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Research ArticleArticle

Characterization of CB1 Cannabinoid Receptors Using Receptor Peptide Fragments and Site-Directed Antibodies

Allyn C. Howlett, Chao Song, Barbara A. Berglund, Gerald H. Wilken and J. Jill Pigg
Molecular Pharmacology March 1998, 53 (3) 504-510; DOI: https://doi.org/10.1124/mol.53.3.504
Allyn C. Howlett
Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, St. Louis, Missouri 63104
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Chao Song
Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, St. Louis, Missouri 63104
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Barbara A. Berglund
Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, St. Louis, Missouri 63104
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Gerald H. Wilken
Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, St. Louis, Missouri 63104
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J. Jill Pigg
Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, St. Louis, Missouri 63104
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Abstract

The mechanism by which CB1 cannabinoid receptors are coupled to the Gi/Go class of G proteins was studied. A peptide representing the juxtamembrane carboxyl terminus robustly stimulated guanosine-5′-O-(3-thio)triphosphate binding. Peptides simulating subdomains of the third intracellular loop (IL3) activated minimally when present alone but produced additive effects when present in combination. Peptides representing the amino-side IL3 and the juxtamembrane carboxyl terminus autonomously inhibited adenylate cyclase, and this response was not significantly augmented or inhibited by peptides representing other intracellular domains. Site-directed antipeptide antibodies developed against the domains of the amino terminus, first extracellular loop, amino-side IL3, and juxtamembrane carboxyl terminus of CB1 receptors failed to influence binding of [3H]CP-55940. However, IgG raised against the amino-side IL3 diminished the agonist-dependent inhibition of adenylate cyclase. These experiments suggest that the juxtamembrane carboxyl terminus is critical for G protein activation by CB1 cannabinoid receptors and that the amino-side IL3 also may interact with Gi proteins leading to inhibition of adenylate cyclase.

Footnotes

    • Received August 4, 1997.
    • Accepted November 13, 1997.
  • Send reprint requests to: Dr. Allyn C. Howlett, Department of Pharmacological and Physiological Science, 1402 South Grand Boulevard, St. Louis, MO 63104. E-mail:howletta{at}slu.edu

  • ↵1 Current affiliation: Department of Surgery, Beth Israel Deaconess Hospital, Harvard Medical School, Boston, MA 02115.

  • This work was supported National Institute on Drug Abuse Grants R01-DA03690, R01-DA06312, and K05-DA00182.

  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 53 (3)
Molecular Pharmacology
Vol. 53, Issue 3
1 Mar 1998
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Research ArticleArticle

Characterization of CB1 Cannabinoid Receptors Using Receptor Peptide Fragments and Site-Directed Antibodies

Allyn C. Howlett, Chao Song, Barbara A. Berglund, Gerald H. Wilken and J. Jill Pigg
Molecular Pharmacology March 1, 1998, 53 (3) 504-510; DOI: https://doi.org/10.1124/mol.53.3.504

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Research ArticleArticle

Characterization of CB1 Cannabinoid Receptors Using Receptor Peptide Fragments and Site-Directed Antibodies

Allyn C. Howlett, Chao Song, Barbara A. Berglund, Gerald H. Wilken and J. Jill Pigg
Molecular Pharmacology March 1, 1998, 53 (3) 504-510; DOI: https://doi.org/10.1124/mol.53.3.504
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