Abstract
The effect of AlF4- on the degranulation process in human neutrophils was investigated. In intact neutrophils, AlF4- induced degranulation, whereas in electropermeabilized neutrophils AlF4- did not stimulate degranulation. In electropermeabilized neutrophils, fluoride ions proved to be inhibitory for the degranulation induced by addition of Ca2+ and/or GTP-gamma-S. Another phosphatase inhibitor, okadaic acid, inhibited degranulation induced by Ca2+ or by GTP-gamma-S but not degranulation induced by the combination of Ca2+ plus GTP-gamma-S. It is concluded that under suboptimal conditions of stimulation with Ca2+ or GTP-gamma-S, protein dephosphorylation plays an important role in the degranulation response in human neutrophils.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, CD / analysis
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Antigens, Neoplasm*
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Cell Adhesion Molecules*
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Cell Degranulation / drug effects*
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Ethers, Cyclic / pharmacology
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Fluorides / pharmacology*
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GTP-Binding Proteins / physiology
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Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
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Humans
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Membrane Glycoproteins / analysis
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Neutrophils / drug effects*
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Neutrophils / physiology
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Okadaic Acid
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Permeability
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Platelet Membrane Glycoproteins / analysis
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Tetraspanin 30
Substances
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Antigens, CD
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Antigens, Neoplasm
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CD63 protein, human
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Cell Adhesion Molecules
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Ethers, Cyclic
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Membrane Glycoproteins
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Platelet Membrane Glycoproteins
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Tetraspanin 30
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Okadaic Acid
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Guanosine 5'-O-(3-Thiotriphosphate)
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GTP-Binding Proteins
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Fluorides