Pancreatic and intestinal processing of proglucagon in man
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Pancreatic and intestinal processing of proglucagon in man. / Holst, J J; Poulsen, Steen Seier.
I: Diabetologia, Bind 30, Nr. 11, 11.1987, s. 874-81.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Pancreatic and intestinal processing of proglucagon in man
AU - Holst, J J
AU - Poulsen, Steen Seier
PY - 1987/11
Y1 - 1987/11
N2 - 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.
AB - 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.
KW - Adult
KW - Amino Acid Sequence
KW - Chromatography, Gel
KW - Chromatography, High Pressure Liquid
KW - Gastrointestinal Hormones
KW - Glucagon
KW - Glucagon-Like Peptide 1
KW - Glucagon-Like Peptide 2
KW - Humans
KW - Ileum
KW - Intestine, Small
KW - Pancreas
KW - Pancreatic Hormones
KW - Peptides
KW - Proglucagon
KW - Protein Precursors
KW - Radioimmunoassay
M3 - Journal article
C2 - 3446554
VL - 30
SP - 874
EP - 881
JO - Diabetologia
JF - Diabetologia
SN - 0012-186X
IS - 11
ER -
ID: 47488479