Journal article

Molecular and Biochemical Characterization of a Unique Mutation in CCS, the Human Copper Chaperone to Superoxide Dismutase

Peter Huppke, Cornelia Brendel, Georg Christoph Korenke, Iris Marquardt, Anthony Donsante, Ling Yi, Julia D Hicks, Peter J Steinbach, Callum Wilson, Orly Elpeleg, Lisbeth Birk Moller, John Christodoulou, Stephen G Kaler, Jutta Gaertner

HUMAN MUTATION | WILEY-BLACKWELL | Published : 2012

Abstract

Copper (Cu) is a trace metal that readily gains and donates electrons, a property that renders it desirable as an enzyme cofactor but dangerous as a source of free radicals. To regulate cellular Cu metabolism, an elaborate system of chaperones and transporters has evolved, although no human Cu chaperone mutations have been described to date. We describe a child from a consanguineous family who inherited homozygous mutations in the SLC33A1, encoding an acetyl CoA transporter, and in CCS, encoding the Cu chaperone for superoxide dismutase. The CCS mutation, p.Arg163Trp, predicts substitution of a highly conserved arginine residue at position 163, with tryptophan in domain II of CCS, which inte..

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Grants

Awarded by Intramural Research Program of the US National Institutes of Health


Awarded by German Research Foundation


Awarded by CENTER FOR INFORMATION TECHNOLOGY


Awarded by EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT


Awarded by EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH &HUMAN DEVELOPMENT


Funding Acknowledgements

Intramural Research Program of the US National Institutes of Health (Project #HD008768-08) and the German Research Foundation (GA 354/9-1).