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Research ArticleCELLULAR AND MOLECULAR

CB1 Cannabinoid Receptor-Mediated Cell Migration

Zhao-Hui Song and Miao Zhong
Journal of Pharmacology and Experimental Therapeutics July 2000, 294 (1) 204-209;
Zhao-Hui Song
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Miao Zhong
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Abstract

Recent studies have suggested that cell migratory responses are often mediated by Gi protein-coupled receptors. Because it is known that CB1 cannabinoid receptors are coupled to pertussis toxin-sensitive G proteins, we proposed that CB1 may mediate cell migration. To test this hypothesis, modified Boyden chamber assays were used to investigate cell migration mediated by CB1 cannabinoid receptors. HU-210, WIN55212-2, and anandamide, three cannabinoid agonists with distinct chemical structures, induced migration of human embryonic kidney 293 cells stably transfected with humanCB1 gene, but not 293 cells transfected with an empty expression vector. These migratory responses were concentration-dependent. The EC50 values for HU-210, WIN55212-2, and anandamide were 0.19 ± 0.04, 12.2 ± 1.4, and 39.9 ± 3.7 nM, respectively. The maximal migration index for HU-210, WIN55212-2, and anandamide were 8.9 ± 1.6, 9.5 ± 1.6, and 8.8 ± 1.3, respectively. Pretreating cells with 100 ng/ml pertussis toxin eliminated the cannabinoid agonist-induced cell migration. SR141716A, a selective antagonist for CB1, inhibited the cannabinoid agonist-induced migratory responses in a concentration-dependent manner. Checkerboard analysis demonstrated that anandamide-induced cell migrations are due to chemotaxis as well as chemokinesis. Furthermore, anandamide-induced migratory responses were inhibited, in a concentration-dependent manner, by PD098059, an inhibitor of mitogen-activated protein kinase activation, but not by 8-bromoadenosine-3′,5′-cyclic monophosphate, a cell-permeable cAMP analog. These data demonstrate that cannabinoid agonists are able to induce chemotaxis and chemokinesis, and that these migratory responses are mediated by G protein-coupled, CB1 cannabinoid receptors. In addition, these data suggest that activation of mitogen-activated protein kinase plays an important role, whereas inhibition of adenylate cyclase is probably not involved in the cell migration mediated by CB1.

Footnotes

  • Send reprint requests to: Z. H. Song, Ph.D., Department of Pharmacology and Toxicology, University of Louisville School of Medicine, Louisville, KY 40292. E-mail:zhsong{at}louisville.edu

  • ↵1 This work was supported in part by National Institutes of Health Grant DA-11551.

  • Abbreviations:
    MAPK
    mitogen-activated protein kinase
    8-Br-cAMP
    8-bromoadenosine-3′,5′-cyclic monophosphate
    DMEM
    Dulbecco's modified Eagle's medium
    ERK
    extracellular signal-regulated kinase
    • Received November 15, 1999.
    • Accepted March 22, 2000.
  • The American Society for Pharmacology and Experimental Therapeutics
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Journal of Pharmacology and Experimental Therapeutics: 294 (1)
Journal of Pharmacology and Experimental Therapeutics
Vol. 294, Issue 1
1 Jul 2000
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Research ArticleCELLULAR AND MOLECULAR

CB1 Cannabinoid Receptor-Mediated Cell Migration

Zhao-Hui Song and Miao Zhong
Journal of Pharmacology and Experimental Therapeutics July 1, 2000, 294 (1) 204-209;

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Research ArticleCELLULAR AND MOLECULAR

CB1 Cannabinoid Receptor-Mediated Cell Migration

Zhao-Hui Song and Miao Zhong
Journal of Pharmacology and Experimental Therapeutics July 1, 2000, 294 (1) 204-209;
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