Further investigations of the role of acetylation in ...



Title Further investigations of the role of acetylation in sulphonamide hypersensitivity reactions
Author(s) C. E. Nuss, D. M. Grant, S. P. Spielberg, Alastair E. Cribb
Journal Biomarkers
Date 1996
Volume 1
Issue 4
Start page 267
End page 272
Abstract Sulphonamide hypersensitivity reactions are believed to be mediated through reactive intermediates derived from oxidation of the para-amino group to form sulphonamide hydroxylamines. Sulphamethoxazole hydroxylamine (SMX-HA) can be acetylated by N-acetyltransferase (NAT) enzymes to form an acetoxy metabolite (acetoxySMX). In the current studies, acetoxySMX was found to be not toxic over the concentration range of 0 to 500 mu M towards a human lymphoblastoid cell line (RPMI 1788) or a human hepatoma cell line (HepG2). Further, transient expression of NAT1 in COS-1 cells or stable transfection of NAT1 and NAT2 in HepG2 cells did not alter the toxicity of SMX-HA in vitro. The activity of NAT1 in isolated mononuclear leucocytes (a reflection of systemic NAT1 activity) determined with para-aminobenzoic acid as a substrate was not different between controls (n = 11) or patients with a known hypersensitivity reaction (n = 5) (4.1 +/- 1.2 nmol min(-1) mg(-1) vs 5.7 +/- 1.4 nmol min(-1) mg(-1)). Thus, acetoxySMX is unlikely to play a significant role in mediating SMX hypersensitivity reactions and a constitutive deficiency in NAT1 activity is not a common finding in patients susceptible to SMX hypersensitivity reactions.

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