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Molecular Pharmacology

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Research ArticleArticle

Lysophosphatidic Acid Modulates α1b-Adrenoceptor Phosphorylation and Function: Roles of Gi and Phosphoinositide 3-Kinase

Patricia Casas-González, José Vázquez-Prado and J. Adolfo García-Sáinz
Molecular Pharmacology May 2000, 57 (5) 1027-1033;
Patricia Casas-González
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José Vázquez-Prado
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J. Adolfo García-Sáinz
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Abstract

The effect of lysophosphatidic acid on the phosphorylation and function of α1b-adrenoceptors transfected into rat-1 fibroblasts was studied. This phospholipid mitogen increased in a concentration-dependent fashion (EC50 ∼50 nM) the phosphorylation of these adrenoceptors. Lysophosphatidic acid-induced α1b-adrenoceptor phosphorylation was relatively rapid (t1/2 ∼1 min), intense (2.5-fold), and sustained for at least 60 min. The effect of lysophosphatidic acid was blocked by pretreatment with pertussis toxin. The α1b-adrenoceptor phosphorylation induced by lysophosphatidic acid was not blocked by genistein, a tyrosine kinase inhibitor, but it was inhibited by inhibitors of protein kinase C (bisindolylmaleimide I, staurosporine, and Ro 31-8220) and phosphoinositide 3-kinase (wortmannin and LY 294002). The ability of norepinephrine to increase cytosol calcium concentration was markedly decreased in cells previously challenged with lysophosphatidic acid. Norepinephrine-induced [35S]GTPγS binding in membrane preparations was used as an index of the functional coupling of the α1b-adrenoceptors and G proteins. Norepinephrine-stimulated [35S]GTPγS binding was markedly decreased in membranes from cells pretreated with lysophosphatidic acid. This effect of lysophosphatidic acid was blocked by pretreatment with wortmannin or staurosporine. Our data indicate that: 1) activation of lysophosphatidic acid receptors induce phosphorylation of α1b-adrenoceptors; 2) this effect is mediated through pertussis toxin-sensitive G proteins, phosphatidylinositol 3-kinase, and protein kinase C; and 3) the phosphorylation of α1b-adrenoceptors induced by the lipid mitogen is associated to adrenoceptor desensitization.

Footnotes

  • Send reprint requests to: J. Adolfo Garcı́a-Sáinz, M.D., Ph.D., Inst. Fisiologı́a Celular, UNAM, Ap. Postal 70–248, México, D. F. 04510. E-mail: agarcia{at}ifisiol.unam.mx

  • This research was partially supported by grants from Dirección General de Asuntos del Personal Académico (IN 200596 and IN 205199) and Consejo Nacional de Ciencia y Tecnologı́a (27569N).

  • Abbreviations:
    PKC
    protein kinase C
    AR
    adrenoceptor
    LPA
    lysophosphatidic acid
    DMEM
    Dulbecco's modified Eagle's medium
    GRK
    G protein-coupled receptor kinase
    PI3K
    phosphoinositide 3-kinase
    [Ca2+]i
    cytosol calcium concentration
    NE
    norepinephrine
    TPA
    tetradecanoyl phorbol acetate
    PDK1
    phosphoinositide-dependent protein kinase-1
    • Received August 30, 1999.
    • Accepted January 20, 2000.
  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 57 (5)
Molecular Pharmacology
Vol. 57, Issue 5
1 May 2000
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Research ArticleArticle

Lysophosphatidic Acid Modulates α1b-Adrenoceptor Phosphorylation and Function: Roles of Gi and Phosphoinositide 3-Kinase

Patricia Casas-González, José Vázquez-Prado and J. Adolfo García-Sáinz
Molecular Pharmacology May 1, 2000, 57 (5) 1027-1033;

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Research ArticleArticle

Lysophosphatidic Acid Modulates α1b-Adrenoceptor Phosphorylation and Function: Roles of Gi and Phosphoinositide 3-Kinase

Patricia Casas-González, José Vázquez-Prado and J. Adolfo García-Sáinz
Molecular Pharmacology May 1, 2000, 57 (5) 1027-1033;
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