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Mechanisms of amino acid-induced insulin secretion from the glucose-responsive BRIN-BD11 pancreatic B-cell line

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

McClenaghan, Neville, Barnett, CR, O'Harte, Finbarr and Flatt, Peter (1996) Mechanisms of amino acid-induced insulin secretion from the glucose-responsive BRIN-BD11 pancreatic B-cell line. JOURNAL OF ENDOCRINOLOGY, 151 (3). pp. 349-357. [Journal article]

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Abstract

The effects of different classes of amino acids known to be transported and utilized by pancreatic B-cells were examined using the novel glucose-responsive pancreatic B-cell line, BRIN-BD11. Amino acids tested included alpha-aminoisobutyric acid, L-alanine, L-arginine, L-glutamine, glycine, L-leucine, L-lysine, L-proline and L-serine. At non-stimulatory (1.1 mmol/l) glucose, acute incubations with either 1 or 10 mmol/l amino acid evoked 1.3- to 4.7-fold increases of insulin release. Raising glucose to 16.7 mmol/l enhanced the effects of all amino acids except L-glutamine, and increased insulin output at 10 mmol/l compared with 1 mmol/l amino acid. Glyceraldehyde (10 mmol/l) also served to promote 10 mmol/l amino acid-induced insulin secretion with the exceptions of L-arginine, glycine, L-lysine and L-proline. At 16.7 mmol/l glucose, diazoxide (300 mu mol/l) significantly decreased the secretory response to all amino acids except L-glutamine. Likewise, verapamil (20 mu mol/l) or depletion of extracellular Ca2+ reduced insulin output indicating the importance of Ca2+ influx in the actions of amino acids. These data indicate that BRIN-BD11 cells transport and utilize amino acids, acting in association with glycolysis, K+-ATP channels and/or voltage-dependent Ca2+ channels to promote Ca2+ influx and insulin secretion. The response of BRIN-BD11 cells to glucose and amino acids indicates that this is a useful cell line for future research on the mechanism of nutrient regulation of insulin secretion.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Diabetes
ID Code:3150
Deposited By:Professor Peter Flatt
Deposited On:08 Jan 2010 13:42
Last Modified:15 Jun 2011 11:10

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