Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin

Gary M. Bokoch; Alfred G. Gilman

doi:10.1016/0092-8674(84)90008-4

Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin

Gary M. Bokoch, Alfred G. Gilman

Pharmacology

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

Treatment of guinea pig neutrophils with pertussis toxin (islet-activating protein; IAP) results in inhibition of N-formyl peptide receptor-mediated release of arachidonic acid and granular enzymes. Inhibition by the toxin is specific, in that responses to the calcium ionophore A23187 are not affected. The action of the toxin is not associated with alterations in cellular concentrations of cyclic AMP but is correlated with the ability of the toxin to catalyze the ADP-ribosylation of a 41,000 dalton membrane protein. This protein comigrates on SDS-polyacrylamide gels with the α subunit of G_i, the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. It is likely that this G protein is involved in receptor-mediated signal transduction in neutrophils by mechanisms that do not involve cyclic AMP.

Original language	English (US)
Pages (from-to)	301-308
Number of pages	8
Journal	Cell
Volume	39
Issue number	2 PART 1
DOIs	https://doi.org/10.1016/0092-8674(84)90008-4
State	Published - Dec 1984

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/0092-8674(84)90008-4

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title = "Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin",

abstract = "Treatment of guinea pig neutrophils with pertussis toxin (islet-activating protein; IAP) results in inhibition of N-formyl peptide receptor-mediated release of arachidonic acid and granular enzymes. Inhibition by the toxin is specific, in that responses to the calcium ionophore A23187 are not affected. The action of the toxin is not associated with alterations in cellular concentrations of cyclic AMP but is correlated with the ability of the toxin to catalyze the ADP-ribosylation of a 41,000 dalton membrane protein. This protein comigrates on SDS-polyacrylamide gels with the α subunit of Gi, the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. It is likely that this G protein is involved in receptor-mediated signal transduction in neutrophils by mechanisms that do not involve cyclic AMP.",

author = "Bokoch, {Gary M.} and Gilman, {Alfred G.}",

note = "Funding Information: The authors would like to thank Thomas Rail and Carol D. Manning for excellent technical assistance, and Sherry Warchol for assistance in prep- aration of the manuscript. This work was supported by United States Publrc Health Service Grant NS18153 and by a grant from the American Cancer Society (BC24OF). G. M. B. was a recipient of a National Institutes of Health postdoctoral fellowship (5 F32 GM08399).",

year = "1984",

month = dec,

doi = "10.1016/0092-8674(84)90008-4",

language = "English (US)",

volume = "39",

pages = "301--308",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "2 PART 1",

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T1 - Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin

AU - Bokoch, Gary M.

AU - Gilman, Alfred G.

N1 - Funding Information: The authors would like to thank Thomas Rail and Carol D. Manning for excellent technical assistance, and Sherry Warchol for assistance in prep- aration of the manuscript. This work was supported by United States Publrc Health Service Grant NS18153 and by a grant from the American Cancer Society (BC24OF). G. M. B. was a recipient of a National Institutes of Health postdoctoral fellowship (5 F32 GM08399).

PY - 1984/12

Y1 - 1984/12

N2 - Treatment of guinea pig neutrophils with pertussis toxin (islet-activating protein; IAP) results in inhibition of N-formyl peptide receptor-mediated release of arachidonic acid and granular enzymes. Inhibition by the toxin is specific, in that responses to the calcium ionophore A23187 are not affected. The action of the toxin is not associated with alterations in cellular concentrations of cyclic AMP but is correlated with the ability of the toxin to catalyze the ADP-ribosylation of a 41,000 dalton membrane protein. This protein comigrates on SDS-polyacrylamide gels with the α subunit of Gi, the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. It is likely that this G protein is involved in receptor-mediated signal transduction in neutrophils by mechanisms that do not involve cyclic AMP.

AB - Treatment of guinea pig neutrophils with pertussis toxin (islet-activating protein; IAP) results in inhibition of N-formyl peptide receptor-mediated release of arachidonic acid and granular enzymes. Inhibition by the toxin is specific, in that responses to the calcium ionophore A23187 are not affected. The action of the toxin is not associated with alterations in cellular concentrations of cyclic AMP but is correlated with the ability of the toxin to catalyze the ADP-ribosylation of a 41,000 dalton membrane protein. This protein comigrates on SDS-polyacrylamide gels with the α subunit of Gi, the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. It is likely that this G protein is involved in receptor-mediated signal transduction in neutrophils by mechanisms that do not involve cyclic AMP.

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JO - Cell

JF - Cell

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ER -

Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin

Abstract

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