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Human colon produces fully processed glucagon‐like peptide‐1 (7–36) amide
Author(s) -
Deacon Carolyn F.,
Johnsen Anders H.,
Holst Jens J.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00983-g
Subject(s) - proglucagon , peptide , chemistry , glucagon like peptide 2 , enteroendocrine cell , biochemistry , glucagon like peptide 1 , size exclusion chromatography , glucagon , peptide sequence , gastrointestinal hormone , amino acid , amide , chromatography , peptide hormone , microbiology and biotechnology , biology , endocrine system , gene , endocrinology , enzyme , hormone , type 2 diabetes , diabetes mellitus
The human colon contains many open‐type endocrine cells which express the preproglucagon gene and possess glucagon‐like peptide‐1 (GLP‐1) immunoreactivity, but the molecular form of the peptide is unknown. Acid ethanol extracts of human colon ( n = 4) were subjected to gel filtration and successive purification by high‐pressure liquid chromatography, monitored by specific RIAs. A single GLP‐1‐immunoreactive peak was isolated and identified as GLP‐1 (7–36)amide by amino acid sequence analysis and mass spectrometry. We conclude that proglucagon is processed in the large intestine in the same manner as in the small intestine, and results in the formation of fully processed biologically active GLP‐1.