Comparison of the effects of leucines, non-metabolizable leucine analogues and other insulin secretagogues on the activity of glutamate dehydrogenase

Gylfe, E.; Gylfe, E

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Comparison of the effects of leucines, non-metabolizable leucine analogues and other insulin secretagogues on the activity of glutamate dehydrogenase

Gylfe, E.

Acta Diabetologica Latina 13(1-2): 20-24

1976

ISSN/ISBN: 0001-5563

PMID: 987682

Accession: 005014037

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Summary

Glutamate dehydrogenase (GLDH) from bovine liver was employed in a model system for testing a possible role of GLDH in insulin release. The ability of different insulin secretagogues to stimulate the activity of the diethylstilbestrol-inhibited enzyme was tested. The 2 insulin-releasing amino acids, L-leucine and its non-metabolizable analogue 2-aminobicyclo(2,2,1)heptane-2-carboxylic acid [b(-)-BCH], were the best stimulators of GLDH activity. The non-secreting stereoisomers, D-leucine and b(+)-BCH, were less effective. Glucose, L-arginine and the leucine metabolite .alpha.-ketoisocaproic acid lacked significant effects on GLDH activity. Small and diverging effects were obtained with sulfonylurea compounds: whereas carbutamide caused slight stimulation, tolbutamide and glipizide had no effect, and glibenclamide was an inhibitor. The specificity of the insulin-releasing amino acids L-leucine and b(-)-BCH in stimulating GLDH activity makes it tempting to speculate about a connection between allosteric regulation of pyridine nucleotide-dependent enzymes and insulin release.

Comparison of the effects of leucines, non-metabolizable leucine analogues and other insulin secretagogues on the activity of glutamate dehydrogenase

Gylfe, E.

Acta Diabetologica Latina 13(1-2): 20-24

1976

Full-Text Article emailed within 1 workday

Summary

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