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Pancreatic and intestinal processing of proglucagon in man

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We developed antisera and radioimmunoassays against synthetic replicas of glucagon-like peptide-1 (1-36) and -2, predicted products of the glucagon precursor, and against glucagon-like peptide-1 (7-36) identical to the sequence of glucagon-like peptide-1, but lacking its first six N-terminal amino acids. With these tools, we studied the localisation and molecular nature of glucagon-like immunoreactivity in human pancreas, small intestine and plasma. By immunohistochemistry glucagon-like peptide-1, and glucagon-like peptide-2 immunoreactivity coexisted with glucagon in pancreatic islet cells and with enteroglucagon in small intestinal enteroglucagon-producing cells. By chromatography of tissue extracts we found that glucagon-like peptide-1 and glucagon-like peptide-2-immunoreactivities in the human pancreas (307 +/- 51 and 107 +/- 37 pmol/g tissue) were mainly contained in a large peptide, whereas in the small intestine glucagon-like peptide-1 and glucagon-like peptide-2 immunoreactivities were found in separate smaller molecules (49 +/- 21 and 77 +/- 28/g tissue). By isocratic high pressure liquid chromatography of the large pancreatic glucagon-like peptide we found that this peptide is heterogeneous. By chromatographic analysis glucagon-like peptide-1 immunoreactivity in fasting plasma was mainly found in a large peptide corresponding to the pancreatic form, while after a meal a smaller molecular form coeluting by gel filtration with glucagon-like peptide-1 predominated.
OriginalsprogEngelsk
TidsskriftDiabetologia
Vol/bind30
Udgave nummer11
Sider (fra-til)874-81
Antal sider8
ISSN0012-186X
StatusUdgivet - nov. 1987

ID: 47488479