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2003). Zinc release from MT, by displacement with cadmium or thiol oxidation by hydrogen peroxide, activates MTF-1. , 1999). Because of such strong interactions, free zinc ions are very potent cellular effectors and may have regulatory functions at protein sites. August 18, 2008 34 11:32 9in x 6in B-653 ch02 W. , 2001). , 1999). , 1999). , 2001; Haase and Maret, 2003). Fluctuations must occur with tight control to avoid unspecific reactions and cytotoxic effects of zinc ions. MT is the ideal candidate to exert such control.

Metal response element (MRE)-binding transcription factor-1 (MTF-1): Structure, function, and regulation. Antioxid Redox Signal 2001; 3:577–596. Haase H, Maret W. Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling. Exp Cell Res 2003; 291: 289–298. Haase H, Maret W. A differential assay for the reduced and oxidized states of metallothionein and thionein. Anal Biochem 2004; 333:19–26. Hao Q, Hong S-H, Maret W. Lipid raft-dependent endocytosis of metallothionein in HepG2 cells.

G. , 1992). , 1995), and in opposite order α > β with nitrilotriacetic acid (NTA) (Li and Otvos, 1998); on the other hand, bidentate ligands such as ethylenediaminediacetic acid and triethylenetetramine were found to be ineffective, even at thermodynamically competent concentrations. From these studies, it has been suggested that a tripod configuration of chelating ligands is required in thiolate substitution and that only specific regions of the protein domains may provide an easy access to the metal clusters.

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