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Association of the N-formyl-Met-Leu-Phe receptor in human neutrophils with a GTP-binding protein sensitive to pertussis toxin.
Open accessAbstract
Pertussis toxin inhibits the N-formyl-Met-Leu-Phe (fMet-Leu-Phe) mediated human neutrophil functions of enzyme release, superoxide generation, aggregation, and chemotaxis. As pertussis toxin modifies the GTP binding receptor-regulatory protein "Ni," the association of the fMet-Leu-Phe receptor with such a protein was further examined in purified neutrophil plasma membranes. Both fMet-Leu-Phe-mediated guanine nucleotide exchange and nucleotide-mediated regulation of the fMet-Leu-Phe receptor are inhibited by pertussis toxin. In addition, membrane pretreatment with pertussis toxin abolishes the fMet-Leu-Phe-mediated inhibition of adenylate cyclase. Actions of pertussis toxin are due to the ADP-ribosylation of a single subunit at 41 kDa in the neutrophil plasma membrane, which comigrates on NaDodSO4 gels with the Ni GTP-binding protein in the platelet plasma membrane. Our results suggest that (i) the fMet-Leu-Phe receptor is associated with a Ni GTP regulatory protein, and (ii) a fMet-Leu-Phe-Ni complex is important in the control of several neutrophil functions, probably involving multiple transduction systems, including adenylate cyclase.
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Metadata
- Authors
- Lad, P. M., Olson, C. V., & Smiley, P. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1985-02
- Volume
- 82
- Issue
- 3
- Pages
- 869-873
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2088833154
- Cited by
- 158
- References
- 0
- FWCI
- 9.92
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Association of the N-formyl-Met-Leu-Phe receptor in human neutrophils with a GTP-binding protein sensitive to pertussis toxin. https://app.cochat.ai/papers/10.1073/pnas.82.3.869
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- Lad, P. M., Olson, C. V., & Smiley, P. A. (1985). Association of the N-formyl-Met-Leu-Phe receptor in human neutrophils with a GTP-binding protein sensitive to pertussis toxin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.3.869
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