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Direct coupling of opioid receptors to both stimulatory and inhibitory guanine nucleotide-binding proteins in F-11 neuroblastoma-sensory neuron hybrid cells.
Proc Natl Acad Sci U S A. 1993 Apr 01; 90(7):3019-23.PN

Abstract

Evidence is presented for linkage of opioid receptors directly to the stimulatory G protein (guanine nucleotide-binding protein), Gs, in addition to the generally accepted linkage to the inhibitory and "other" G proteins, gi and Go, in F-11 (neuroblastoma-dorsal root ganglion neuron) hybrid cells. Treatment of intact F-11 cells with cholera toxin decreased specific binding of the opioid agonist [D-Ala2,D-Leu5]enkephalin to F-11 cell membranes by 35%, with the remaining binding retaining high affinity for agonist. Under these conditions cholera toxin influenced the alpha subunit of Gs (Gs alpha) but had no effect on the alpha subunit of Gi/o (Gi/o alpha), based on ADP-ribosylation studies. Pertussis toxin treatment decreased high-affinity opioid agonist binding by about 50%; remaining binding was also of high affinity, even though pertussis toxin had inactivated Gi/o alpha selectively and essentially completely. Simultaneous treatment with both toxins had an additive effect, reducing specific binding by about 80%. While opioid agonists inhibited forskolin-stimulated adenylate cyclase activity of F-11 cells as expected, opioids also stimulated basal adenylate cyclase activity, indicative of interaction with Gs as well as Gi. Cholera toxin treatment attenuated opioid-stimulation of basal adenylate cyclase, whereas pertussis toxin treatment enhanced stimulation. In contrast, inhibition by opioid of forskolin-stimulated activity was attenuated by pertussis toxin but not by cholera toxin. It is concluded that a subset of opioid receptors may be linked directly to Gs and thereby mediate stimulation of adenylate cyclase. This Gs-adenylate cyclase interaction is postulated to be responsible for the novel excitatory electrophysiologic responses to opioids found in our previous studies of sensory neurons and F-11 cells.

Authors+Show Affiliations

Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8385355

Citation

Cruciani, R A., et al. "Direct Coupling of Opioid Receptors to Both Stimulatory and Inhibitory Guanine Nucleotide-binding Proteins in F-11 Neuroblastoma-sensory Neuron Hybrid Cells." Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 7, 1993, pp. 3019-23.
Cruciani RA, Dvorkin B, Morris SA, et al. Direct coupling of opioid receptors to both stimulatory and inhibitory guanine nucleotide-binding proteins in F-11 neuroblastoma-sensory neuron hybrid cells. Proc Natl Acad Sci U S A. 1993;90(7):3019-23.
Cruciani, R. A., Dvorkin, B., Morris, S. A., Crain, S. M., & Makman, M. H. (1993). Direct coupling of opioid receptors to both stimulatory and inhibitory guanine nucleotide-binding proteins in F-11 neuroblastoma-sensory neuron hybrid cells. Proceedings of the National Academy of Sciences of the United States of America, 90(7), 3019-23.
Cruciani RA, et al. Direct Coupling of Opioid Receptors to Both Stimulatory and Inhibitory Guanine Nucleotide-binding Proteins in F-11 Neuroblastoma-sensory Neuron Hybrid Cells. Proc Natl Acad Sci U S A. 1993 Apr 1;90(7):3019-23. PubMed PMID: 8385355.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Direct coupling of opioid receptors to both stimulatory and inhibitory guanine nucleotide-binding proteins in F-11 neuroblastoma-sensory neuron hybrid cells. AU - Cruciani,R A, AU - Dvorkin,B, AU - Morris,S A, AU - Crain,S M, AU - Makman,M H, PY - 1993/4/1/pubmed PY - 1993/4/1/medline PY - 1993/4/1/entrez SP - 3019 EP - 23 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 90 IS - 7 N2 - Evidence is presented for linkage of opioid receptors directly to the stimulatory G protein (guanine nucleotide-binding protein), Gs, in addition to the generally accepted linkage to the inhibitory and "other" G proteins, gi and Go, in F-11 (neuroblastoma-dorsal root ganglion neuron) hybrid cells. Treatment of intact F-11 cells with cholera toxin decreased specific binding of the opioid agonist [D-Ala2,D-Leu5]enkephalin to F-11 cell membranes by 35%, with the remaining binding retaining high affinity for agonist. Under these conditions cholera toxin influenced the alpha subunit of Gs (Gs alpha) but had no effect on the alpha subunit of Gi/o (Gi/o alpha), based on ADP-ribosylation studies. Pertussis toxin treatment decreased high-affinity opioid agonist binding by about 50%; remaining binding was also of high affinity, even though pertussis toxin had inactivated Gi/o alpha selectively and essentially completely. Simultaneous treatment with both toxins had an additive effect, reducing specific binding by about 80%. While opioid agonists inhibited forskolin-stimulated adenylate cyclase activity of F-11 cells as expected, opioids also stimulated basal adenylate cyclase activity, indicative of interaction with Gs as well as Gi. Cholera toxin treatment attenuated opioid-stimulation of basal adenylate cyclase, whereas pertussis toxin treatment enhanced stimulation. In contrast, inhibition by opioid of forskolin-stimulated activity was attenuated by pertussis toxin but not by cholera toxin. It is concluded that a subset of opioid receptors may be linked directly to Gs and thereby mediate stimulation of adenylate cyclase. This Gs-adenylate cyclase interaction is postulated to be responsible for the novel excitatory electrophysiologic responses to opioids found in our previous studies of sensory neurons and F-11 cells. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/8385355/Direct_coupling_of_opioid_receptors_to_both_stimulatory_and_inhibitory_guanine_nucleotide_binding_proteins_in_F_11_neuroblastoma_sensory_neuron_hybrid_cells_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=8385355 DB - PRIME DP - Unbound Medicine ER -