Cloning and mapping of murine superoxide dismutase copper chaperone (Ccsd)and mapping of the human ortholog

Copper does not exist in a free state within cells but is found consistentl y bound to metalloproteins. Specific metallochaperones escort copper to num erous targets within the cell, providing protection from the toxic effects of intracellular free copper. Many metallochaperones have been characterize d in yeast, mouse, and human. To further characterize mouse metallochaperon es, we cloned murine Ccsd from an adult mouse cDNA brain library, including both the coding region and the 5' and 3' UTRs. We obtained a 1,174-bp cDNA with an 825-bp open reading frame, translating a 274 amino acid protein th at is 86.9% identical to human CCS. Using a mouse x hamster radiation hybri d panel, we mapped Ccsd to a proximal position on mouse chromosome 19. We m apped human CCS to 11q13 (homologous with mouse chromosome 19), utilizing a human x hamster radiation hybrid panel. The human and mouse metallochapero nes are ubiquitously expressed in the major tissues of the body but seem to have different transcription products. Copyright (C) 2000 S.Karger AG, Bas el.