50 of approximately 10(-5) M). Ca(2+)-induced CCK-8 release was maximal at 10(-4) M Ca2+, amounting to approximately 10% of the initial 6,000 +/- 550 fmol of CCK-8 content/mg of synaptosomal protein. Only 30% of the Ca(2+)-induced CCK-8 release was dependent on the presence of exogenously added ATP. Two different monoclonal anti-B-50 antibodies were introduced into permeated synaptosomes to study their effect on Ca(2+)-induced CCK-8 release. The N-terminally directed antibodies (NM2), which inhibited PKC-mediated B-50 phosphorylation, inhibited Ca(2+)-induced CCK-8 release in a dose-dependent manner, whereas the C-terminally directed antibodies (NM6) affected neither B-50 phosphorylation nor CCK-8 release. The PKC inhibitors PKC19-36 and 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7), which inhibited B-50 phosphorylation in permeated synaptosomes, had no effect on Ca(2+)-induced CCK-8 release. Our data strongly indicate that B-50 is involved in the mechanism of presynaptic CCK-8 release, at a step downstream of the Ca2+ trigger. As CCK-8 is stored in large dense-cored vesicles, we conclude that B-50 is an essential factor in the exocytosis from this type of neuropeptide-containing vesicle.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/GAP-43 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Sincalide
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
602-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8336144-Adenosine Triphosphate,
pubmed-meshheading:8336144-Animals,
pubmed-meshheading:8336144-Antibodies, Monoclonal,
pubmed-meshheading:8336144-Calcium,
pubmed-meshheading:8336144-Cell Fractionation,
pubmed-meshheading:8336144-Centrifugation, Density Gradient,
pubmed-meshheading:8336144-Cerebral Cortex,
pubmed-meshheading:8336144-GAP-43 Protein,
pubmed-meshheading:8336144-Male,
pubmed-meshheading:8336144-Membrane Glycoproteins,
pubmed-meshheading:8336144-Nerve Tissue Proteins,
pubmed-meshheading:8336144-Potassium,
pubmed-meshheading:8336144-Protein Kinase C,
pubmed-meshheading:8336144-Rats,
pubmed-meshheading:8336144-Rats, Wistar,
pubmed-meshheading:8336144-Sincalide,
pubmed-meshheading:8336144-Synaptosomes
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pubmed:year |
1993
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pubmed:articleTitle |
Evidence for a role of protein kinase C substrate B-50 (GAP-43) in Ca(2+)-induced neuropeptide cholecystokinin-8 release from permeated synaptosomes.
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pubmed:affiliation |
Division of Molecular Neurobiology, Rudolf Magnus Institute, Utrecht, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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