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Inne
Effects of divalent metal ions on the αB-crystallin chaperone-like activity: spectroscopic evidence for a complex between copper(II) and protein.
Autorzy
Rok wydania
2004
Czasopismo
Journal of Inorganic Biochemistry
Numer woluminu
98
Strony
1103-1109
DOI
10.1016/j.jinorgbio.2004.03.013
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
αB-crystallin is a small heat shock protein, showing chaperone-like activity, that is expressed in the lens and in several other tissues. The role of some metal ions in the αB-crystallin biology starts to be well documented. In some neuro-degenerative pathologies, like Parkinson and Alzheimer's diseases, αB-crystallin is expressed at high levels. In the same pathologies an accumulation of divalent metal cations is observed. In order to investigate the interactions between human αB-crystallin and divalent metal ions, the effect of copper, zinc and calcium on the chaperone-like activity of the protein has been studied. Copper and zinc at concentrations 0.1 and 1 mM significantly increase the chaperone-like activity, whereas calcium 1 mM completely inhibits activity. Electron paramagnetic resonance (EPR) and circular dichroism (CD) spectra indicate the possible complex formation between Cu(II) and protein at physiological pH. Molecular modeling calculations, carried out for the probable Cu(II) binding site, suggest that a complex with three histidine residues is possible.
Słowa kluczowe
αB-crystallin, Metal complexes, Chaperone-like activity
Adres publiczny
https://doi.org/10.1016/j.jinorgbio.2004.03.013
Strona internetowa wydawcy
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