Post-mortem and in vitro dimerization of metallothionein in cadmium-accumulated rat liver and kidney

Suzuki, Kazuo; Ohnuki, Riko; Yaguchi, Kumiko

doi:10.1016/0378-4274(83)90013-9

Cited by 15 publications

(9 citation statements)

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“…Summarizing the earlier literature available on MT multiple forms in Mytilus spp. and other bivalve species, with a particular emphasis on the molecular mass determination, we may notice that the majority of data are in accordance with the statement that dimeric forms of MTs, both in mammals and in invertebrates, were mostly produced in organisms either by oxidation following exposure to excess metal ions (Suzuki et al 1983), or by S-S bridge formation during the procedure of sample preparation (Minkel et al 1980). Later on, it has also been suggested that these oxidative mammalian MT products were not the same as the native dimeric species proposed to be in continuous reversible equilibrium with MT monomers (Otvos et al 1993).…”

Section: Discussionsupporting

confidence: 65%

Multiple forms of metallothionein from the digestive gland of naturally occurring and cadmium-exposed mussels, Mytilus galloprovincialis

Ivanković

Pavičić

Kozar

et al. 2002

Helgoland Marine Research

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Polymorphism of metallothioneins in the digestive gland of naturally occurring (control) and experimentally Cd-exposed mussels Mytilus galloprovincialis (200 µg Cd l -1 ; 14 days) was studied by applying the conventional methods of Sephadex column liquid chromatography , and by an electrochemical method (DPASV) for determination of Cd, Zn and Cu concentrations in chromatographic fractions. In both control and Cd-exposed mussels, two distinct molecular mass components of the metallothioneins, monomeric (MT-10) and dimeric (MT-20), were resolved by Sephadex G-75 gel filtration chromatography. In control mussels, the MT-10 component was predominantly expressed as containing markedly higher constitutive levels of Zn (100×) and Cu (10×) than of Cd. Each of these two molecular mass components was further resolved into seven metal-rich peaks by anion-exchange chromatography. In Cd-exposed mussels the larger proportion of Cd was bound to the MT-20 than to the MT-10 component, suggesting that the dimeric component may be considered as a primarily inducible metallothionein. The elution positions of metal-binding maxima of Cd-exposed and control mussels on the respective DEAE chromatographic profiles were comparable. A great similarity in elution positions of Cd maxima between the composite and single-specimen samples was also observed. Our study confirms a high multiplicity of MT forms in mussels from the Mytilus genus not only under the laboratory high-level metal exposure conditions, but also at a natural seawater metal exposure level. The ecotoxicological significance of dimeric and monomeric MT forms, as well as their possible application in the biomonitoring of seawater for trace metals, has been considered.

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Section: Discussionsupporting

confidence: 65%

Multiple forms of metallothionein from the digestive gland of naturally occurring and cadmium-exposed mussels, Mytilus galloprovincialis

Ivanković

Pavičić

Kozar

et al. 2002

Helgoland Marine Research

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“…metal release) and oxidation, whether occurring in vivo or during protein isolation, can lead to intermolecular disulphide bond formation. However, in vitro air oxidation leads to the formation of intramolecular disulphide bonds (Suzuki et al, 1983). Intermolecular bond formation reflects a propensity of MT to aggregate under certain conditions.…”

Section: Vol 221mentioning

confidence: 99%

“…The ability of MT to dimerize through disulphide linkages is well known (Suzuki & Yamamura, 1980;Suzuki et al, 1983), and higher-order polymers of MT have been postulated to function as neonatal Cu2+-binding proteins (Porter, 1974). Conditions of thiol exposure (i.e.…”

Section: Vol 221mentioning

confidence: 99%

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Chemical modifications of metallothionein. Preparation and characterization of polymers

Templeton¹,

Cherian²

1984

Biochemical Journal

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Reaction of rat liver metallothionein-II with two bifunctional cross-linking reagents, glutaraldehyde and dimethyl suberimidate, produces high yields of polymeric species. It is argued that cross-linking is trapping preformed aggregates of the protein, which therefore represent a stabilized quaternary structure of metallothionein. The two polymeric species differ in a number of respects. With dimethyl suberimidate, the polymer retains all metal-binding sites of the monomer, and has an unaltered isoelectric point. Reaction with glutaraldehyde causes loss of one or two Cd2+/Zn2+-binding sites and elevates the pI. Both species are nearly spherical aggregates, in contrast with the highly asymmetrical metallothionein. Both polymers are linked through lysine residues, and the thiol groups remain reduced. The biological significance of these aggregates is discussed.

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“…Nevertheless, several studies have detected in i o oxidative MT dimers after animals were exposed to high levels of Cd [21,22]. Other studies have shown that Cd, especially in the presence of MT, may play a role in production of reactive oxygen species resulting in oxidative stress [23][24][25].…”

Section: Introductionmentioning

confidence: 97%

Oxidative dimerization in metallothionein is a result of intermolecular disulphide bonds between cysteines in the α-domain

Zangger

Shen

Öz

et al. 2001

Biochemical Journal

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Upon storage under aerobic conditions metallothioneins (MTs) form a new species, which is characterized by a molecular mass approximately twice the size of monomeric MT and shifted ""$/"""Cd-and "H-NMR resonances. The investigation of this oxidative dimerization process by NMR spectroscopy allowed us to structurally characterize this MT species that has been described to occur in i o and might be synthesized under conditions of oxidative stress. The oxidative dimer was characterized by the formation of an intermolecular cysteine disulphide bond involving the α-domain, and a detailed analysis of chemical shift changes and intermolecular nuclear Overhauser effects points towards a disulphide bond involving Cys$'. In contrast to the metal-bridged (non-oxidative) dimerization, the metalcysteine cluster structures in both MT domains remain intact and

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Post-mortem and in vitro dimerization of metallothionein in cadmium-accumulated rat liver and kidney

Cited by 15 publications

References 4 publications

Multiple forms of metallothionein from the digestive gland of naturally occurring and cadmium-exposed mussels, Mytilus galloprovincialis

Multiple forms of metallothionein from the digestive gland of naturally occurring and cadmium-exposed mussels, Mytilus galloprovincialis

Chemical modifications of metallothionein. Preparation and characterization of polymers

Oxidative dimerization in metallothionein is a result of intermolecular disulphide bonds between cysteines in the α-domain

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