Is the glutathione conjugate of trans-4-hydroxy-2-nonenal transported by the multispecific organic anion transporting-ATPase of human erythrocytes?

• Autorzy: Dygas A. , Makowski P. , Pikula S.
• Języki publikacji: EN

Abstrakty

EN

Trans-4-hydroxy-2-nonenal (4-HNE), a cytotoxic end product of lipid peroxidation, is present in normal human blood plasma at concentrations of 0.1-1.0 μM. It can be, however, further metabolized within a cell, and one of the main products is 4-HNE glutathione conjugate (HNE-SG). In human erythrocyte membrane the system for active extrusion of glutathione (GSH) conjugates of various endo- and xenobiotics has been described; it exhibits either a low (Km at submillimolar concentration range) or a high (Km at low micromolar range) affinity for the transported substrates, such as for example S-(2,4-dinitrophenyl)glutathione (Dnp-SG). In the present study it has been shown that the high affinity transport system for Dnp-SG is competitively inhibited by HNE-SG with Ki of 0.2 μM, while 4-HNE inhibits non-competitively the activity of the transport system for Dnp-SG with Ki of 220 μM. These observations point to the possibility that HNE-SG shares the same transport system with GSH conjugates of other endo- and xenobiotics in erythrocytes. This may be of importance for overall detoxification of the organism under oxidative stress.

Słowa kluczowe

EN

man; blood plasma; ATPase; erythrocyte; oxidative stress; glutathione; trans-4-hydroxy-2-nonenal; lipid peroxidation; anion transporter; cytotoxic product

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1998
• Tom: 45
• Numer: 1
• Opis fizyczny: p.59-65,fig.

Twórcy

autor

Dygas A.

• M.Nencki Institute of Experimental Biology, L.Pasteura 3, 02-093 Warsaw, Poland

autor

Makowski P.

autor

Pikula S.

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