Differential Ca2+ Signaling Induced by Activation of the Epidermal Growth Factor and Nerve Growth Factor Receptors

Tinhofer, Ingeborg; Maly, Karl; Dietl, Paul; Hochholdinger, Franz; Mayr, Stefan; Obermeier, Axel; Grunicke, H.

doi:10.1074/jbc.271.48.30505

Cited by 38 publications

(31 citation statements)

References 42 publications

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“…However, this possibility can be ruled out, because the non-NMDA type glutamate receptor antagonist 6-cyano-7-nitroquinoxaline-2,3-dione, which is known to block glutamate-induced neurotrophin secretion, did not abolish neurotrophin secretion elicited by neurotrophins. Therefore, neurotrophin-induced secretion of neurotrophins is likely to be a direct consequence of Trk activation, which is known to activate phospholipase C-␥-1, leading to the formation of inositol 1,4,5 trisphosphate and calcium mobilization from the endoplasmic reticulum (57,58).…”

Section: Discussionmentioning

confidence: 99%

Neurotrophin release by neurotrophins: Implications for activity-dependent neuronal plasticity

Canossa

Griesbeck

Berninger

et al. 1997

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

242

209

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Neurotrophins, secreted in an activitydependent manner, are thought to be involved in the activitydependent refinement of synaptic connections. Here we demonstrate that in hippocampal neurons and the rat pheochromocytoma cell line PC12 application of exogenous neurotrophins induces secretion of neurotrophins, an effect that is mediated by the activation of tyrosine kinase neurotrophin receptors (Trks). Like activity-dependent secretion of neurotrophins, neurotrophin-induced neurotrophin secretion requires mobilization of calcium from intracellular stores. Because neurotrophins are likely to be released from both dendrites and axons, neurotrophin-induced neurotrophin release represents a potential positive feedback mechanism, contributing to the reinforcement and stabilization of synaptic connections.

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Section: Discussionmentioning

confidence: 99%

Neurotrophin release by neurotrophins: Implications for activity-dependent neuronal plasticity

Canossa

Griesbeck

Berninger

et al. 1997

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

242

209

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“…Activation of EGFR by EGF resulted in recruitment of various signaling components including the PLCg (Tinhofer et al, 1996), while G q -coupled receptors are linked to the stimulation of PLCb (Piiper et al, 1997). Both isoforms of PLC are capable of hydrolyzing PIP 2 into DAG and IP 3 , which in turn leads to PKC activation and Ca 2 þ release.…”

Section: Co-stimulation With Gpcr Agonists and Egf Did Not Co-operatementioning

confidence: 99%

Epidermal growth factor differentially augments G_i‐mediated stimulation of c‐Jun N‐terminal kinase activity

Chan

Wong

2004

British J Pharmacology

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1 Signaling networks involving different receptor systems allow extracellular signals to be integrated and transformed into various biological activities. In this report, we studied the activity of the c-Jun N-terminal kinase (JNK) subgroup of mitogen-activated protein kinases (MAPKs), in response to stimulation by G protein-coupled receptors (GPCRs) and co-activation with epithermal growth factor receptor (EGFR). 2 Stimulation of exogenous GPCRs in Cos-7 cells induced JNK activation of different magnitudes depending on their G-protein coupling specificities (G q 4G i 4G s ), and a moderate JNK activation was linked to stimulation of endogenous EGFR by EGF. 3 Co-stimulation with GPCR agonists and EGF resulted in differential augmentation of JNK activities, with G i -coupled receptors associated with a synergistic JNK activation upon co-stimulation with EGF, while G q -and G s -coupled receptors were incapable of triggering this effect. 4 This G i /EGF-induced synergistic JNK activation was inhibited by pertussis toxin and AG1478, and may involve Src family tyrosine kinases, PI3 K, Ca 2 þ /calmodulin and small GTPases as important intermediates, while Ca 2 þ mobilization was triggered by the stimulation of G q -coupled receptor or EGF treatment, but not by the G i -or G s -coupled receptors. 5 Transient expression of Gbg subunits with EGF treatment, or co-activation of exogenous G icoupled receptor with thapsigargin also resulted in a synergistic JNK activation. Activation of G icoupled receptor accompanied with EGF treatment enhanced the expression level and activity of MAPK phosphatase type I, which occurred after the maximal synergistic JNK activation. 6 Our results support a mechanistic model where EGF signaling may differentially regulate the JNK activities triggered by GPCRs of different coupling specificities.

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“…Calcium release from intracellular stores and store-operated calcium influx after treatment with the calcium ionophore A 23187 or bFGF were measured by single cell fluorescence technique employing fura-2 as previously described (Grynkiewicz et al, 1985;Tinhofer et al, 1996). Cells were grown on sterile slide covers for 24 h and labelled with 1 µM fura-2 for 30 min.…”

Section: Measurement Of Intracellular Calcium Concentrationsmentioning

confidence: 99%

Androgen receptor protein is down-regulated by basic fibroblast growth factor in prostate cancer cells

et al. 2000

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Interactions between polypeptide growth factors and the androgen receptor (AR) are important for regulation of cellular events in carcinoma of the prostate. Basic fibroblast growth factor (bFGF), the prototype of heparin-binding growth factors, and the AR are commonly expressed in prostate cancer. bFGF diminished prostate-specific antigen protein in the supernatants of androgen-stimulated human prostate cancer cells LNCaP by 80%. In the present study, we asked whether the bFGF effect on prostate-specific antigen is preceded by action on AR expression. LNCaP cells were treated with bFGF and AR protein expression was determined by immunoblotting and ligand binding assay. bFGF down-regulated AR protein in a dose-dependent manner showing a maximal effect at 50 ng ml −1 both in the presence or absence of dihydrotestosterone. Down-regulation of AR protein expression occurred already after 8 h of bFGF treatment and a maximal inhibition was observed 24 h after addition of bFGF to culture media. As AR expression can be reduced by an increase in intracellular calcium levels, we investigated whether the bFGF effect on AR protein is mediated by this mechanism. Calcium release from intracellular stores and store-operated calcium influx after treatment with either bFGF or calcium ionophore A 23187 were measured by single cell fluorescence technique. The ionophore A 23187 was able to induce calcium influx and an increase in cytoplasmic calcium concentration in LNCaP cells. In contrast, bFGF was incapable of eliciting a similar effect. In contrast to AR protein, AR mRNA levels were not affected by bFGF as shown by semiquantitative reverse transcription polymerase chain reaction. In summary, these studies show that bFGF is a potent negative regulator of AR protein expression in the human prostate cancer cell line LNCaP. © 2000 Cancer Research Campaign

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Differential Ca2+ Signaling Induced by Activation of the Epidermal Growth Factor and Nerve Growth Factor Receptors

Cited by 38 publications

References 42 publications

Neurotrophin release by neurotrophins: Implications for activity-dependent neuronal plasticity

Neurotrophin release by neurotrophins: Implications for activity-dependent neuronal plasticity

Epidermal growth factor differentially augments G_i‐mediated stimulation of c‐Jun N‐terminal kinase activity

Androgen receptor protein is down-regulated by basic fibroblast growth factor in prostate cancer cells

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Differential Ca2+ Signaling Induced by Activation of the Epidermal Growth Factor and Nerve Growth Factor Receptors

Cited by 38 publications

References 42 publications

Neurotrophin release by neurotrophins: Implications for activity-dependent neuronal plasticity

Neurotrophin release by neurotrophins: Implications for activity-dependent neuronal plasticity

Epidermal growth factor differentially augments Gi‐mediated stimulation of c‐Jun N‐terminal kinase activity

Androgen receptor protein is down-regulated by basic fibroblast growth factor in prostate cancer cells

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Epidermal growth factor differentially augments G_i‐mediated stimulation of c‐Jun N‐terminal kinase activity