Abstract
We have previously1 isolated from porcine small intestine a peptide known as glicentin. The C-terminal portion of glicentin consists of the sequence of glucagon extended at its C terminus by an octapeptide2,3, and differs slightly from the sequence of a proposed fragment of proglucagon4. Glicentin-like material has been demonstrated in the pancreatic A cell5,6, wherein it is located in the periphery of the secretory granules7, whereas glucagon is located in the centre of the granules. To study the relationship of glicentin to the biosynthesis of glucagon, we have now investigated the glucagon-like and glicentin-like peptides in extracts8 and perfusates of the porcine pancreas. Our findings that a peptide with glicentin-like immunoreactivity, and intermediate in size between glicentin and glucagon, is secreted synchronously with glucagon suggest that this glicentin-related peptide is a major cleavage product of proglucagon.
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References
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Moody, A., Holst, J., Thim, L. et al. Relationship of glicentin to proglucagon and glucagon in the porcine pancreas. Nature 289, 514–516 (1981). https://doi.org/10.1038/289514a0
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DOI: https://doi.org/10.1038/289514a0
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