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In Vitro Effects of γ-Glutamyltranspeptidase Inhibitor Acivicin on Human Myeloid and B Lineage Cells

  • Brigitte Bauvois
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 421)

Abstract

Gamma-glutamyltranspeptidase (γ-GT, EC 2.3.2.2) (Figure 1) is a widely distributed enzyme that acts as a transferase in the transfer of the γ-glutamyl group from a wide variety of peptide donors to other amino acids and peptide acceptors, and as a hydrolase in removing the γ-glutamyl residue from such peptides [1]. γ-GT activity was initially detected at the surface of human monocytes [2]. Using a spectrophotometric method, we showed it to be a sensitive assay of γ-GT activity detected on the surface of intact cells, as well as in highly purified cell membrane fractions. Cell-surface γ-GT (assayed with γ—Glu-para-nitroanilide as substrate and Gly-Gly as acceptor and abolished by the specific inhibitor of γ-GT i.e. acivicin) was confirmed in the myeloblastic (HL-60) and monoblastic (U937) cell lines [3]. Peripheral blood monocytes, granulocytes as well as macrophages developed in vitro from monocytes. were also found to exhibit γ-GT activity [3]. Another line of evidence that human myeloid cells express γ-GT was obtained from Northern blot analysis. In humans, there are at least four potential genes for γ-GT located on chromosome 22 [4]. Using a liver γ-GT probe, we have detected an mRNA species of 2.4 kb, corresponding to that previously described for the HepG2 cell line [5] in both cell lines and in granulocytes and macrophages [3]. Resting human B cells purified from blood as well as plasma cell lines (U266, RPMI 8226, Eskol) expressed γ-GT activity. However, no γ-GT transcripts were detected in any cells of the B lineage.

Keywords

U266 Cell Peripheral Blood Monocyte Vitro Effect Human Myeloid Cell Ectoenzyme Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Brigitte Bauvois
    • 1
  1. 1.UNITÉ 365 INSERMInstitut Curie, Section De RechercheParis Cedex 05France

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