A Cadmium Protein From Equine Kidney Cortex

Margoshes, Marvin; Vallée, Bert L.

doi:10.1021/ja01574a064

Cited by 1,234 publications

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“…Almost half a century ago, an unusual cadmium-binding protein was isolated from the horse kidney (1). Due to its high content of metals and cysteine residues, this protein was named metallothionein (MT) (2,3).…”

Section: Introductionmentioning

confidence: 99%

Metallothioneins and brain injury: What transgenic mice tell us

Hidalgo

2004

Environ Health Prev Med

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In rodents, the metallothionein (MT) family is composed of four members, MT-1 to MT-4. MT-1&2 are expressed in virtually all tissues including those of the Central Nervous System (CNS), while MT-3 (also called Growth Inhibitory Factor) and MT-4 are expressed prominently in the brain and in keratinizing epithelia, respectively. For the understanding of the physiological functions of these proteins in the brain, the use of transgenic mice has provided essential information. Results obtained in MT-1&2-null mice and in MT-1-overexpressing mice strongly suggest that these MT isoforms are important antioxidant, anti-inflammatory and antiapoptotic proteins in the brain. Results in MT-3-null mice show a very different pattern, with no support for MT-1&2-like functions. Rather, MT-3 could be involved in neuronal sprouting and survival. Results obtained in a model of peripheral nervous system injury also suggest that MT-3 could be involved in the control of nerve growth.

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Section: Introductionmentioning

confidence: 99%

Metallothioneins and brain injury: What transgenic mice tell us

Hidalgo

2004

Environ Health Prev Med

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“…Although it would seem that a protein as widespread as MT must play a biological role that is essential for the survival of organisms (Vallee, 1995), the function of MT has been a subject for debate since it was discovered 40 years ago (Margoshes & Vallee, 1957). One function often cited for MT is the detoxification of heavy metals, cadmium in particular.…”

Section: Introductionmentioning

confidence: 99%

“…TLVO domains are joined by a linker region, the N-terminal or P-domain binding three metal cations and the C-terminal or cy-domain binding four metal cations. Metallothioneins in invertebrate species also contain multiple cysteine side chains that bind metal cations.Although it would seem that a protein as widespread as MT must play a biological role that is essential for the survival of organisms (Vallee, 1995), the function of MT has been a subject for debate since it was discovered 40 years ago (Margoshes & Vallee, 1957). One function often cited for MT is the detoxification of heavy metals, cadmium in particular.…”

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Monitoring metal ion flux in reactions of metallothionein and drug‐modified metallothionein by electrospray mass spectrometry

et al. 1998

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The capabilities of electrospray ionization mass spectrometry are demonstrated for monitoring the flux of metal ions out of and into the metalloprotein rabbit liver metallothionein and, in one example, chlorambucil-alkylated metallothionein. Metal ion transfers may be followed as the reactions proceed in situ to provide kinetic information. More uniquely to this technique, metal ion stoichiometries may be determined for reaction intermediates and products. Partners used in these studies include EDTA, carbonic anhydrase, a zinc-bound hexamer of insulin, and the core domain of bacteriophage T4 gene 32 protein, a binding protein for single-stranded DNA.Keywords: acquired drug resistance; DNA binding protein; electrospray mass spectrometry; insulin; metal ion flux; metallothionein; stress response Metallothioneins (MT) comprise a family of small metal binding proteins that occurs widely throughout the animal kingdom. Plants and bacteria also produce types of metallothioneins. Vertebrate MTs share essentially the same structure (Kagi, 1993), with 20 cysteines coordinating seven divalent metal cations (Schultze et al., 1988; Robbins et al., 1991). TLVO domains are joined by a linker region, the N-terminal or P-domain binding three metal cations and the C-terminal or cy-domain binding four metal cations. Metallothioneins in invertebrate species also contain multiple cysteine side chains that bind metal cations.Although it would seem that a protein as widespread as MT must play a biological role that is essential for the survival of organisms (Vallee, 1995), the function of MT has been a subject for debate since it was discovered 40 years ago (Margoshes & Vallee, 1957). One function often cited for MT is the detoxification of heavy metals, cadmium in particular. However, the incidence of toxic concentrations of heavy metals in the environment is sporadic; thus, the need to detoxify heavy metals does not seem to account for the ability of virtually all living cells to synthesize metallothioneins transcriptionally or enzymatically (Steffens, 1990;

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“…Since its first recognition (12) as a cadmium-and zinc-containing protein in equine kidney, this protein has been purified from various sources, especially from parenchymatous tissues of vertebrates (8). Although the total metal content is constant, reaching 6-7 gram atoms per mole of the protein, the metal composition, however, is variable and depends on the tissue of origin and on the pretreatment of the animal with metals.…”

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confidence: 99%