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N ‐acetyl‐L‐cysteine‐induced up‐regulation of HIV‐1 gene expression in monocyte‐derived macrophages correlates with increased NF‐κB DNA binding activity
Author(s) -
Nottet Hans S. L. M.,
Moelans Inge I. M. D.,
Vos N. Machiel,
Graaf Loek,
Visser Maarten R.,
Verhoef Jan
Publication year - 1997
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.61.1.33
Subject(s) - biology , microbiology and biotechnology , transfection , chloramphenicol acetyltransferase , electrophoretic mobility shift assay , hiv long terminal repeat , gene expression , monocyte , mutant , transcription factor , oligonucleotide , transcription (linguistics) , gene , nf κb , long terminal repeat , promoter , biochemistry , signal transduction , immunology , linguistics , philosophy
Nuclear factor κB (NF‐κB) is an important cellular regulator of human immunodeficiency virus (HIV) gene expression. In T cells, N ‐acetyl‐l‐cysteine (NAC) inhibits the induction of NF‐κB and transcription of HIV‐1. However, NAC up‐regulates HIV‐1 replication in monocyte‐derived macrophages (MDM). In this study we demonstrate that NAC treatment of MDM transfected with a chloramphenicol acetyltransferase (CAT) construct under transcriptional control of the HIV‐1 long terminal repeat resulted in an up‐regulation of CAT activity. Furthermore, MDM transfected with a HIV‐1‐NF‐κB‐CAT construct also produced increased CAT activity after NAC treatment. In addition, electrophoretic mobility shift assays revealed that nuclei of NAC‐treated MDM contained increased binding activity to wild‐type, but not mutant, κB oligonucleotides. Components of the binding activity were identified with antibodies as the NF‐κB subunits p50 and p65. These data indicate that NAC‐induced enhancement of HTV‐1 replication in MDM is regulated at the level of viral gene expression and mediated by NF‐κB. J. Leukoc. Biol . 61: 33–39; 1997.