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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2003-1-6
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pubmed:abstractText |
Chromaffin cells possess a mesh of filamentous actin underneath the plasma membrane which acts as a barrier to the chromaffin vesicles access to exocytotic sites. Disassembly of cortical F-actin in response to stimulation allows the movement of vesicles from the reserve pool to the release-ready vesicle pool and, therefore, to exocytotic sites. The dynamics of cortical F-actin is controlled by two mechanisms: a) stimulation-induced Ca2+ entry and scinderin activation and b) protein kinase C (PKC) activation and MARCKS phosphorylation as demonstrated here by experiments with recombinant proteins, antisense olygodeoxynucleotides and vector mediated transient expressions. Under physiological conditions (i.e., cholinergic receptor stimulation followed by Ca2+ entry), mechanism (a) is the most important for the control of cortical F-actin network whereas when Ca2+ is released from intracellular stores (i.e., histamine stimulation) cortical F-actin is regulated mainly by mechanism b.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Gelsolin,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosidases,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRKCSH protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/myristoylated alanine-rich C...,
http://linkedlifedata.com/resource/pubmed/chemical/scinderin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0364-3190
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1371-85
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12512942-Actins,
pubmed-meshheading:12512942-Amino Acid Sequence,
pubmed-meshheading:12512942-Animals,
pubmed-meshheading:12512942-Calcium,
pubmed-meshheading:12512942-Cerebral Cortex,
pubmed-meshheading:12512942-Enzyme Activation,
pubmed-meshheading:12512942-Gelsolin,
pubmed-meshheading:12512942-Glucosidases,
pubmed-meshheading:12512942-Humans,
pubmed-meshheading:12512942-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:12512942-Membrane Proteins,
pubmed-meshheading:12512942-Microfilament Proteins,
pubmed-meshheading:12512942-Molecular Sequence Data,
pubmed-meshheading:12512942-Phosphoproteins,
pubmed-meshheading:12512942-Protein Kinase C
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pubmed:year |
2002
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pubmed:articleTitle |
Pathways that control cortical F-actin dynamics during secretion.
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pubmed:affiliation |
Secretory Process Research Program, Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ontario, Canada K1H 8M5. jtrifaro@uottawa.ca
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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