Abstract
The role of a specific guanine nucleotide binding (G protein) protein in coupling murine B lymphocyte receptor immunoglobulin to inositol phospholipid hydrolysis was investigated. Using an in vitro system with isolated membranes, we have observed specific enhancement of GTP binding subsequent to ligand-induced receptor crosslinking. Induced increases were inhibited by pretreatment with pertussis toxin which catalyzed ADP-ribosylation of a 43 kDa substrate. Involvement of this G protein with receptor immunoglobulin-induced inositol phospholipid hydrolysis was evidenced by the ability of pertussis toxin to block this response. This report, then, indicates that the B lymphocyte antigen receptor belongs to a family of receptors which are linked to inositol phospholipid hydrolysis through a G protein.
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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Adenosine Diphosphate Ribose / metabolism
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Animals
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B-Lymphocytes / immunology*
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Cell Membrane / immunology
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GTP-Binding Proteins / physiology*
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Guanosine 5'-O-(3-Thiotriphosphate)
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Guanosine Diphosphate / pharmacology
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Guanosine Triphosphate / metabolism
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Hydrolysis
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Immunoglobulin M / immunology
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Immunoglobulin mu-Chains / immunology
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Lymphoma / immunology
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Mice
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Pertussis Toxin
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Phosphatidylinositols / metabolism*
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Receptors, Immunologic / physiology*
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Thionucleotides / metabolism
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Tumor Cells, Cultured
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Virulence Factors, Bordetella / pharmacology
Substances
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Immunoglobulin M
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Immunoglobulin mu-Chains
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Phosphatidylinositols
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Receptors, Immunologic
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Thionucleotides
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Virulence Factors, Bordetella
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Guanosine Diphosphate
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Adenosine Diphosphate Ribose
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Guanosine 5'-O-(3-Thiotriphosphate)
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Guanosine Triphosphate
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Pertussis Toxin
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GTP-Binding Proteins