TY - JOUR
T1 - The copper chaperone for superoxide dismutase
AU - Culotta, Valeria Cizewski
AU - Klomp, Leo W.J.
AU - Strain, Jeffrey
AU - Casareno, Ruby Leah B.
AU - Krems, Bernhard
AU - Gitlin, Jonathan D.
PY - 1997/9/19
Y1 - 1997/9/19
N2 - Copper is distributed to distinct localizations in the cell through diverse pathways. We demonstrate here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated through a soluble factor identified as Saccharomyces cerevisiae LYS7 and human CCS (copper chaperone for SOD). This factor is specific for SOD1 and does not deliver copper to proteins in the mitochondria, nucleus, or secretory pathway. Yeast cells containing a lys7Δ null mutation have normal levels of SOD1 protein, but fail to incorporate copper into SOD1, which is therefore devoid of superoxide scavenging activity. LYS7 and CCS specifically restore the biosynthesis of holoSOD1 in vivo. Elucidation of the CCS copper delivery pathway may permit development of novel therapeutic approaches to human diseases that involve SOD1, including amyotrophic lateral sclerosis.
AB - Copper is distributed to distinct localizations in the cell through diverse pathways. We demonstrate here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated through a soluble factor identified as Saccharomyces cerevisiae LYS7 and human CCS (copper chaperone for SOD). This factor is specific for SOD1 and does not deliver copper to proteins in the mitochondria, nucleus, or secretory pathway. Yeast cells containing a lys7Δ null mutation have normal levels of SOD1 protein, but fail to incorporate copper into SOD1, which is therefore devoid of superoxide scavenging activity. LYS7 and CCS specifically restore the biosynthesis of holoSOD1 in vivo. Elucidation of the CCS copper delivery pathway may permit development of novel therapeutic approaches to human diseases that involve SOD1, including amyotrophic lateral sclerosis.
UR - http://www.scopus.com/inward/record.url?scp=0030802648&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030802648&partnerID=8YFLogxK
U2 - 10.1074/jbc.272.38.23469
DO - 10.1074/jbc.272.38.23469
M3 - Article
C2 - 9295278
AN - SCOPUS:0030802648
SN - 0021-9258
VL - 272
SP - 23469
EP - 23472
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 38
ER -