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. 1986 Jul 1;237(1):277–279. doi: 10.1042/bj2370277

The polyamine-dependent modulation of phenylalanine hydroxylase phosphorylation state and enzymic activity in isolated liver cells.

M J Fisher, A J Dickson, C I Pogson
PMCID: PMC1146977  PMID: 3800881

Abstract

The role of polyamines in the control of phenylalanine hydroxylase phosphorylation state and enzymic activity was investigated. Pre-treatment of liver cells with spermine (1 mM) abolishes the glucagon (1 nM)-stimulated increase in hydroxylase phosphorylation. Concurrently there is a decrease in phenylalanine hydroxylation flux, reflecting decreased enzyme activity; 50% inhibition occurs at approx. 10 microM-spermine. These results are discussed in the context of reports concerning the properties of protein phosphatase 2A.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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