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Research Article Free access | 10.1172/JCI107046

Glucagon-stimulating activity of 20 amino acids in dogs

Dalva Marreiro Rocha, Gerald R. Faloona, and Roger H. Unger

1Department of Internal Medicine, The University of Texas Southwestern Medical School at Dallas and Veterans Administration Hospital, Dallas, Texas 75216

Find articles by Rocha, D. in: PubMed | Google Scholar

1Department of Internal Medicine, The University of Texas Southwestern Medical School at Dallas and Veterans Administration Hospital, Dallas, Texas 75216

Find articles by Faloona, G. in: PubMed | Google Scholar

1Department of Internal Medicine, The University of Texas Southwestern Medical School at Dallas and Veterans Administration Hospital, Dallas, Texas 75216

Find articles by Unger, R. in: PubMed | Google Scholar

Published September 1, 1972 - More info

Published in Volume 51, Issue 9 on September 1, 1972
J Clin Invest. 1972;51(9):2346–2351. https://doi.org/10.1172/JCI107046.
© 1972 The American Society for Clinical Investigation
Published September 1, 1972 - Version history
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Abstract

The effect of 20 L-amino acids upon pancreatic glucagon secretion has been studied in conscious dogs. Each amino acid was administered intravenously over a 15 min period in a dose of 1 mmole/kg of body weight to a group of four or five dogs. Pancreatic glucagon and insulin were measured by radioimmunoassay. 17 of the 20 amino acids caused a substantial increase in plasma glucagon. Asparagine had the most glucagon-stimulating activity (GSA), followed by glycine, phenylalanine, serine, aspartate, cysteine, tryptophan, alanine, glutamate, threonine, glutamine, arginine, ornithine, proline, methionine, lysine, and histidine. Only valine, leucine, and isoleucine failed to stimulate glucagon secretion, and isoleucine may have reduced it. No relationship between glucagon-stimulating activity and insulin-stimulating activity was observed. The amino acids which enter the gluconeogenic pathway as pyruvate and, which are believed to provide most of the amino acid-derived glucose, had a significantly greater GSA than the amino acids which enter as succinyl CoA or as α-ketoglutarate. However, pyruvate itself did not stimulate glucagon secretion. The R-chain structure of the amino acid did not appear to be related to its GSA, except that the aliphatic branched chain amino acids, valine, leucine, and isoleucine, were devoid of GSA.

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