Src-kinase-dependent epidermal growth factor receptor transactivation in salivary mucin secretion in response to β-adrenergic G-protein-coupled receptor activation

  title={Src-kinase-dependent epidermal growth factor receptor transactivation in salivary mucin secretion in response to $\beta$-adrenergic G-protein-coupled receptor activation},
  author={Bronislaw L. Slomiany and Amalia Slomiany},
The principal regulatory factors that control the flow and make-up of salivary secretion are neurotransmitters, released by parasympathetic and sympathetic innervation, that trigger activation of G protein-coupled receptors (GPCRs) on the acinar cells of salivary glands and stimulate the generation of soluble second messengers. In this study, we report that activation of GPCR by β-adrenergic agonist leading to stimulation in salivary mucin secretion occurs with the involvement of epidermal… 

Figures from this paper

Mitogen-activated protein kinase up-regulation and activation during rat parotid gland atrophy and regeneration: role of epidermal growth factor and beta2-adrenergic receptors.
Results support the view that cell proliferation is involved in duct ligation-induced atrophy of the rat parotid gland and gland recovery upon ligature removal, and up-regulation of ERKs and p38, and the activation of these MAPKs by up-regulated EGF and beta2-ARs, may be important signaling components underlying glandular atrophy and subsequent regeneration.
Characterization of the α 1 -Adrenoceptor Subtype Activating Extracellular Signal-Regulated Kinase in Submandibular Gland Acinar Cells
Results show only α 1B -adrenoceptors activate ERK1/2 and suggest subtype-specific ERK 1/2 signaling by α 1b - adrenoceptor may be determined by localization to cholesterol-rich microdomains in submandibular cells.
Transcription-Dependent Epidermal Growth Factor Receptor Activation by Hepatocyte Growth Factor
It is established that EGFR can be activated with functional consequences by HGF as a result of EGFR ligand expression, expanding the understanding of receptor tyrosine kinase signaling networks and may have considerable consequences for oncogenic mechanisms and cancer therapeutics.
RETRACTED ARTICLE: β adrenergic receptor modulated signaling in glioma models: promoting β adrenergic receptor-β arrestin scaffold-mediated activation of extracellular-regulated kinase 1/2 may prove to be a panacea in the treatment of intracranial and spinal malignancy and extra-neuraxial carcinoma
Generating compounds and targeted mutations of the β adrenergic receptor favoring β arrestin binding and scaffold facilitated activation of ERK1/2 may hold potential promise and therapeutic benefit in adjuvantly treating most or all cancers.
Étude du rôle de la tyrosine kinase Src dans la régulation de la signalisation des récepteurs opioïdes delta (∆OR)
The results show that pharmacological inhibition with PP2 or molecular inhibition of the kinase with low expression levels of a dominant negative mutant of Src potentiate the magnitude and duration of agonist-dependent activation of the ERK pathway and show that Src has a biphasic effect on ERK activity.
Conjugated bile acids promote ERK1/2 and AKT activation via a pertussis toxin–sensitive mechanism in murine and human hepatocytes
It is demonstrated that unconjugated bile acids activate hepatocyte receptor tyrosine kinases and intracellular signaling pathways in a ROS‐dependent manner and not in established rodent or human hepatoma cell lines.
The Growing Promiscuity of G Protein Coupled Receptors
There have now been several reports, including from the authors' own laboratory, that GPCR receptor transactivation can be reported from members of the protein tyrosine kinase family, including receptors for EGF, PDGF, IGF-1 and FGF.
Src redox regulation: again in the front line.


Gs Protein-coupled Receptor Agonists Induce Transactivation of the Epidermal Growth Factor Receptor in T84 Cells
GsPCR agonists rapidly transactivate the EGFr in T84 cells by a signaling pathway involving cAMP and PKA, through a mechanism that likely involves PI3K, which is required for the full expression of cAMP-dependent Cl- secretory responses.
Sensitization of Epidermal Growth Factor-induced Signaling by Bradykinin Is Mediated by c-Src
Communication between receptor tyrosine kinase (RTK)- and G protein-coupled receptor (GPCR)-mediated signaling systems has received increasing attention in recent years. Here, we report that
The β2-Adrenergic Receptor Mediates Extracellular Signal-regulated Kinase Activation via Assembly of a Multi-receptor Complex with the Epidermal Growth Factor Receptor*
GPCR activation mimics growth factor-mediated stimulation of the epidermal growth factor receptor (EGFR) with respect to many facets of RTK function, and RTK transactivation is revealed to be a process involving both association of receptors of distinct classes and the interaction of the transactivated RTK with the cells endocytic machinery.
c-Src Is Activated by the Epidermal Growth Factor Receptor in a Pathway That Mediates JNK and ERK Activation by Gonadotropin-releasing Hormone in COS7 Cells*
The unique pathway elucidated here in which c-Src and PI3K are sequentially activated downstream of the EGF receptor may serve as a prototype of signaling mechanisms by GnRHR and by additional GPCRs in various cell types.
Distinct Roles for Src Tyrosine Kinase in β2-Adrenergic Receptor Signaling to MAPK and in Receptor Internalization*
The data demonstrate that although Src and β-arrestin 2 play essential roles in β2-adrenergic receptor internalization, they are not required for the activation of the mitogen-activated protein kinase (MAPK) pathway by the β2+ receptor.
Src and Pyk2 Mediate G-protein-coupled Receptor Activation of Epidermal Growth Factor Receptor (EGFR) but Are Not Required for Coupling to the Mitogen-activated Protein (MAP) Kinase Signaling Cascade*
It is shown that Src kinases are critical for activation of Pyk2 in response to GPCR-stimulation and thatPyk2 and Src are essential for GPCr-induced tyrosine phosphorylation of EGFR, and that Pyk1, Src, and SRC are dispensable for G PCR-induced activation of MAP kinase.
Neurotransmitter Control of Secretion
  • B. Baum
  • Biology
    Journal of dental research
  • 1987
It is very well established that the principal control of salivary secretion is derived from autonomic innervation, which provides the intracellular signal for secretory events (protein, fluid, electrolyte secretion) to begin.
Dependence of Peroxisome Proliferator-activated Receptor Ligand-induced Mitogen-activated Protein Kinase Signaling on Epidermal Growth Factor Receptor Transactivation*
PPARα and γ ligands activate two distinct signaling cascades in GN4 cells leading to MAPK activation, suggesting a possible role for Pyk2 as an upstream activator of p38.
Role of adrenergic and cholinergic mediators in salivary phospholipids secretion.