SUMMARYThe effect of gut glucagon-like immunoreactivity (GLI) devoid of pancreatic glucagon was studied in piglets. All glucagon-like peptides with an accessible C-terminal were removed from the gut extract by specific antibodies reacting with the C-terminal of the glucagon molecule. Endogenous secretion of pancreatic and gut glucagon was blocked by somatostatin infusion, and then the purified gut glucagon preparation was infused. The latter prevented the hypoglycemia resulting from somatostatin infusion, and increased the glucagon level detectable by C-terminal specific antibodies in the blood of the animals. This rise was significant statistically from the 30th min of GLI administration (26.7 ± 7.2 pg/ml versus 137.0 ± 67.0 pg/ml; P < 0.05) and increased until the end of the infusion (90th min, 218 ± 60 pg/ml; P < 0.005). It has been suggested that, owing to the in vivo enzymatic degradation of the infused gut glucagon, biologically active "pancreatic" glucagon fractions are formed extracellularly. DIABETES 30:792-794, September 1981. R ecently data have been accumulated pointing to the similarities of pancreatic glucagon derived from the A-cells of the pancreas and the stomach, and enteric glucagon-like immunoreactivity (GLI) produced by the L-cells of the gut, and raising the possibility of a common biosynthetic precursor. One of the components of gut GLI, the 100-amino acid polypeptide, glicentin, has been shown to contain the full sequence of glucagon, extended from the C-terminus by an additional 8-amino acid chain and from the N-terminus by a 63 amino-acid chain.
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