TY  - JOUR
A1  - Henze, Andrea
A1  - Raila, Jens
A1  - Scholze, Alexandra
A1  - Zidek, Walter
A1  - Tepel, Martin
A1  - Schweigert, Florian J.
T1  - Does N-Acetylcysteine modulate post-translational modifications of transthyretin in hemodialysis patients?
JF  - Antioxidants & redox signaling
N2  - It is assumed that effects of the thiol antioxidant N-acetylcysteine (NAC) are mediated by interaction with protein-associated cysteine residues, however, information on protein level in vivo are missing. Therefore, we analyzed NAC-induced modifications of the protein transthyretin (TTR) in plasma of hemodialysis patients in a randomized, placebo-controlled study. TTR was selected due to its low molecular weight and the free cysteine residue in the polypeptide chain, which is known to be extensively modified by formation of mixed disulfides. The intravenous application of NAC during a hemodialysis session resulted in a substantial increase of native TTR from median 15% (range 8.8%-30%) to median 40% (37-50) and reduction of S-cysteinylated TTR [51% (44-60) vs. 6.6% (2.4-10)]. Additionally the pronounced formation of a TTR-NAC adduct was detected. However, all these modifications seemed to be reversible. Additionally, in vitro incubation of plasma with NAC confirmed the in vivo results and indicated that changes in post-translational modification pattern of TTR were a function of NAC concentration. Based on these observations and the essential metabolic and biochemical role of protein-associated cysteine residues we hypothesize that the interaction of NAC with proteins may explain altered protein functions due to modification of cysteine residues. Antioxid. Redox Signal. 19, 1166-1172.
Y1  - 2013
U6  - https://doi.org/10.1089/ars.2012.5125
SN  - 1523-0864
VL  - 19
IS  - 11
SP  - 1166
EP  - 1172
PB  - Liebert
CY  - New Rochelle
ER  -