Tissue and plasma concentrations of amidated and glycine-extended glucagon-like peptide I in humans
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Tissue and plasma concentrations of amidated and glycine-extended glucagon-like peptide I in humans. / Orskov, C; Rabenhøj, L; Wettergren, A; Kofod, Hans; Holst, J J.
In: Diabetes, Vol. 43, No. 4, 04.1994, p. 535-9.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Tissue and plasma concentrations of amidated and glycine-extended glucagon-like peptide I in humans
AU - Orskov, C
AU - Rabenhøj, L
AU - Wettergren, A
AU - Kofod, Hans
AU - Holst, J J
PY - 1994/4
Y1 - 1994/4
N2 - Using specific radioimmunoassays, we studied the occurrence of amidated and glycine-extended glucagon-like peptide I (GLP-I) molecules in the human small intestine and pancreas and in the circulation system in response to a breakfast meal. Through gel permeation chromatography of extracts of the human pancreas (n = 5), we found that 71% of the GLP-I immunoreactivity eluted as a large molecule corresponding to the major proglucagon fragment, 24% corresponded to GLP-I 1-36 amide, and 5% to GLP-I 1-37. By gel permeation chromatography of extracts of human small intestine (n = 6), we found that all immunoreactivity eluted in one peak at the common elution position of the two insulin-releasing peptides, GLP-I 7-36 amide and GLP-I 7-37. Of the GLP-I immunoreactivity, 80% corresponded to GLP-I 7-36 amide and 20% to GLP-I 7-37. The mean concentrations of amidated GLP-I and glycine-extended GLP-I in fasting plasma were 7 +/- 1 and 6 +/- 1 pM, respectively (n = 6). In response to a breakfast meal, the concentration of amidated GLP-I rose significantly amounting to 41 +/- 5 pM 90 min after the meal ingestion, whereas the concentration of glycine-extended GLP-I only rose slightly to a maximum of 10 +/- 1 pM. Thus, both amidated and glycine-extended GLP-I molecules are produced in the small intestine and in the pancreas in humans. Both amidated and glycine-extended GLP-I are measurable in fasting plasma.(ABSTRACT TRUNCATED AT 250 WORDS)
AB - Using specific radioimmunoassays, we studied the occurrence of amidated and glycine-extended glucagon-like peptide I (GLP-I) molecules in the human small intestine and pancreas and in the circulation system in response to a breakfast meal. Through gel permeation chromatography of extracts of the human pancreas (n = 5), we found that 71% of the GLP-I immunoreactivity eluted as a large molecule corresponding to the major proglucagon fragment, 24% corresponded to GLP-I 1-36 amide, and 5% to GLP-I 1-37. By gel permeation chromatography of extracts of human small intestine (n = 6), we found that all immunoreactivity eluted in one peak at the common elution position of the two insulin-releasing peptides, GLP-I 7-36 amide and GLP-I 7-37. Of the GLP-I immunoreactivity, 80% corresponded to GLP-I 7-36 amide and 20% to GLP-I 7-37. The mean concentrations of amidated GLP-I and glycine-extended GLP-I in fasting plasma were 7 +/- 1 and 6 +/- 1 pM, respectively (n = 6). In response to a breakfast meal, the concentration of amidated GLP-I rose significantly amounting to 41 +/- 5 pM 90 min after the meal ingestion, whereas the concentration of glycine-extended GLP-I only rose slightly to a maximum of 10 +/- 1 pM. Thus, both amidated and glycine-extended GLP-I molecules are produced in the small intestine and in the pancreas in humans. Both amidated and glycine-extended GLP-I are measurable in fasting plasma.(ABSTRACT TRUNCATED AT 250 WORDS)
KW - Adult
KW - Chromatography, Gel
KW - Eating
KW - Fasting
KW - Female
KW - Glucagon
KW - Glucagon-Like Peptide 1
KW - Humans
KW - Immunohistochemistry
KW - Intestine, Small
KW - Male
KW - Middle Aged
KW - Pancreas
KW - Peptide Fragments
KW - Proglucagon
KW - Protein Precursors
KW - Protein Processing, Post-Translational
M3 - Journal article
C2 - 8138058
VL - 43
SP - 535
EP - 539
JO - Diabetes
JF - Diabetes
SN - 0012-1797
IS - 4
ER -
ID: 45574294