Crosstalk between angiotensin II and platelet derived growth factor-BB mediated signal pathways in cardiomyocytes

Wang, Cheng; Wu, Li‐Ling; Liu, Jie; Zhang, Zhiguo; Fan, Dong; Li, Li

doi:10.1097/00029330-200802010-00010

Cited by 16 publications

(10 citation statements)

References 14 publications

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“…Usually this has been thought of in terms of activation of the growth factor receptors following GPCR stimulation (23,40,75). Recently, Wang et al (78) demonstrated signaling through the angiotensin type I receptor (AT1R) activates the PDGFR␤-dependent signaling cascade. However, all of these studies imply a one-way activation of RTK signaling cascades following GPCR stimulation.…”

Section: Discussionmentioning

confidence: 99%

“…We are interested in the possibility that PDGF might regulate RGS5 expression because RGS5 and the PDGF-R␤ are expressed in pericytes, which function to stabilize neovasculature (7,12,13,21,53). The effect of PDGF upon a GPCR-mediated pathway is not unexpected because there is growing evidence of cross-talk between GPCRs and receptor tyrosine kinases (RTKs) (40,54,78,81). Treatment of VSMCs with PDGF-BB resulted in the immediate and sustained downregulation of RGS5 expression (Fig.…”

Section: Agonist-dependent Regulation Of Rgs5 Expressionmentioning

confidence: 99%

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PDGF-dependent regulation of regulator of G protein signaling-5 expression and vascular smooth muscle cell functionality

Gunaje¹,

Bahrami²,

Schwartz³

et al. 2011

American Journal of Physiology-Cell Physiology

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Regulator of G protein signaling (RGS) proteins, and notably members of the RGS-R4 subfamily, control vasocontractility by accelerating the inactivation of Gα-dependent signaling. RGS5 is the most highly and differently expressed RGS-R4 subfamily member in arterial smooth muscle. Expression of RGS5 first appears in pericytes during development of the afferent vascular tree, suggesting that RGS5 is a good candidate for a regulator of arterial contractility and, perhaps, for determining the mass of the smooth muscle coats required to regulate blood flow in the branches of the arterial tree. Consistent with this hypothesis, using cultured vascular smooth muscle cells (VSMCs), we demonstrate RGS5 overexpression inhibits G protein-coupled receptor (GPCR)-mediated hypertrophic responses. The next objective was to determine which physiological agonists directly control RGS5 expression in VSMCs. GPCR agonists failed to directly regulate RGS5 mRNA expression; however, platelet-derived growth factor (PDGF) acutely represses expression. Downregulation of RGS5 results in the induction of migration and the activation of the GPCR-mediated signaling pathways. This stimulation leads to the activation of mitogen-activated protein kinases directly downstream of receptor stimulation, and ultimately VSMC hypertrophy. These results demonstrate that RGS5 expression is a critical mediator of both VSMC contraction and potentially, arterial remodeling.

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Section: Discussionmentioning

confidence: 99%

Section: Agonist-dependent Regulation Of Rgs5 Expressionmentioning

confidence: 99%

PDGF-dependent regulation of regulator of G protein signaling-5 expression and vascular smooth muscle cell functionality

Gunaje¹,

Bahrami²,

Schwartz³

et al. 2011

American Journal of Physiology-Cell Physiology

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“…Since c-Src has been shown to be a necessary component in various instances of transactivation (Kruk et al, 2013b;Tanimoto et al, 2004;Yano et al, 2007), this latter tyrosine residue may be important in the desensitization mechanism. An additional candidate for inducing desensitization is PKC, which has been shown to feed back to regulate activity of upstream components of its signaling pathway such as PLC and both enzymes are necessary components of transactivation pathways (Kruk et al, 2013b;Wang et al, 2008). Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Although required for central nervous system development (Alvarez et al, 2006), PDGF receptor signaling has been shown to be neuroprotective after ischemic or excitotoxic insults in developed neurons (Beazely et al, 2009;Sakata et al, 1998;Vasefi et al, 2013). In addition to ligand-induced activation of PDGF receptors, several GPCR agonists including angiotensin II (Heeneman et al, 2000;Wang et al, 2008), dopamine (Oak et al, 2001), endothelin (Gomez Sandoval and Anand-Srivastava, 2011), sphingosine-1-phosphate (Tanimoto et al, 2004), lysophosphatidic acid (Goppelt-Struebe et al, 2000;Wang et al, 2003), and leukotrienes (McMahon et al, 2002) can induce a PDGF-independent PDGF receptor activation, a process known as transactivation. We have recently shown that 5-HT can transactivate PDGFβ receptors in neurons and have elucidated many of the components of this pathway: 5-HT binds Gα i -coupled (and possibly Gα q -coupled) 5-HT receptors, leading to PLC-and calciumdependent PKC activity, and NADPH oxidase that mediates the production of low concentrations of reactive oxygen species (Kruk et al, 2013a(Kruk et al, , 2013b.…”

Section: Contents Lists Available At Sciencedirectmentioning

confidence: 99%

Fluoxetine-induced transactivation of the platelet-derived growth factor type β receptor reveals a novel heterologous desensitization process

Kruk

Vasefi

Gondora

et al. 2015

Molecular and Cellular Neuroscience

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“…42,43 TbRI demonstrates strong serine phosphorylation activity; however, it also is known to express weak tyrosine kinase activity and is correctly identified as a dual specificity kinase. 18,19,44,45 Thus, although TbRI serine phosphorylates Smad proteins in their extreme carboxy termini, it also phosphorylates tyrosine (as well as serine) residues on Shc.…”

Section: Discussionmentioning

confidence: 99%

Endothelin-1 Stimulation of Proteoglycan Synthesis in Vascular Smooth Muscle is Mediated by Endothelin Receptor Transactivation of the Transforming Growth Factor-β Type I Receptor

Little

Burch

Getachew

et al. 2010

Journal of Cardiovascular Pharmacology

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We utilized human vascular smooth muscle cells to address the question if a G-protein-coupled receptor, the endothelin (ET) receptor, could transactivate a serine/threonine kinase receptor, specifically the transforming growth factor (TGF)-[beta] receptor, T[beta]RI. Functionality of the interaction was addressed by studying endothelin-1-stimulated proteoglycan synthesis. Signaling molecules were assessed by Western blotting and proteoglycan synthesis by [35S]sulfate and 35S-met/cys incorporation and molecular size by SDS-PAGE. Endothelin-1 treatment led to a time- and concentration-dependent increase in cytosolic phosphoSmad2C, which was inhibited by the mixed endothelin receptor antagonist bosentan and the T[beta]RI antagonist SB431542. Endothelin-1 treatment led to a time-dependent increase in nuclear phosphoSmad2C. Endothelin-1-stimulated proteoglycan synthesis was partially inhibited (40%) by SB431542 and completely blocked by bosentan. The effect of endothelin-1 to stimulate an increase in glycosaminoglycan size on biglycan was also blocked in a concentration-dependent manner by SB431542. These data extend the current paradigm of G-protein coupled receptor signaling to include the transactivation of the serine kinase receptor for TGF-[beta] (T[beta]RI). This response should be considered in the context of response to endothelin-1, and the options for therapeutically targeting endothelin-1 are accordingly broadened to include downstream signaling otherwise associated with TGF-[beta] receptor activation.

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Crosstalk between angiotensin II and platelet derived growth factor-BB mediated signal pathways in cardiomyocytes

Cited by 16 publications

References 14 publications

PDGF-dependent regulation of regulator of G protein signaling-5 expression and vascular smooth muscle cell functionality

PDGF-dependent regulation of regulator of G protein signaling-5 expression and vascular smooth muscle cell functionality

Fluoxetine-induced transactivation of the platelet-derived growth factor type β receptor reveals a novel heterologous desensitization process

Endothelin-1 Stimulation of Proteoglycan Synthesis in Vascular Smooth Muscle is Mediated by Endothelin Receptor Transactivation of the Transforming Growth Factor-β Type I Receptor

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