Reanalysis of the involvement of γ‐glutamyl transpeptidase in the cell activation process

FEBS Letters

Bauvois, Brigitte³  Antczak, Christophe³  London, Robert E¹  Karp, David R² 

[1] Laboratory of Structural Biology, MR-01, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA;Harold C. Simmons Arthritis Research Center, Department of Internal Medicine, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390, USA;Institut Curie, Section de Recherche, INSERM U365, 75248 Paris Cedex 05, France

关键词: Acivicin;    Apoptosis;    Differentiation;    Ectoprotease;    Proliferation;    Signaling;    γ-GT;    γ-glutamyl transpeptidase;    γ-Glu-pNA;    L-γ-glutamyl-para-nitroaniline;    GlyGly;    glycylglycine;    FCS;    fetal calf serum;    pNA;    para-nitroaniline;    L-ABBA;    L-2-amino-4-boronobutanoic acid;    APN;    aminopeptidase N;    MAPK;    mitogen-activated protein kinase;   

DOI  :  10.1016/S0014-5793(01)03057-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The inhibitor of γ-glutamyl transpeptidase (γ-GT) acivicin modulates cellular responses including growth, myeloid maturation and apoptosis. Whether these effects result from the inhibition of γ-GT enzyme activity remains unclear. We compared the cellular effects of acivicin against a more potent and specific inhibitor of γ-GT (L-2-amino-4-boronobutanoic acid (L-ABBA)) in γ-GT-negative (B lymphoblastoid Ramos) and γ-GT-positive (myelomonocytic HL-60, γ-GT-transfected Ramos) cell lines. Under non-oxidative stress conditions, acivicin-induced cell growth arrest, apoptosis and macrophage maturation occurred independent of γ-GT while L-ABBA did not influence any of these processes. Acivicin triggered tyrosine phosphorylation and increased nuclear factor κB activity. Further insight into the role of γ-GT in cellular processes is needed.

【 授权许可】

Unknown