Cellular transport of the glutamine analog acivicin does not require γ-glutamyl transpeptidase

L. M. Allen, A. A. Yunis

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Abstract

The possible significance of high levels of γ-glutamyl transpeptidase (γ-GT) to the cellular transport of acivicin (NSC 163501; AT-125) by human pancreatic carcinoma cells (MIA PaCa-2) in culture was studied. Acivicin could not be substituted for glycylglycine in the γ-GT assay whereas other amino acids, to varying degrees, could be (i.e. glutamine). Amino acids such as leucine, DL-bicyclohexane, and phenylalanine reduced cellular uptake of acivicin by 50%. Inhibitors of γ-GT, azaserine and dioxonorleucine, did not affect acivicin uptake. It was concluded that acivicin, an irreversible inhibitor of γ-GT, is predominantly translocated into MIA PaCa-2 cells by the L-amino acid preferring pathway. A secondary pathway is via the ASC-system.

Original languageEnglish (US)
Pages (from-to)125-126
Number of pages2
JournalIRCS Medical Science
Volume11
Issue number2
StatePublished - Jan 1 1983

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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