Pertussis toxin inhibits enkephalin stimulation of GTPase of NG108-15 cells.
Open accessAbstract
In neuroblastoma-glioma (NG108-15) hybrid cells, opiates inhibit adenylate cyclase and stimulate a low Km GTPase. It has been postulated that the stimulation of GTPase plays a role in opiate inhibition of adenylate cyclase (Koski, G., and Klee, W. A. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 4185-4189). Treatment of NG108-15 cells with pertussis toxin attenuates receptor-mediated inhibition of adenylate cyclase. The toxin acts by catalyzing the ADP-ribosylation of a 41,000-dalton substrate believed to be a part of the receptor-adenylate cyclase complex. We have found that toxin treatment of NG108-15 results in inhibition of the opiate-stimulated GTPase. The concentration of toxin required for inhibition of this GTPase was similar to that needed for both attenuation of opiate inhibition of adenylate cyclase and ADP ribosylation of the 41,000-dalton substrate. Inhibition of the opiate-induced GTPase by pertussis toxin in isolated membranes required NAD, consistent with the hypothesis that this effect of the toxin resulted from ADP ribosylation of a protein component of the system. Since the opiate-stimulated GTPase is believed to play a role in the receptor-mediated decrease in adenylate cyclase activity, inhibition of this GTPase may be an important part of the mechanism by which the toxin interferes with opiate action on adenylate cyclase.
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All three opioid receptor types are Gi protein-coupled receptors that are inhibitory when activated.
“All three receptor types are GI protein-coupled receptors that are inhibitory when activated (Burns et al 1983; Tsunoo et al 1986; North et al 1987; for a review see Knapp et al 1995).”
From The behavioral, anatomical and pharmacological parallels between social attachment, love and addiction (2012) · cites this paper as Burns et al 1983
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Burkett, J. P., & Young, L. J. (2012) · Psychopharmacology · doi:10.1007/s00213-012-2794-x · Cited by 307 · see citing works
“All three receptor types are GI protein-coupled receptors that are inhibitory when activated (Burns et al. 1983; Tsunoo et al. 1986; North et al. 1987; for a review, see Knapp et al. 1995).”
- Authors
- Burns, D. L., Hewlett, E. L., Moss, J., & Vaughan, M.
- Affiliations
- National Institutes of Health (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1983-02
- Volume
- 258
- Issue
- 3
- Pages
- 1435-1438
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1585463957
- Cited by
- 187
- References
- 32
- Citations by year
- 2022: 1 · 2016: 2 · 2015: 1 · 2012: 1
- FWCI
- 12.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- pertussis toxin, enkephalin, GTPase, NG108-15 cells, ADP-ribosylation, opioid receptors, NAD+
- MeSH terms
- Adenosine Diphosphate Ribose, Analgesics, Animals, Bacterial Toxins, Bordetella pertussis, Cell Line, Enkephalin, Methionine, Glioma, Hybrid Cells, Kinetics, Molecular Weight, Neuroblastoma, Virulence Factors, Bordetella, Phosphoric Monoester Hydrolases, GTP Phosphohydrolases, Pertussis Toxin, Adenylate Cyclase Toxin, Mice, Rats
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