Modulation of glutathione transferase P1-1 activity by retinoic acid in neuroblastoma cells

The ability of retinoic acid to modulate glutathione S‐transferase P1–1 (GSTP1–1) activity has important implications both for cancer prevention and for anticancer therapy. We investigated GSTP1–1 expression and activity in the human neuroblastoma cell line SK‐N‐BE(2) (genotype A*/B*) under basal co...

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Published in:Journal of cellular biochemistry 1999-12, Vol.75 (3), p.375-381
Main Authors: Bernardini, S., Melino, G., Cortese, C., Ballerini, S., Annicchiarico-Petruzzelli, M., Bernassola, F., Corazzari, M., Federici, G.
Format: Article
Language:English
Subjects:
Antineoplastic Agents - pharmacology
Base Sequence
DNA Primers - genetics
Gene Expression - drug effects
Glutathione S-Transferase pi
Glutathione Transferase - genetics
Glutathione Transferase - metabolism
glutathione transferase P1-1
Humans
Isoenzymes - genetics
Isoenzymes - metabolism
Kinetics
neuroblastoma
Neuroblastoma - drug therapy
Neuroblastoma - enzymology
Neuroblastoma - genetics
retinoic acid
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA, Neoplasm - genetics
RNA, Neoplasm - metabolism
Tretinoin - pharmacology
Tumor Cells, Cultured
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Summary:The ability of retinoic acid to modulate glutathione S‐transferase P1–1 (GSTP1–1) activity has important implications both for cancer prevention and for anticancer therapy. We investigated GSTP1–1 expression and activity in the human neuroblastoma cell line SK‐N‐BE(2) (genotype A*/B*) under basal conditions and during 48‐h incubation with 0.1 μM all‐trans‐retinoic acid. The steady‐state levels of glutathione transferase P1–1 mRNA and protein during 48‐h incubation with all‐trans‐retinoic acid did not increase substantially, but we detected a significant reduction of GSTP1–1 specific activity. This reduction in enzymatic activity could not be ascribed to a differential action of retinoic acid on the gene variants A* and B*; indeed, the two GSTP1–1 isoforms have different affinities toward 1‐chloro‐2,4‐dinitrobenzene (CDNB), while we found a substantial invariance of the Km CDNB in the cytosol during retinoid treatment. A modulatory effect of retinoic acid on other enzymes involved in glutathione transferase P1–1 metabolism, such as the retinoic acid‐induced tissue trans‐glutaminase, might be hypothesized, as well as a direct inactivation of GSTP1–1 by the oxidative stress that characterizes the early phases of apoptosis. J. Cell. Biochem. 75:375–381, 1999. © 1999 Wiley‐Liss, Inc.
ISSN:0730-2312
1097-4644
DOI:10.1002/(SICI)1097-4644(19991201)75:3<375::AID-JCB3>3.0.CO;2-I