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Bradykinin-stimulated transient modulation of epidermal growth factor receptors in A-431 human epidermoid carcinoma cells by Kazuo Hosoi; Kinji Kurihara; Takao Ueha is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Of nine biological factors (ATP, bradykinin, vasopressin, substance P, angiotensin II, norepinephrine, epinephrine, 12‐tetradecanoylphorbol 13‐acetate (TPA), and A23187 calcium ionophore) examined, bradykinin, as well as ATP, TPA, and A23187, significantly increased the phosphorylation of epidermal growth factor (EGF) receptors and reduced the binding of EGF to their high‐affinity site. The reduction in EGF binding by bradykinin, ATP, and TPA was similarly reversed by concomitant incubation with staurosporine, a protein kinase C inhibitor, implying that the phosphorylation of EGF receptors was catalyzed probably by a protein kinase C of the same or similar type in each case. This possibility was confirmed by the fact that the major phosphorylation site of EGF receptors by the stimulation with either bradykinin, ATP or TPA was the same (Thi‐654). Different from the stimulations with ATP and TPA, the effect of bradykinin of decreasing the high‐affinity EGF binding was transient (a minimum binding at 2.5 min); the reduced EGF binding was, however, sustained for up to 30 min in the presence of calyculin A, a phosphoprotein phosphatase inhibitor. Moreover, the homogenate pre

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Author

Kazuo Hosoi; Kinji Kurihara; Takao Ueha

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0021-9541)

Published

1993

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)