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

L. M. Allen, Adel A Yunis

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 - 1983

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acivicin
gamma-Glutamyltransferase
Glutamine
Amino Acids
Azaserine
Glycylglycine
Phenylalanine
Cell culture
Leucine
Assays
Cells

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Cellular transport of the glutamine analog acivicin does not require γ-glutamyl transpeptidase. / Allen, L. M.; Yunis, Adel A.

In: IRCS Medical Science, Vol. 11, No. 2, 1983, p. 125-126.

Research output: Contribution to journalArticle

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