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ACTH and brain membrane phosphorylation: a model for modulation by neuropeptides.

Acta Biologica Et Medica Germanica

|January 1, 1982

Summary

Adrenocorticotropic hormone (ACTH) influences brain phosphorylation, affecting synaptic transmission. This study identifies a calcium-dependent enzyme linking protein and lipid phosphorylation to regulate brain membrane ion permeability and peptide-induced behaviors.

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Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Synaptic transmission may be modulated by alterations in the phosphorylation of synaptic membrane proteins and lipids.
Neuropeptides, such as ACTH, are hypothesized to exert behavioral effects by influencing brain protein and lipid phosphorylation.

Purpose of the Study:

To review evidence linking neuropeptide ACTH to brain phosphorylation.
To isolate and characterize an ACTH-sensitive enzyme involved in synaptic membrane phosphorylation.
To elucidate the role of protein B-50 phosphorylation in lipid turnover and its implications for brain function.

Main Methods:

Isolation and partial characterization of an ACTH-sensitive, cAMP-independent protein kinase from rat brain synaptosomal plasma membranes.
Assay of enzyme activity in the presence and absence of calcium ions.
Investigation of the substrate protein B-50 and its role in phosphoinositide metabolism.

Main Results:

An ACTH-sensitive, calcium-dependent protein kinase was isolated.
The phosphorylation of substrate protein B-50 was found to regulate the conversion of diphosphoinositol to triphosphoinositol.
A model was proposed linking protein and lipid phosphorylation to peptide-mediated regulation of brain membrane calcium permeability.

Conclusions:

The identified neurochemical events, involving protein and lipid phosphorylation, are likely relevant to the biological activity of ACTH.
Peptide-induced alterations in ion permeability may modulate transynaptic information processing in the brain.
The B-50 protein's phosphorylation state is a key determinant in regulating phosphoinositide turnover and calcium ion flux.

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