Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors

Katada, Toshiaki; Kurosu, Hiroshi; Okada, Taro; Suzuki, Takahiro; Tsujimoto, Noriko; Takasuga, Shunsuke; Kontani, Kenji; Hazeki, Osamu; Ui, Michio

doi:10.1016/s0009-3084(99)00020-1

Cited by 33 publications

(31 citation statements)

References 30 publications

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“…Results with inhibitors of tyrosine kinases indicate that no tyrosine kinases are implicated in the fMLP-mediated actin reorganization. Although it was reported that GPCR can intracellularly transactivate tyrosine kinase receptors (22,23), our findings along with the time course data indicate that FPR response is independent of tyrosine kinase receptors.…”

Section: Resultscontrasting

confidence: 62%

N-Formyl Peptide Receptor Ligation Induces Rac-dependent Actin Reorganization through Gβγ Subunits and Class Ia Phosphoinositide 3-Kinases

Belisle¹,

Abo²

2000

Journal of Biological Chemistry

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The N-formyl peptide receptor is a G protein-coupled transmembrane receptor involved in stimulating a variety of differential responses in neutrophils including chemotaxis, degranulation, superoxide production, transcriptional activation, and actin reorganization. Although it is known that N-formyl-Met-Leu-Phe induces actin reorganization, the sequence of events from the receptor to the actin cytoskeleton is not well characterized. To study the signaling pathway from the N-formyl peptide receptor to the actin cytoskeleton, we developed a model system utilizing microinjection techniques with a nonhematopoietic cell line. An expression vector coding for the N-formyl peptide receptor was microinjected into porcine aortic endothelial cells and stimulated with N-formyl-Met-Leu-Phe to induce actin reorganization and membrane ruffling. The receptor-mediated signal was blocked by pertussis toxin and by a dominant negative Rac-N17, indicating the involvement of G i ␣ subunit and the small guanosine triphosphatase Rac, respectively. Moreover, G␤␥ subunits and membrane targeted forms of phosphatidylinositol (PI) 3-kinase ␣ were sufficient to induce similar actin reorganization, and coexpression of various mutants of PI 3-kinase with the N-formyl peptide receptor identified a link to class Ia PI-3 kinase-mediated actin reorganization.

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Section: Resultscontrasting

confidence: 62%

N-Formyl Peptide Receptor Ligation Induces Rac-dependent Actin Reorganization through Gβγ Subunits and Class Ia Phosphoinositide 3-Kinases

Belisle¹,

Abo²

2000

Journal of Biological Chemistry

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“…However, the expression of dnPI3K (p110␣) in cardiomyocytes was sufficient to abolish the cardioprotective effects of ARIA deletion, indicating that the reduced cardiomyocyte death observed in ARIA Ϫ/Ϫ mice can largely be attributed to class IA PI3K (p110␣). This would be partially because cardioprotective proteins such as IGF-1 and neuregulin-1 predominantly activate receptor tyrosine kinases that subsequently activate class IA PI3K (40). Nevertheless, class IB PI3K may play a minor role in the cardioprotective effects of ARIA deletion.…”

Section: Discussionmentioning

confidence: 99%

Manipulation of Cardiac Phosphatidylinositol 3-Kinase (PI3K)/Akt Signaling by Apoptosis Regulator through Modulating IAP Expression (ARIA) Regulates Cardiomyocyte Death during Doxorubicin-induced Cardiomyopathy

Kitamura

Koide

Akakabe

et al. 2014

Journal of Biological Chemistry

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Background:The PI3K/Akt signaling regulates many aspects of cardiomyocyte homeostasis. Results: ARIA regulates cardiac PI3K/Akt signaling and modifies cardiomyocyte death and stress-induced cardiac dysfunction. Conclusion: ARIA is a novel factor involved in the regulation of cardiac PI3K/Akt signals. Significance: ARIA-mediated manipulation of cardiac PI3K/Akt signaling is an intriguing therapeutic target to treat cardiac dysfunction.

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“…Insulin signaling and G protein signaling have been reported to affect each other, suggesting crosstalks between these pathways (30). Moreover, at the whole-animal level, insulin sensitivity is augmented in guanine nucleotide-binding regulatory protein-deficient mice and reduced in G i -deficient animals (31,32).…”

Section: Effect Of Propionic Acid Is Modulated By Adenosine and Insulinmentioning

confidence: 99%

Short-chain fatty acids stimulate leptin production in adipocytes through the G protein-coupled receptor GPR41

Xiong

Miyamoto

Shibata

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

619

475

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Leptin is an adipose-derived hormone that regulates a wide variety of physiological processes, including feeding behavior, metabolic rate, sympathetic nerve activity, reproduction, and immune response. Circulating leptin levels are tightly regulated according to energy homeostasis in vivo. Although mechanisms for the regulation of leptin production in adipocytes are not well understood, G protein-coupled receptors may play an important role in this adipocyte function. Here we report that C2-C6 short-chain fatty acids, ligands of an orphan G protein-coupled receptor GPR41, stimulate leptin expression in both a mouse adipocyte cell line and mouse adipose tissue in primary culture. Acute oral administration of propionate increases circulating leptin levels in mice. The concentrations of short-chain fatty acids required to stimulate leptin production are within physiological ranges, suggesting the relevance of this pathway in vivo.

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Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors

Cited by 33 publications

References 30 publications

N-Formyl Peptide Receptor Ligation Induces Rac-dependent Actin Reorganization through Gβγ Subunits and Class Ia Phosphoinositide 3-Kinases

N-Formyl Peptide Receptor Ligation Induces Rac-dependent Actin Reorganization through Gβγ Subunits and Class Ia Phosphoinositide 3-Kinases

Manipulation of Cardiac Phosphatidylinositol 3-Kinase (PI3K)/Akt Signaling by Apoptosis Regulator through Modulating IAP Expression (ARIA) Regulates Cardiomyocyte Death during Doxorubicin-induced Cardiomyopathy

Short-chain fatty acids stimulate leptin production in adipocytes through the G protein-coupled receptor GPR41

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