In vitro interaction of mercury, copper (II) and cadmium with human glutathione transferase pi.
The in vitro interaction of mercury, copper (II) and cadmium with human glutathione transferase (GST) pi was studied using reduced glutathione (GSH) and 1-chloro-2,4-dinitrobenzene as substrate. Tumor specific human GST pi was isolated from the human hepatoma derived PLC/PRF/5 cell line. The inhibition of the GST pi activity was dose dependent. Kinetic studies never revealed competitive inhibition. A parabolic inhibition was found with GSH as the variable substrate. The heavy metals are spontaneously conjugated with GSH and cysteine, but interact with GST pi by direct binding to this protein. This binding could have a protective function against heavy metals.
Almar
M M
MM
Instituut voor Hygiëne en Epidemiologie, Brussel, Belgium.
Dierickx
P J
PJ
D000818:Animals; D002104:Cadmium / Q000494:pharmacology*; D002478:Cells, Cultured; D003300:Copper / Q000494:pharmacology*; D003545:Cysteine / Q000494:pharmacology; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors*; D006801:Humans; D007700:Kinetics; D008114:Liver Neoplasms, Experimental / Q000201:enzymology; D008628:Mercury / Q000494:pharmacology*
D002104:Cadmium; D003300:Copper; D005982:Glutathione Transferase; D008628:Mercury; D003545:Cysteine