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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1990-10-23
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pubmed:abstractText |
The control of cytoskeletal actin and exocytosis was examined in intact and digitonin-permeabilized chromaffin cells. Cytoskeletal actin was assayed by determining the actin content of Triton-insoluble cytoskeletons. The secretagogues nicotine, high K+ and Ba2+ resulted in a rapid reduction in the amount of actin associated with the cytoskeleton. The effect of nicotine but not high K+ on cytoskeletal actin was independent of external Ca2+ and the reduction in cytoskeletal actin was mimicked by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate suggesting a role for protein kinase C. In digitonin-permeabilized cells micromolar calcium produced both catecholamine secretion and a reduction in cytoskeletal actin. The reduction in cytoskeletal actin was transient. Secretion was enhanced by the GTP analogue guanosine 5'-(3-O-thio)triphosphate and the analogue also reduced cytoskeletal actin at low calcium levels. The effects of guanosine 5'-(3-O-thio)triphosphate were inhibited by the phospholipase C inhibitor neomycin and were mimicked by 12-O-tetradecanoylphorbol-13-acetate. An additional GTP analogue, guanyl-5'-yl imidodiphosphate, had no effect on cytoskeletal actin. These results provide further evidence for a requirement for reorganisation of cortical actin in the secretory processes and suggest that the reduction in actin associated with the cytoskeleton may be mediated by protein kinase C and/or calcium in intact and permeabilized chromaffin cells.
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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/Barium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Digitonin,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Neomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Nicotine,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides
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pubmed:status |
MEDLINE
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pubmed:issn |
0898-6568
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
323-34
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2518377-Actins,
pubmed-meshheading:2518377-Adrenal Medulla,
pubmed-meshheading:2518377-Animals,
pubmed-meshheading:2518377-Barium,
pubmed-meshheading:2518377-Calcium,
pubmed-meshheading:2518377-Cattle,
pubmed-meshheading:2518377-Cell Membrane Permeability,
pubmed-meshheading:2518377-Cytoskeleton,
pubmed-meshheading:2518377-Digitonin,
pubmed-meshheading:2518377-Exocytosis,
pubmed-meshheading:2518377-GTP-Binding Proteins,
pubmed-meshheading:2518377-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:2518377-Guanosine Triphosphate,
pubmed-meshheading:2518377-Kinetics,
pubmed-meshheading:2518377-Neomycin,
pubmed-meshheading:2518377-Nicotine,
pubmed-meshheading:2518377-Potassium,
pubmed-meshheading:2518377-Protein Kinase C,
pubmed-meshheading:2518377-Tetradecanoylphorbol Acetate,
pubmed-meshheading:2518377-Thionucleotides
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pubmed:year |
1989
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pubmed:articleTitle |
The control of cytoskeletal actin and exocytosis in intact and permeabilized adrenal chromaffin cells: role of calcium and protein kinase C.
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pubmed:affiliation |
Physiological Laboratory, University of Liverpool, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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