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Calcium-dependent activation of glycogen phosphorylase in rat pheochromocytoma PC12 cells by nerve growth factor.

Abstract：

:Glycogen phosphorylase in PC12 cells exists in two forms analogous to those found in brain and muscle. The active phosphorylated form of the enzyme, phosphorylase-a, represents about 20-30% of total glycogen phosphorylase in these cells. Incubation of PC12 cells with 100 ng 7S nerve growth factor/ml increased phosphorylase-a within minutes. In contrast to nerve growth factor, insulin (6 ng/ml) and epidermal growth factor (6 ng/ml) decreased phosphorylase-a. Activation of phosphorylase-a by nerve growth factor was not accompanied by increases in cyclic AMP; however, removal of extracellular Ca2+ or incubation of cells with calcium channel blockers inhibited activation of glycogen phosphorylase by nerve growth factor.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Davis LH,Kauffman FC

doi

10.1016/s0006-291x(86)80583-6

subject

Has Abstract

pub_date

1986-07-31 00:00:00

pages

917-24

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(86)80583-6

journal_volume

138

pub_type

杂志文章

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