Abstract
In cultured chick ciliary neurons, when ATP synthesis is inhibited, ATP depletion is reduced approximately 50% by slowing actin filament turnover with jasplakinolide or latrunculin A. Jasplakinolide inhibits actin disassembly, and latrunculin A prevents actin assembly by sequestering actin monomers. Cytochalasin D, which allows assembly-disassembly, but only at pointed ends, is less effective in conserving ATP. Ouabain, an Na(+)-K(+)-ATPase inhibitor, and jasplakinolide both prevent approximately 50% of the ATP loss. When applied together, they completely prevent ATP loss over a period of 20 min, suggesting that filament stabilization reduces ATP consumption by decreasing actin-ATP hydrolysis directly rather than indirectly by modulating the activity of Na(+)-K(+)-ATPase, a major energy consumer.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actin Cytoskeleton / drug effects
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Actin Cytoskeleton / metabolism*
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Actin Cytoskeleton / ultrastructure
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Actins / metabolism*
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Adenosine Triphosphate / metabolism*
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Animals
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Bridged Bicyclo Compounds, Heterocyclic / pharmacology
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Calcium / analysis
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Cell Hypoxia
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Cells, Cultured
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Chick Embryo
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Depsipeptides*
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Energy Metabolism
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Enzyme Inhibitors / pharmacology
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Hydrolysis
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Neurons / cytology
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Neurons / drug effects
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Neurons / metabolism*
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Ouabain / pharmacology
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Peptides, Cyclic / pharmacology
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Sodium / analysis
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Sodium-Potassium-Exchanging ATPase / antagonists & inhibitors
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Thiazoles / pharmacology
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Thiazolidines
Substances
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Actins
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Bridged Bicyclo Compounds, Heterocyclic
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Depsipeptides
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Enzyme Inhibitors
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Peptides, Cyclic
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Thiazoles
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Thiazolidines
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jasplakinolide
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Ouabain
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Adenosine Triphosphate
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Sodium
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Sodium-Potassium-Exchanging ATPase
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latrunculin A
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Calcium