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• W1966591878 abstract "The reactivity of Zn7- and Cd7-metallothionein (MT) with S-nitrosopenicillamine (SNAP), S-nitrosoglutathione (GSNO), and 2-(N,N-diethylamino)-diazenolate-2-oxide (DEA/NO) was investigated to explore the hypothesis that metallothionein is a signficant site of cellular reaction of nitric oxide or NO compounds. Zn7-MT reacted with SNAP or GSNO only under aerobic conditions and in the presence of light, which stimulates the decomposition of S-nitrosothiolates to NO. Zn2+ is released, and protein thiols are modified. DEA/NO, which degrades spontaneously to release NO, also reacted with Zn7-MT only when oxygen was present. Anaerobically, DEA/NO reacted with Zn7-MT in the presence of 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide, which converts NO to NO2. Glutathione competed effectively with Zn7-MT for reactive nitrogen oxide species in reaction mixtures. Reaction of Cd7-MT with SNAP also required oxygen and light to react. In this case, only a fraction of the Cd2+ bound to Cd7-MT was displaced by SNAP. Apo-metallothionein was much more reactive with SNAP and DEA-NO than Zn7- or Cd7-MT. TE671 and LLC-PK1 cell lines were incubated with DEA/NO to examine the role that MT might play in the cellular reactions of this NO donor compound. Incubation of cells with 0−80 μM Zn2+ for 24 h resulted in progressively increasing concentrations of Zn-unsaturated MT. One hour of cellular exposure to a range of DEA/NO concentrations followed by 24 h of incubation caused no evident acute toxicity at less than 0.45 mM. Preinduction of MT did not alter this response. The effects of DEA/NO on proteomic, metallothionein, and low molecular weight (LMW) thiol pools, including glutathione (GSH), were measured. Substantial fractions of the proteomic and LMW thiol pools underwent reaction with little dislocation of Zn2+. In addition, one-third of the MT thiol pool reacted without labilizing any of the bound Zn2+. These results demonstrated that it was free thiols associated with MT that reacted with DEA/NO not those bound to Zn2+. Moreover, under the conditions of the experiments, DEA/NO reacted with the spectrum of cellular thiols in proportion to their fraction in the cytosol and did not preferentially react with MT sulfhydryl groups." @default.
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• W1966591878 date "2010-01-19" @default.
• W1966591878 modified "2023-09-25" @default.
• W1966591878 title "Reactivity of Zn-, Cd-, and Apo-Metallothionein with Nitric Oxide Compounds: In Vitro and Cellular Comparison" @default.
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• W1966591878 doi "https://doi.org/10.1021/tx900387k" @default.
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