Evidence That Glicentin Contains the Entire Sequence of Glucagon

Overview

Journal Biochem J

Specialty Biochemistry

Date 1980 May 1

PMID 6893148

Citations 35

Authors

J J Holst

Affiliations

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Abstract

Glicentin (a highly purified 100-amino acid peptide with glucagon-like immunoreactivity from porcine gut) was subjected to limited digestion with trypsin and carboxypeptidase B, and the resulting peptides were studied by gel filtration and region-specific glucagon radioimmunoassays. Similar digests of glucagon and purified fragments of glucagon were studied in parallel. Glicentin gave rise to peptides that corresponded closely to the 1-17 and 19-29 fragments of glucagon. Also, 125I-labelled glicentin and 125I-labelled glucagon gave rise to identical fragments after trypsin treatment. On the basis of this and other evidence [Jacobsen, Demandt, Moody & Sundby (1977) Biochim. Biophys. Acta 493, 452-459] it is concluded that glicentin contains the entire glucagon sequence at residues number 64-92 and thus fulfills one of the requirements for being a 'proglucagon'.

Citing Articles

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Discovery of the GI Effects of GLP-1: An Historical Perspective.

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Striking the Balance: GLP-1/Glucagon Co-Agonism as a Treatment Strategy for Obesity.

Hope D, Vincent M, Tan T Front Endocrinol (Lausanne). 2021; 12:735019.

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Proglucagon-Derived Peptides as Therapeutics.

Lafferty R, Oharte F, Irwin N, Gault V, Flatt P Front Endocrinol (Lausanne). 2021; 12:689678.

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Glucagon acutely regulates hepatic amino acid catabolism and the effect may be disturbed by steatosis.

Winther-Sorensen M, Galsgaard K, Santos A, Trammell S, Sulek K, Kuhre R Mol Metab. 2020; 42:101080.

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