scholarly journals Secretion of Gut GLI and Glicentin.

1995 ◽  
Vol 1 (2) ◽  
pp. 177-190 ◽  
Author(s):  
Akira OHNEDA
Keyword(s):  
Gut Gli

A Possible Role for Gut GLI: an Inhibitor of Lipolysis

1977 ◽  
Vol 9 (06) ◽  
pp. 465-469 ◽  
Author(s):  
Eva Krug ◽  
P. Mialhe
Keyword(s):  
Gut Gli

Evidence for the porcine pancreas containing and secreting a peptide related to glicentin (porcine gut GLI-1)

1980 ◽  
Vol 1 ◽  
pp. S77 ◽  
Author(s):  
A.J. Moody ◽  
J.J. Holst ◽  
L. Thim ◽  
S.Lindkær Jensen
Keyword(s):  
Porcine Pancreas ◽  
Gli 1 ◽  
Gut Gli

Release of Gut GLI by Luminal Hypotonicity

1981 ◽  
Vol 13 (08) ◽  
pp. 471-472 ◽  
Author(s):  
T. Matsuyama ◽  
M. Namba ◽  
K. Shima ◽  
K. Nonaka ◽  
S. Tarui
Keyword(s):  
Gut Gli

Sequence analysis of porcine GUT GLI-1

1977 ◽  
Vol 493 (2) ◽  
pp. 452-459 ◽  
Author(s):  
Henning Jacobsen ◽  
Anni Demandt ◽  
Alister J. Moody ◽  
Finn Sundby
Keyword(s):  
Sequence Analysis ◽  
Gli 1 ◽  
Gut Gli

PANCREATIC-GLUCAGON-LIKE IMMUNOREAGTIVITY AFTER INTRAVENOUS INSULIN IN NORMALS AND CHRONIC-PANCREATITIS PATIENTS

1971 ◽  
Vol 67 (2) ◽  
pp. 401-404 ◽  
Author(s):  
I. Persson ◽  
F. Gyntelberg ◽  
L. G. Heding ◽  
J. Boss-Nielsen
Keyword(s):  
Chronic Pancreatitis ◽  
Plasma Glucose ◽  
Normal Subjects ◽  
Insulin Injection ◽  
Normal Group ◽  
Pancreatic Glucagon ◽  
Intravenous Insulin ◽  
Gut Gli

Plasma glucose and pancreatic-glucagon-like immunoreactivity (GLI) were measured in normal subjects and in patients with chronic pancreatitis after an intravenous insulin injection. Both groups showed a fall of about 40 mg/100 ml in plasma glucose at from 0 to 30 minutes. In the normal group, the pancreatic GLI increased significantly above the 0-value at 30 and 60 minutes. No increase was observed in the pancreatitis patients. In all cases a decrease in gut GLI was observed during the test.

Elevated content and secretion of gut GLI in VMH-lesioned rats

1992 ◽  
Vol 29 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Makoto Naitoh ◽  
Shinobu Satoh ◽  
Tetsuya Kogawa ◽  
Katsuaki Tanaka ◽  
Shuji Inoue
Keyword(s):  
Elevated Content ◽  
Gut Gli

Characterization of Response of Gut GLI to Fat Ingestion in Dogs

2008 ◽  
Vol 16 (S 1) ◽  
pp. 105-109 ◽  
Author(s):  
A. Ohneda ◽  
T. Kobayashi ◽  
J. Nihei
Keyword(s):  
Gut Gli

scholarly journals The Enigmatic N-Terminal Domain of Proglucagon; A Historical Perspective

2021 ◽  
Vol 12 ◽  
Author(s):  
J. Michael Conlon
Keyword(s):  
Amino Acids ◽  
Erroneous Conclusion ◽  
Subsequent Work ◽  
Terminal Domain ◽  
C Terminus ◽  
Specific Antisera ◽  
Pancreatic Peptide ◽  
Insulin Radioimmunoassay ◽  
Gut Gli

Enteroglucagon refers to the predominant peptide with glucagon-like immunoreactivity (GLI) that is released by the intestine into the circulation in response to nutrients. Development of a radioimmunoassay for glucagon revealed issues that were not apparent in applications of the insulin radioimmunoassay. The fact that some antisera raised against glucagon recognized glucagon-related peptides in extracts of both pancreas and gut whereas others recognized only components in the pancreas remained a mystery until it was realized that the “gut GLI cross-reactive” antisera were directed against an epitope in the N-terminal to central region of glucagon whereas the “pancreatic glucagon specific” antisera were directed against an epitope in the C-terminal region. Unlike the cross-reactive antisera, the glucagon specific antisera did not recognize components in which glucagon was extended from its C-terminus by additional amino acids. Initial attempts to purify enteroglucagon from porcine ileum led to the erroneous conclusion that enteroglucagon comprised 100 amino acids with an apparent molecular mass of 12,000 Da and was consequently given the name glicentin. Subsequent work established that the peptide constituted residues (1-69) of proglucagon (Mr 8128). In the 40 years since the structural characterization of glicentin, attempts to establish an unambiguous physiological function for enteroglucagon have not been successful. Unlike the oxyntomodulin domain at the C-terminus of enteroglucagon, the primary structure of the N-terminal domain (glicentin-related pancreatic peptide) has been poorly conserved among mammals. Consequently, most investigations of the bioactivity of porcine glicentin may have been carried out in inappropriate animal models. Enteroglucagon may simply represent an inactive peptide that ensures that the intestine does not release equimolar amounts of a hyperglycemic agent (glucagon) and a hypoglycemic agent (GLP-1) after ingestion of nutrients.

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