Abstract
The purpose of this study was to determine whether the loss of protein kinase C (PKC) from adrenal chromaffin cells affected the enhancement of high K +- and forskolin-stimulated tyrosine hydroxylase (tyrosine 3-monooxygenase, EC 1.14.16.2) activity observed in cells treated with insulin-like growth factor-I (IGF-I). Forskolin-stimulated tyrosine hydroxylase activation was not affected by down-regulation of PKC. High K +-stimulated tyrosine hydroxylase activity decreased substantially after treating the cells for ∼18 h with active, but not inactive, phorbol ester (300 nM). After down-regulation of PKC, high K +-stimulated tyrosine hydroxylase activity in cells cultured with IGF-I decreased by 61 ± 5% ( n = 14) compared to 36 ± 8% ( n = 14) in cells cultured without IGF-I. These data suggest that PKC is required for the enhancement of high K +-stimulated tyrosine hydroxylase activity observed with IGF-I treatment.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
