Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase.

Hjalmarsson, Karin; Marklund, Stefan L.; Engström, Åke; Edlund, Thomas

doi:10.1073/pnas.84.18.6340

Cited by 226 publications

(167 citation statements)

References 40 publications

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“…The nucleotide sequence of human EC-SOD cDNA 002947 in EMBL database) has been reported by Hjalmarsson et al (1987). Based on the sequence, 10 specific oligonucleotide primers were designed for polymerase chain reaction (PCR) and direct sequencing (Fig.…”

Section: Resultsmentioning

confidence: 99%

Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum

Yamada

Adachi

et al. 1995

Jap J Human Genet

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Summary Extracellular-superoxide dismutase (EC-SOD) is one of the SOD isozymes mainly distributed in the extracellular fluid. In the vascular system, it is located on the endothelial cell surface according to studies on the heparin binding capacity. By measurement of serum EC-SOD levels of Japanese in healthy persons (n=103) and hemodialysis patients (n= 150), 7 healthy subjects and 24 hemodialysis patients were classified into group II associated with high EC-SOD levels. By molecular analysis of the EC-SOD coding region from the group II individuals in Sweden, a single nucleotide substitution of G to C generating an amino acid change of arginine to glycine has been identified in the region associated with the heparin affinity of the enzyme. The same mutation was detected in the Japanese as a homozygote in both alleles of 2 hemodialysis patients and as a heterozygote in one allele of all the healthy group II individuals and 17 hemodialysis patients. The amino acid substitution may result in the decrease of the heparin affinity which is favorable for the existence of EC-SOD in the serum.

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Section: Resultsmentioning

confidence: 99%

Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum

Yamada

Adachi

et al. 1995

Jap J Human Genet

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“…is expressed in some organisms (11,12). In all cases, enzyme catalysis involves redox cycling of the manganese or copper ion at the active site.…”

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confidence: 99%

Activation of CuZn Superoxide Dismutases from Caenorhabditis elegans Does Not Require the Copper Chaperone CCS

Jensen

Culotta

2005

Journal of Biological Chemistry

104

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Reactive oxygen species are produced as the direct result of aerobic metabolism and can cause damage to DNA, proteins, and lipids. A principal defense against reactive oxygen species involves the superoxide dismutases (SOD) that act to detoxify superoxide anions. Activation of CuZn-SODs in eukaryotic cells occurs posttranslationally and is generally dependent on the copper chaperone for SOD1 (CCS), which inserts the catalytic copper cofactor and catalyzes the oxidation of a conserved disulfide bond that is essential for activity. In contrast to other eukaryotes, the nematode Caenorhabditis elegans does not contain an obvious CCS homologue, and we have found that the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on CCS for activation when expressed in Saccharomyces cerevisiae. CCS-independent activation of CuZn-SODs is not unique to C. elegans; however, this is the first organism identified that appears to exclusively use this alternative pathway. As was found for mammalian SOD1, wSOD-1 exhibits a requirement for reduced glutathione in CCS-independent activation. Unexpectedly, wSOD-1 was inactive even in the presence of CCS when glutathione was depleted. Our investigation of the cysteine residues that form the disulfide bond in wSOD-1 suggests that the ability of wSODs to readily form this disulfide bond may be the key to obtaining high levels of activation through the CCS-independent pathway. Overall, these studies demonstrate that the CuZn-SODs of C. elegans have uniquely evolved to acquire copper without the copper chaperone and this may reflect the lifestyle of this organism.

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“…However, some reports have suggested that Cu/ZnSOD may also reside in the nucleus, peroxisomes, and lysosomes. [20][21][22] A third form, ecSOD, 23 is secreted into the extracellular environment.…”

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Subcellular site of superoxide dismutase expression differentially controls AP-1 activity and injury in mouse liver following ischemia/reperfusion

et al. 2001

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The cellular redox state has been increasingly recognized as a critical component of stress-induced cellular responses and disease. Inherent in these responses are reactive oxygen species (ROS), including • O 2 Ϫ , H 2 O 2 , and • OH, which inflict direct cellular damage in addition to acting as intracellular second messengers modulating signal transduction pathways. These intracellular highways of communication are critical in determining cell fates and whole-organ responses following environmental injury. Pathologic events caused by transient tissue hypoxia followed by oxygen reperfusion (ischemic/reperfusion [I/R]) are the cause of numerous types of surgical and environmentally induced injuries in the liver associated with transplantation and resection. Pathologic changes encountered following reperfusion of an ischemic organ include the immediate generation of ROS, as well as subsequent neutrophil-predominant inflammatory responses that lead to a second round of deleterious ROS generation at sites of damage. Recently, it has become increasingly appreciated that ROS are involved as second messengers in a number of cellular signaling events leading to the induction of AP-1 and nuclear factor-B pathways.

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Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase.

Cited by 226 publications

References 40 publications

Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum

Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum

Activation of CuZn Superoxide Dismutases from Caenorhabditis elegans Does Not Require the Copper Chaperone CCS

Subcellular site of superoxide dismutase expression differentially controls AP-1 activity and injury in mouse liver following ischemia/reperfusion

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