Mammalian metallothioneins: properties and functions

Metallomics ◽  
2012 ◽  
Vol 4 (8) ◽  
pp. 739 ◽  
Author(s):  
Petr Babula ◽  
Michal Masarik ◽  
Vojtech Adam ◽  
Tomas Eckschlager ◽  
Marie Stiborova ◽  
...  
Keyword(s):  
Mammalian Metallothioneins

Mammalian Metallothioneins

2012 ◽  
pp. 81-135
Author(s):  
Duncan Sutherland ◽  
Martin Stillman
Keyword(s):  
Mammalian Metallothioneins

scholarly journals Purification and properties of plaice metallothionein, a cadmium-binding protein from the liver of the plaice (Pleuronectes platessa)

1979 ◽  
Vol 183 (2) ◽  
pp. 277-283 ◽  
Author(s):  
J Overnell ◽  
T L Coombs
Keyword(s):  
Positive Reaction ◽  
Binding Protein ◽  
Periodic Acid ◽  
Molar Ratio ◽  
Amino Acid Residues ◽  
Thiol Groups ◽  
Single Chain ◽  
Periodic Acid Schiff ◽  
Pleuronectes Platessa ◽  
Mammalian Metallothioneins

A low-molecular-weight protein induced in the liver of the plaice (Pleuronectes platessa) by exposure to cadmium was purified and characterized. It is closely similar to mammalian metallothioneins in all of its properties in that it is a single-chain cadmium-binding protein of approx. 7000 mol.wt. with a high cysteine content (31 mol%) and no aromatic amino acid residues. The thiol groups of the cysteine residues complex with the cadmium in a SH/Cd molar ratio of 3:1 and produce a characteristic absorption maximum at 250 nm. Unlike the mammalian metallothioneins, however, metal analyses reveal only traces of zinc and copper in addition to cadmium. The presence of carbohydrate previously assumed from a positive reaction with periodic acid/Schiff reagent has now been disproved, and the positive reaction attributed to interaction with the thiol groups in the protein.

scholarly journals Metalloadsorption by Escherichia coliCells Displaying Yeast and Mammalian Metallothioneins Anchored to the Outer Membrane Protein LamB

1998 ◽  
Vol 180 (9) ◽  
pp. 2280-2284 ◽  
Author(s):  
Carolina Sousa ◽  
Pavel Kotrba ◽  
Tomas Ruml ◽  
Angel Cebolla ◽  
Víctor De Lorenzo
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Metal Binding ◽  
Wild Type ◽  
Lambda Phage ◽  
E Coli ◽  
Hybrid Proteins ◽  
Mammalian Metallothioneins

ABSTRACT Yeast (CUP1) and mammalian (HMT-1A) metallothioneins (MTs) have been efficiently expressed in Escherichia coli as fusions to the outer membrane protein LamB. A 65-amino-acid sequence from the CUP1 protein of Saccharomyces cerevisiae (yeast [Y] MT) was genetically inserted in permissive site 153 of the LamB sequence, which faces the outer medium. A second LamB fusion at position 153 was created with 66 amino acids recruited from the form of human (H) MT that is predominant in the adipose tissue, HMT-1A. Both LamB153-YMT and LamB153-HMT hybrids were produced in vivo as full-length proteins, without any indication of instability or proteolytic degradation. Each of the two fusion proteins was functional as the port of entry of lambda phage variants, suggesting maintenance of the overall topology of the wild-type LamB. Expression of the hybrid proteins in vivo multiplied the natural ability of E. colicells to bind Cd2+ 15- to 20-fold, in good correlation with the number of metal-binding centers contributed by the MT moiety of the fusions.

scholarly journals Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins

2017 ◽  
Vol 46 (24) ◽  
pp. 7683-7693 ◽  
Author(s):  
Elena Atrián-Blasco ◽  
Alice Santoro ◽  
Dean L. Pountney ◽  
Gabriele Meloni ◽  
Christelle Hureau ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Copper Metabolism ◽  
Biological Functions ◽  
Amyloidogenic Peptides ◽  
Mammalian Metallothioneins ◽  
And Oxidative Stress

Tutorial focusing on the chemistry of mammalian metallothioneins, important to understand its biological functions in zinc and copper metabolism, detoxification and oxidative stress.

scholarly journals Chemistry and biology of mammalian metallothioneins

2011 ◽  
Vol 16 (7) ◽  
pp. 1067-1078 ◽  
Author(s):  
Milan Vašák ◽  
Gabriele Meloni
Keyword(s):  
Mammalian Metallothioneins

scholarly journals Isolation and characterization of six human hepatic isometallothioneins

1985 ◽  
Vol 231 (2) ◽  
pp. 375-382 ◽  
Author(s):  
P E Hunziker ◽  
J H R Kägi
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Reversed Phase ◽  
Low Ph ◽  
Autopsy Material ◽  
Isolation And Characterization ◽  
Cysteine Content ◽  
Hepatic Metallothionein ◽  
Mammalian Metallothioneins

Human hepatic metallothionein (MT) was separated into six isoforms by using reversed-phase h.p.l.c. at the analytical and preparative levels. By comparison with the h.p.l.c. elution profiles of the charge-separable species MT-1 and MT-2 isolated by the procedure of Bühler & Kägi [(1974) FEBS Lett. 39, 229-234], five of these isoproteins are identified as hitherto unresolved subforms of MT-1, and one is identical with MT-2. The six isoforms have distinct and reproducible retention times at neutral pH, where the metal remains bound to the protein, and at low pH, where the metal is removed. Their amino acid compositions display the high cysteine content and the lack of aromatic amino acids and of histidine typical of mammalian metallothioneins, but they differ significantly with respect to all other amino acids. A survey of autopsy material indicates that in adult human liver all six isoforms are usually expressed, albeit in somewhat variable relative proportions.

scholarly journals Unravelling the mechanistic details of metal binding to mammalian metallothioneins from stoichiometric, kinetic, and binding affinity data

2018 ◽  
Vol 47 (11) ◽  
pp. 3613-3637 ◽  
Author(s):  
Judith S. Scheller ◽  
Gordon W. Irvine ◽  
Martin J. Stillman
Keyword(s):  
Binding Affinity ◽  
Metal Binding ◽  
Binding Constants ◽  
Equilibrium Binding ◽  
Mammalian Metallothioneins

Equilibrium binding constants are now readily accessible for metalation of metallothioneins.

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