Lysophosphatidic acid induces $alpha;1B-adrenergic receptor phosphorylation through G$beta;$gamma;, phosphoinositide 3-kinase, protein kinase C and epidermal growth factor receptor transactivation

Casas‐González, Patricia; Ruiz-Martı́nez, Alejandro; García‐Sáinz, J. Adolfo

doi:10.1016/s1388-1981(03)00089-1

Cited by 30 publications

(35 citation statements)

References 37 publications

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“…Our results indicate that this process is involved in the modulation of ␣ 1b -ARs, which is consistent with previous findings from our laboratory (Vá zquez-Prado et al, 1997;Medina et al, 1998;Casas-Gonzá lez et al, 2003;García-Sá inz et al, 2004). The dynamic association of PI3K with ␣ 1b -ARs in response to 17␤-estradiol is consistent with a role in these effects.…”

Section: Discussionsupporting

confidence: 93%

“…Thus, it has been observed that activation of seven transmembrane domain receptors coupled to G q/11 (such as endothelin ET A receptors or bradykinin B2 receptors) (Vá zquez-Prado et al, 1997;Medina et al, 1998) or G i (such as lysophosphatidic acid receptors) (Casas-Gonzá lez et al, 2003) or receptors with intrinsic tyrosine kinase activity (such as those for epidermal growth factor, platelet-derived growth factor, and insulin) García-Sá inz et al, 2004) can induce ␣ 1b -AR phosphorylation and desensitization. Protein kinase C and phosphoinositide 3-kinase (PI3K) are key participants in these effects (reviewed by García-Sá inz et al, 2000).…”

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confidence: 99%

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Estrogens Cross-Talk to α_1b-Adrenergic Receptors

et al. 2006

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␤-Estradiol induced ␣ 1b -adrenergic receptor desensitization in U373 MG cells stably expressing ␣ 1b -adrenoceptors, as evidenced by a reduction in the adrenergic-mediated Ca 2ϩ mobilization; desensitization was associated with receptor phosphorylation and internalization. These effects of ␤-estradiol were rapid (taking place during 15 min) and were blocked by the estrogen receptor antagonist ICI 182,780 (faslodex). Likewise, inhibitors of phosphoinositide 3-kinase [wortmannin and 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)] and of protein kinase C [staurosporine, 3-[1-[3-(amidinothio)propyl-1H-indol-3-yl]-3-(1-methyl-1H-indol-3-yl) maleimide (Ro31-8220), and rottlerin] blocked the desensitization and phosphorylation of ␣ 1b -adrenoceptors induced by estradiol. The formation of a complex was suggested by coimmunoprecipitation assays. The regulatory and catalytic subunits of phosphoinositide 3-kinase (p85 and p110) and protein kinase C ␦ were associated with ␣ 1b -adrenoceptors in the absence of stimulus, and such association further increased in a dynamic fashion in response to ␤-estradiol. In cells cotransfected with the estrogen receptor ␣ and ␣ 1b -adrenoceptors, ␤-estradiol induced phosphorylation, desensitization and internalization of the adrenergic receptors; pretreatment with ICI 182,780 inhibited these effects. Our data support the idea that estrogens modulate ␣ 1b -adrenergic action through estrogen receptor ␣.

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Section: Discussionsupporting

confidence: 93%

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confidence: 99%

Estrogens Cross-Talk to α_1b-Adrenergic Receptors

et al. 2006

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“…dressed the mechanism and role of transactivation of RTKs in the mediation and regulation of promitogenic pathways stimulated by GPCRs (Luttrell et al, 1999;Maudsley et al, 2000;. However, recent evidence has indicated that RTKs can also act as regulators of GPCR signaling (Medina et al, 2000;Casas-Gonzá lez et al, 2003;García-Sá inz et al, 2004). In C9 cells, EGF induced phosphorylation of the AT 1 -R in a dose-dependent manner by 70 to 80% over basal (Fig.…”

Section: Resultsmentioning

confidence: 99%

Agonist-Induced Interactions between Angiotensin AT₁and Epidermal Growth Factor Receptors

et al. 2005

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In rat hepatic C9 cells, angiotensin II (Ang II)-induced activation of angiotensin type 1 (AT 1 ) receptors (AT 1 -Rs) stimulates extracellular signal-regulated kinase (ERK) 1/2 phosphorylation via transactivation of the endogenous epidermal growth factor (EGF) receptor (EGF-R) by a protein kinase C (PKC) ␦/Src/Pyk2-dependent pathway. This leads to phosphorylation of the EGF-R as well as its subsequent internalization. On the other hand, EGF-induced activation of the EGF-R in C9 cells was found to cause phosphorylation of the AT 1 -R. This was prevented by selective inhibition of the intrinsic tyrosine kinase activity of the EGF-R by AG1478 [4-(3Ј-chloroanilino)-6,7-dimethoxy-quinazoline] and was reduced by inhibition of PKC and phosphoinositide 3-kinase. EGF-induced AT 1 -R phosphorylation was associated with a decrease in membrane-associated AT 1 -Rs and a reduced inositol phosphate response to Ang II. Agonist activation of endogenous AT 1 -Rs and EGF-Rs induced the formation of a multireceptor complex containing both the AT 1 -R and the transactivated EGF-R. The dependence of these responses on caveolin was indicated by the finding that cholesterol depletion of C9 cells abolished Ang II-induced inositol phosphate production, activation of Akt/PKB and ERK1/2, and AT 1 -R internalization. Confocal microscopy demonstrated that caveolin-1 was endogenously phosphorylated and was distributed on the plasma membrane in patches that undergo redistribution during Ang II stimulation. Agonist-induced phosphorylation and association of caveolin 1 with the AT 1 -R was observed, consistent with a scaffolding role of caveolin during transactivation of the EGF-R by Ang II. The EGF-induced AT 1 -R/caveolin association was abolished by AG1478, suggesting that activation of the EGF-R promotes the association of caveolin and the AT 1 -R.

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“…Furthermore, some different GPCRs, in addition to FPR shown in this study, are also capable of transactivating EGFR, including the receptors for lysophosphatidic acid (LPA; refs. [24][25][26], thrombin (27)(28)(29), endothelin-1 (30-34), carbachol (35)(36)(37), angiotensin (38)(39)(40), bombesin (41,42), and the chemokine SDF1 (CXCL12; ref. 43).…”

Section: Discussionmentioning

confidence: 99%

Transactivation of the Epidermal Growth Factor Receptor by Formylpeptide Receptor Exacerbates the Malignant Behavior of Human Glioblastoma Cells

Huang

Bian

et al. 2007

Cancer Research

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The G protein-coupled formylpeptide receptor (FPR), which mediates leukocyte migration in response to bacterial and host-derived chemotactic peptides, promotes the chemotaxis, survival, and tumorigenesis of highly malignant human glioblastoma cells. Because glioblastoma cells may also express other receptors for growth signals, such as the epidermal growth factor (EGF) receptor (EGFR), we investigated the role of EGFR in the signaling cascade of FPR and how two receptors cross-talk to exacerbate tumor growth. We found that N-formyl-methionyl-leucyl-phenylalanine, an FPR agonist peptide, rapidly induced EGFR phosphorylation at tyrosine residue (Tyr) 992, but not residues 846, 1068, or 1173, in glioblastoma cells, whereas all these residues were phosphorylated after only EGF treatment. The FPR agonist-induced EGFR phosphorylation in tumor cells was dependent on the presence of FPR as well as GAi proteins, and was controlled by Src tyrosine kinase. The transactivation of EGFR contributes to the biological function of FPR in glioblastoma cells because inhibition of EGFR phosphorylation significantly reduced FPR agonist-induced tumor cell chemotaxis and proliferation. Furthermore, depletion of both FPR and EGFR by short interference RNA abolished the tumorigenesis of the glioblastoma cells. Our study indicates that the glioblastoma-promoting activity of FPR is mediated in part by transactivation of EGFR and the cross-talk between two receptors exacerbates the malignant phenotype of tumor cells. Thus, targeting both receptors may yield antiglioblastoma agents superior to those targeting one of them. [Cancer Res 2007;67(12):5906-13]

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Lysophosphatidic acid induces $alpha;1B-adrenergic receptor phosphorylation through G$beta;$gamma;, phosphoinositide 3-kinase, protein kinase C and epidermal growth factor receptor transactivation

Cited by 30 publications

References 37 publications

Estrogens Cross-Talk to α_1b-Adrenergic Receptors

Estrogens Cross-Talk to α_1b-Adrenergic Receptors

Agonist-Induced Interactions between Angiotensin AT₁and Epidermal Growth Factor Receptors

Transactivation of the Epidermal Growth Factor Receptor by Formylpeptide Receptor Exacerbates the Malignant Behavior of Human Glioblastoma Cells

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Lysophosphatidic acid induces $alpha;1B-adrenergic receptor phosphorylation through G$beta;$gamma;, phosphoinositide 3-kinase, protein kinase C and epidermal growth factor receptor transactivation

Cited by 30 publications

References 37 publications

Estrogens Cross-Talk to α1b-Adrenergic Receptors

Estrogens Cross-Talk to α1b-Adrenergic Receptors

Agonist-Induced Interactions between Angiotensin AT1and Epidermal Growth Factor Receptors

Transactivation of the Epidermal Growth Factor Receptor by Formylpeptide Receptor Exacerbates the Malignant Behavior of Human Glioblastoma Cells

Contact Info

Product

Resources

About

Estrogens Cross-Talk to α_1b-Adrenergic Receptors

Estrogens Cross-Talk to α_1b-Adrenergic Receptors

Agonist-Induced Interactions between Angiotensin AT₁and Epidermal Growth Factor Receptors