Down-regulation of protein kinase C activity preferentially attenuates high K(+)-stimulated tyrosine hydroxylase activity in adrenal chromaffin cells cultured with insulin-like growth factor-I.

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 approximately 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.

journal_name

Neurosci Lett

journal_title

Neuroscience letters

authors

Dahmer MK

doi

10.1016/0304-3940(95)12144-7

subject

Has Abstract

pub_date

1995-12-08 00:00:00

pages

99-102

issue

2

eissn

0304-3940

issn

1872-7972

pii

0304-3940(95)12144-7

journal_volume

201

pub_type

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