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Cyclic-AMP-dependent phosphorylation of glicentin.

J M Conlon, L Thim, A J Moody

Bioscience Reports

|June 1, 1984

Summary

Highly purified glicentin, a peptide related to glucagon, is phosphorylated by cyclic-AMP-dependent protein kinase. Glucagon itself and a smaller glicentin fragment were not phosphorylated, suggesting a specific site on glicentin is targeted.

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Area of Science:

Biochemistry
Molecular Biology
Endocrinology

Background:

Glicentin is a 69-amino-acid peptide found in the intestine, containing the complete glucagon sequence.
Glicentin is potentially biosynthetically related to glucagon.
Cyclic-AMP-dependent protein kinase plays a crucial role in cellular signaling pathways.

Purpose of the Study:

To investigate whether highly purified glicentin serves as a substrate for cyclic-AMP-dependent protein kinase.
To identify potential phosphorylation sites within glicentin.
To compare the phosphorylation of glicentin with related peptides like glucagon.

Main Methods:

A cell-free system was employed to study enzymatic reactions.
Highly purified glicentin was incubated with cyclic-AMP-dependent protein kinase.
Glicentin-related pancreatic peptide and glucagon were used as control substrates.

Main Results:

Highly purified glicentin was phosphorylated by cyclic-AMP-dependent protein kinase.
Glicentin-related pancreatic peptide (residues 1-30) and glucagon did not undergo phosphorylation under the same conditions.
The serine residue at position 34 of glicentin, within the Lys.Arg.His.Ser. sequence, is proposed as the likely phosphorylation site.

Conclusions:

Glicentin is a specific substrate for cyclic-AMP-dependent protein kinase.
The phosphorylation event likely occurs at serine 34 of glicentin.
These findings contribute to understanding the post-translational modification and potential function of glicentin.

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