par Sener, Abdullah 
;Malaisse Lagae, Francine ;Malaisse, Willy
Référence Proceedings of the National Academy of Sciences of the United States of America, 78, 9 II, page (5460-5464)
Publication Publié, 1981
;Malaisse Lagae, Francine ;Malaisse, Willy Référence Proceedings of the National Academy of Sciences of the United States of America, 78, 9 II, page (5460-5464)
Publication Publié, 1981
Article révisé par les pairs
| Résumé : | The leucine analog β-2-aminobicyclo[2.2.1]heptane-2-carboxylic acid (BCH) activates glutamate dehydrogenase [L-glutamate:NAD+ oxidoreductase (deaminating), EC 1.4.1.2] in pancreatic islet homogenates. In intact islets, BCH increased the islet content or output of HN4+, 2-ketoglutarate, malate, pyruvate, and alanine. BCH caused a dose-related increase in 14CO2 output from islets prelabeled with L-[U-14C]glutamine. BCH increased the islet content of ATP and stimulated both 45Ca net uptake and insulin release. The capacity of seven distinct amino acids to activate glutamate dehydrogenase tightly correlated with their ability to augment 14CO2 output from islets prelabeled with [U-14C]-glutamine and to stimulate insulin release in the presence of L-glutamine. The activation of glutamate dehydrogenase by BCH may thus account for the insulin-releasing capacity of the leucine analog. |
