MinireviewThe biology of β-adrenergic receptors: Analysis in human epidermoid carcinoma A431 cells
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Cited by (16)
Src docks to A-kinase anchoring protein gravin, regulating β<inf>2</inf>-adrenergic receptor resensitization and recycling
2007, Journal of Biological ChemistryCitation Excerpt :The InStat statistics program (GraphPad, San Diego, CA) was used for statistical computations. Src Docks to the N-terminal Region (1–200) of AKAP Gravin—Human A431 epidermoid carcinoma cells were employed in this investigation as these cells display 35,000–50,000 β2AR/cell and provide a well studied model of agonist-stimulated receptor desensitization and trafficking (23), a hallmark of members of the superfamily of GPCRs (24). Earlier, it had been shown that inhibition of Src activity alters agonist-induced desensitization (15), whereas, little is known about a role of Src, if any, in resensitization and trafficking of GPCRs.
c-Src Tyrosine Kinase Binds the β2-Adrenergic Receptor via Phospho-Tyr-350, Phosphorylates G-protein-linked Receptor Kinase 2, and Mediates Agonist-induced Receptor Desensitization
2001, Journal of Biological ChemistryCitation Excerpt :To test the hypothesis that Src may be participating in events prior to receptor sequestration and Ras activation, we focused on an analysis of β2-adrenergic receptor-mediated activation and desensitization, using the accumulation of intracellular cyclic AMP as the readout. Human epidermoid A431 carcinoma cells are a widely used model of β2-adrenergic receptor action (18, 19). Challenging A431 cells with the β2-adrenergic agonist isoproterenol (10 μm) leads to peak accumulation of cyclic AMP at 5 min, which declines to approximately half-maximal levels within 30–60 min, reflecting ongoing agonist-induced desensitization (Fig. 1).
Cell-enlargement-related polypeptides are induced via β<inf>1</inf>-adrenoceptors in mouse parotids
2000, Experimental and Molecular PathologyThe β-adrenoceptors
1993, New Comprehensive Biochemistry