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Significance of γ‐glutamyl transpeptidase and thiols in amino acid uptake by rat pancreatic islets: Studies with glutamine and leucine
Author(s) -
Ammon H. P. T.,
Fuß A.,
Verspohl E. J.
Publication year - 1988
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290060409
Subject(s) - glutamine , leucine , amino acid , serine , biochemistry , glutathione , enzyme , chemistry , pancreatic islets , glutamine synthetase , biology , islet , endocrinology , insulin
The importance of γ‐glutamyl transpeptidase, the key enzyme of the γ‐glutamyl cycle and of thiols for the uptake of amino acids into rat pancreatic islets was investigated. Both serine–borate, an inhibitor of γ‐glutamy transpeptidase, and serine which does not inhibit this enzyme, but probabaly is a competitive inhibitor of amino acid uptake, inhibited of glutamine. The inhibitory effect of serine‐borate was not greater than that of serine alone. The uptake of glutamine was not affected by either GSH (reduced glutathione) or diamide (a thiol oxidant). Niether substances affected the uptake of leucine. The results indicate that the uptake of glutamine by rat pancreatic islets is not dependent on the functioning of γ‐glutamyl transpeptidase and that thiols are not important for the uptake of the amino acids glutamine and leucine.