Abstract
Nordihydroguaiaretic acid (NDGA) caused disassembly of the Golgi apparatus of NRK cells in a dose-, time-, and energy-dependent manner but not in a microtubule-dependent manner. In contrast to brefeldin A, NDGA did not cause release of beta-COP, a component of Golgi-derived vesicles. However, NDGA-induced disassembly was blocked by AlF4-, an activator of the heterotrimeric but not the small GTP-binding proteins. In digitonin-permeabilized cells, guanosine 5'-3-O-(thio)triphosphate (GTPgammaS) as well as AlF4- blocked the NDGA-promoted disassembly of the Golgi apparatus, and Gbetagamma (betagamma subunits of heterotrimeric G proteins) reversed this effect. Our present results suggest the possible involvement of heterotrimeric G proteins in the organization of the Golgi apparatus.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Line
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Cell Membrane Permeability
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Cholera Toxin / pharmacology
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Coatomer Protein
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Cycloheximide / pharmacology
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Digitonin
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GTP-Binding Proteins / chemistry*
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GTP-Binding Proteins / metabolism*
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Golgi Apparatus / drug effects
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Golgi Apparatus / physiology*
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Golgi Apparatus / ultrastructure
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Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
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Kidney
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Macromolecular Substances
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Masoprocol / pharmacology
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Membrane Proteins / analysis
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Membrane Proteins / metabolism
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Microtubule-Associated Proteins / analysis
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Microtubule-Associated Proteins / metabolism
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Microtubules / drug effects
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Microtubules / physiology
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Microtubules / ultrastructure
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Rats
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Virulence Factors, Bordetella / pharmacology
Substances
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Coatomer Protein
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Macromolecular Substances
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Membrane Proteins
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Microtubule-Associated Proteins
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Virulence Factors, Bordetella
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Guanosine 5'-O-(3-Thiotriphosphate)
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Masoprocol
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Cholera Toxin
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Cycloheximide
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GTP-Binding Proteins
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Digitonin