| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.5401834 |
| The copper chaperone for superoxide dismutase ( CCS ) interacts with Cu / Zn binding superoxide dismutase 1 ( SOD 1 ) specifically and delivers copper to SOD 1 . 0.5401834^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.55708359 |
| The copper chaperone CCS directly interacts with copper / zinc superoxide dismutase . 0.55708359^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.550655 |
| Using a yeast interaction mating system , yeast CCS was seen to physically interact with SOD 1 , and this interaction required sequences at the predicted dimer interface of CCS Domain 2 . 0.550655^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The copper chaperone for superoxide dismutase . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Undetectable intracellular free copper : the requirement of a copper chaperone for superoxide dismutase . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Crystal structure of the copper chaperone for superoxide dismutase . ^^^ The 1 . 8 A resolution structure of the yeast copper chaperone for superoxide dismutase ( yCCS ) reveals a protein composed of two domains . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The copper chaperone for superoxide dismutase ( SOD 1 ) inserts the catalytic metal cofactor into SOD 1 by an unknown mechanism . ^^^ Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The human copper chaperone for superoxide dismutase ( hCCS ) delivers the essential copper ion cofactor to copper , zinc superoxide dismutase ( SOD 1 ) , a key enzyme in antioxidant defense . ^^^ Crystal structure of the second domain of the human copper chaperone for superoxide dismutase . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Recent studies in Saccharomyces cerevisiae suggest that the delivery of copper to Cu / Zn superoxide dismutase ( SOD 1 ) is mediated by a cytosolic protein termed the copper chaperone for superoxide dismutase ( CCS ) . ^^^ Copper chaperone for superoxide dismutase is essential to activate mammalian Cu / Zn superoxide dismutase . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Cobalt ( 2+ ) binding to human and tomato copper chaperone for superoxide dismutase : implications for the metal ion transfer mechanism . ^^^ The copper chaperone for superoxide dismutase ( CCS ) gene encodes a protein that is believed to deliver copper ions specifically to copper zinc superoxide dismutase ( CuZnSOD ) . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Domains 1 and 3 of the human copper chaperone for superoxide dismutase interact via a cysteine bridged Dicopper ( 1 ) cluster . ^^^ Copper binding to the human copper chaperone for superoxide dismutase ( hCCS ) has been investigated by 10 ray absorption spectroscopy . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The new copper chaperone was named rCCS ( rat Copper Chaperone for Superoxide dismutase ) . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Copper , zinc superoxide dismutase ( SOD 1 ) is activated in vivo by the copper chaperone for superoxide dismutase ( CCS ) . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The copper chaperone for superoxide dismutase ( CCS ) activates the antioxidant enzyme Cu , Zn SOD ( SOD 1 ) by directly inserting the copper cofactor into the apo form of SOD 1 . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The copper chaperone for superoxide dismutase ( CCS ) activates the eukaryotic antioxidant enzyme copper , zinc superoxide dismutase ( SOD 1 ) . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The activity of SOD 1 is dependent upon the presence of a bound copper ion incorporated by the copper chaperone for superoxide dismutase , CCS . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Copper , zinc superoxide dismutase protein but not mRNA is lower in copper deficient mice and mice lacking the copper chaperone for superoxide dismutase . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The metal binding site of oxidized MerP is also similar to the metal binding sites of oxidized copper chaperone for superoxide dismutase and Atx 1 , two copper binding proteins from Saccharomyces cerevisiae . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Drosophila orthologues of the mammalian Cu chaperones , ATOX 1 ( a human orthologue of yeast ATX 1 ) , CCS ( copper chaperone for superoxide dismutase ) , COX 17 ( a human orthologue of yeast COX 17 ) , and SCO 1 and SCO 2 , did not significantly respond transcriptionally to increased Cu levels , whereas MtnA , MtnB and MtnD ( Drosophila orthologues of human metallothioneins ) were up regulated by Cu in a time and dose dependent manner . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Mutation analysis of genes encoding calpain 1 ( CAPN 1 ) , copper chaperone for superoxide dismutase ( CCS ) , ADP ribosylation factor like 2 ( ARL 2 ) , LOC 120664 , a putative homologue of atlastin ( ATLSTL 1 ) and sorting nexin 15 ( SNX 15 ) failed to identify any disease specific mutations . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Cysteine to serine mutants of a maltose binding protein fusion with the human copper chaperone for superoxide dismutase ( hCCS ) were studied with respect to ( 1 ) their ability to transfer Cu to E , Zn superoxide dismutase ( SOD ) and ( 2 ) their Zn and Cu binding and 10 ray absorption spectroscopic ( XAS ) properties . ^^^ Cysteine to serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain 3 dimer interface . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| A copper chaperone for superoxide dismutase that confers three types of copper / zinc superoxide dismutase activity in Arabidopsis . ^^^ The copper chaperone for superoxide dismutase ( CCS ) has been identified as a key factor integrating copper into copper / zinc superoxide dismutase ( CuZnSOD ) in yeast ( Saccharomyces cerevisiae ) and mammals . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Solution structure of the second PDZ domain of the neuronal adaptor X11alpha and its interaction with the C terminal peptide of the human copper chaperone for superoxide dismutase . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| MNK 1 adopts the betaalphabetabetaalphabeta fold common to all the metal binding sequences ( MBS ) found in other metal transport systems ( e . g . , the yeast copper chaperone for superoxide dismutase CCS , the yeast copper chaperone ATX 1 bound to Hg ( 2 ) , and most recently Cu ( 1 ) , the bacterial copper binding protein , CopZ , and the bacterial Hg ( 2 ) binding protein MerP ) , although substantial differences were found in the metal binding loop . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The copper chaperone for superoxide dismutase ( CCS ) is an intracellular metallochaperone required for incorporation of copper into the essential antioxidant enzyme copper / zinc superoxide dismutase ( SOD 1 ) . ^^^ Mechanisms of the copper dependent turnover of the copper chaperone for superoxide dismutase . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The crystal structure of the superoxide dismutase copper chaperone provides some key insights into the molecular mechanism of copper trafficking . . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Cloning and mapping of murine superoxide dismutase copper chaperone ( Ccsd ) and mapping of the human ortholog . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The mutant enzymes also are shown to acquire the catalytic copper in vivo through the action of CCS , a specific copper chaperone for SOD 1 , which in turn suggests that a search for inhibitors of this SOD 1 copper chaperone may represent a therapeutic avenue . . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| That both SOD 1 and CCS are present , together , in cells that degenerate in ALS also emphasizes the potential role of CCS in mutant SOD 1 mediated toxicity . . ^^^ CCS is a copper chaperone that donates copper to the antioxidant enzyme copper / zinc superoxide dismutase 1 ( SOD 1 ) . ^^^ Like SOD 1 , CCS immunoreactivity was intense in Purkinje cells , deep cerebellar neurons , and pyramidal cortical neurons , whereas in spinal cord , CCS was highly expressed in motor neurons . ^^^ Although the distribution of CCS paralleled that of SOD 1 , there was a 12 30 fold molar excess of SOD 1 over CCS . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : Recent studies have identified the human copper chaperone CCS as the presumed factor responsible for copper incorporation into superoxide dismutase ( SOD ) . ^^^ RESULTS : The three dimensional structure of CCS was homology modelled using the periplasmic protein from the bacterial mercury detoxification system and the structure of one subunit of the human SOD dimeric enzyme as templates . ^^^ On the basis of the three dimensional model , a mechanism for the transfer of copper from CCS to SOD is proposed that accounts for electrostatic acceptor recognition , copper storage and copper transfer properties . ^^^ A model for the incorporation of metal from the copper chaperone CCS into Cu , Zn superoxide dismutase . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| A gain of superoxide dismutase ( SOD ) activity obtained with CCS , the copper metallochaperone for SOD 1 . ^^^ The incorporation of copper ions into the cytosolic superoxide dismutase ( SOD 1 ) is accomplished in vivo by the action of the copper metallochaperone CCS ( copper chaperone for SOD 1 ) . ^^^ Mammalian CCS is comprised of three distinct protein domains , with a central region exhibiting remarkable homology ( approximately 50 % identity ) to SOD 1 itself . ^^^ Conserved in CCS are all the SOD 1 zinc binding ligands and three of four histidine copper binding ligands . ^^^ Despite this conservation of sequence between SOD 1 and CCS , CCS exhibited no detectable SOD activity . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Chromosomal localization of CCS , the copper chaperone for Cu / Zn superoxide dismutase . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| We investigated the segregation of the copper chaperone for the superoxide dismutase ( CCS ) gene in two Italian families with amyotrophic lateral sclerosis lacking the mutations in superoxide dismutase 1 gene . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| A Cu chaperone for SOD 1 ( CCS ) is required for the incorporation of copper ion into the protein . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| CCS delivers the copper cofactor to the antioxidant superoxide dismutase 1 ( SOD 1 ) enzyme and is required for its activity . ^^^ Overexpression of X11alpha inhibited SOD 1 activity in transfected Chinese hamster ovary cells which suggests that X11alpha binding to CCS is inhibitory to SOD 1 activation . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| After controlling for age , women had shorter ALs and VCDs , shallower ACDs , but thicker lenses and steeper CCs than men . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The Atx 1 like chaperones transfer copper to intracellular copper transporters , and the CCS chaperones shuttle copper to copper , zinc superoxide dismutase . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| In accordance with this connection to mitochondria , a fraction of active SOD 1 localizes within the intermembrane space ( IMS ) of mitochondria together with its copper chaperone , CCS . ^^^ Neither CCS nor SOD 1 contains typical N terminal presequences for mitochondrial uptake ; however , the mitochondrial accumulation of SOD 1 is strongly influenced by CCS . ^^^ When CCS synthesis is repressed , mitochondrial SOD 1 is of low abundance , and conversely IMS SOD 1 is very high when CCS is largely mitochondrial . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Similarly , CCS positive skein like inclusions were rarely seen in ALS neurons . ^^^ Since a copper mediated toxicity hypothesis has been proposed to explain the cytotoxic gain of function of mutant SOD 1 , we sought to determine the involvement of the copper chaperone for SOD 1 ( CCS ) in the formation of protein aggregates . ^^^ Although all aggregates contained CCS , SOD 1 was not uniformly found in the inclusions . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Human CCS gene : genomic organization and exclusion as a candidate for amyotrophic lateral sclerosis ( ALS ) . ^^^ As SOD 1 receives copper , essential for its normal function , by the copper chaperone , CCS ( Copper Chaperone for SOD ) , we considered CCS as a potential candidate gene for ALS . ^^^ We have evaluated involvement of the CCS in ALS by sequencing the entire coding region for mutations in 20 sporadic ALS patients . ^^^ CONCLUSIONS : No causative mutations for the ALS have been detected in the CCS gene in 20 sporadic ALS patients analyzed , but an intragenic single nucleotide polymorphism has been identified . . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| We tested this hypothesis by ablating the gene encoding the copper chaperone for SOD 1 ( CCS ) in a series of FALS linked SOD 1 mutant mice . ^^^ Metabolic 64Cu labeling in SOD 1 mutant mice lacking the CCS showed that the incorporation of copper into mutant SOD 1 was significantly diminished in the absence of CCS . ^^^ Motor neurons in CCS / mice showed increased rate of death after facial nerve axotomy , a response documented for SOD 1 / mice . ^^^ Thus , CCS is necessary for the efficient incorporation of copper into SOD 1 in motor neurons . ^^^ Although the absence of CCS led to a significant reduction in the amount of copper loaded mutant SOD 1 , however , it did not modify the onset and progression of motor neuron disease in SOD 1 mutant mice . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| CCS knockout mice establish an alternative source of copper for SOD in ALS . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| In vivo , the insertion of copper into SOD 1 is dependent on the copper chaperone for SOD 1 ( CCS ) . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| In particular , emphasis will be placed on the ATX 1 and CCS copper chaperones that act to deliver copper to the secretory pathway and to Cu / Zn superoxide dismutase in the cytosol , respectively . . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| We have previously shown that a fraction of yeast copper / zinc superoxide dismutase ( SOD 1 ) and its copper chaperone CCS localize to the intermembrane space of mitochondria . ^^^ The presence of high levels of CCS in the mitochondrial intermembrane space results in enhanced mitochondrial accumulation of SOD 1 , and this apparently involves CCS mediated retention of SOD 1 within mitochondria . ^^^ This retention of SOD 1 is not dependent on copper loading of the enzyme but does require protein protein interactions at the heterodimerization interface of SOD 1 and CCS as well as conserved cysteine residues in both molecules . ^^^ A model for how CCS mediated post translational modification of SOD 1 controls its partitioning between the mitochondria and cytosol will be presented . . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The insertion of copper into the antioxidant enzyme Cu , Zn superoxide dismutase ( SOD 1 ) depends on the copper chaperone for SOD 1 ( CCS ) . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| These include hCTR 1 , which regulates cellular copper uptake ; HAH 1 , which mediates the transfer of copper to the Menkes and Wilson disease transporters ; CCS , which is related to the transfer of copper to superoxide dismutase ; and hCOX 17 , which directs trafficking of copper to mitochondrial cytochrome c oxidase . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| SOD 1 interacts with and requires its metallochaperone CCS for donating copper . ^^^ We produced dietary Cu deficiency in rodents to determine if the reduction in SOD 1 was related to the level of its specific metallochaperone CCS . ^^^ Interestingly , CCS levels in brain of Cu deficient mice were also higher even though SOD 1 activity and protein were not altered , suggesting that the rise in CCS is correlated with altered Cu status rather than a direct result of lower SOD 1 . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| One fragment , named TDFL 431 , showed high homology to a copper ( Cu ) chaperone for Cu / zinc superoxide dismutase ( CCS ) . ^^^ The Ccs protein is responsible for the delivery of Cu to the Cu / zinc superoxide dismutase enzyme . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Co localization of human Sod 1 and the metallochaperone CCS within the mitochondrial matrix results in suppression of growth defects of sod2Delta cells . ^^^ However , in the absence of CCS within the matrix , the activation of human Sod 1 can be achieved by the addition of copper salts to the growth medium . . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Copper chaperone for SOD 1 ( CCS ) and extracellular Cu , Zn superoxide dismutase ( SOD 3 ) have some sequence identity with SOD 1 , particularly in the regions of metal binding , but play no significant role in mutant SOD 1 induced disease . ^^^ We hypothesized that it would be possible to form CCS or SOD 3 positive aggregates by making these molecules resemble mutant SOD 1 via the introduction of point mutations in codons homologous to a disease causing G85R SOD 1 mutation . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The Cu and Zn containing superoxide dismutase 1 ( SOD 1 ) largely obtains Cu in vivo by means of the action of the Cu chaperone CCS . ^^^ Specifically , when human SOD 1 is expressed in either yeast or mammalian cells that are null for CCS , the SOD 1 enzyme retains a certain degree of activity . ^^^ This CCS independent activity is evident with both wild type and mutant variants of SOD 1 that have been associated with familial amyotrophic lateral sclerosis . ^^^ We demonstrate here that the CCS independent activation of mammalian SOD 1 involves glutathione , particularly the reduced form , or GSH . ^^^ A role for glutathione in CCS independent activation was seen with human SOD 1 molecules that were expressed in either yeast cells or immortalized fibroblasts . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Rodent models were used to investigate whether erythrocyte concentrations of copper , zinc superoxide dismutase ( SOD ) , and the copper metallochaperone for SOD ( CCS ) were sensitive to dietary copper changes . ^^^ Associated with this copper deficiency were consistent reductions in immunoreactive SOD and robust enhancements in CCS . ^^^ In most cases , the ratio of CCS : SOD was several fold higher in red blood cell extracts from copper deficient compared with copper adequate rodents . ^^^ Determination of red cell CCS : SOD may be useful for assessing copper status of humans . . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| For example , in addition to the well characterized soluble Cu / Zn enzyme ( Sod ) and mitochondrial manganese containing form ( Sod 2 ) , Drosophila melanogaster is found to contain a putative copper chaperone ( CCS ) , an extracellular Cu / Zn enzyme ( Sod 3 ) , and an extracellular protein distantly related to the Cu / Zn forms ( Sodq ) . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Here we show that BACE 1 interacts with CCS ( the copper chaperone for superoxide dismutase 1 ( SOD 1 ) ) through domain 1 and the proteins co immunoprecipitate from rat brain extracts . ^^^ BACE 1 expression reduces the activity of SOD 1 in cells consistent with direct competition for available CCS as overexpression of CCS restores SOD 1 activity . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The copper chaperone for SOD 1 ( CCS ) is involved in physiological SOD 1 activation , and its primary function is thought to be delivery of copper to the enzyme . ^^^ Data presented here are consistent with a previously uncharacterized function for CCS in the SOD 1 pathway , namely mediating enzyme activation in response to increases in oxygen tension . ^^^ Activity assays with pure proteins and cell extracts reveal that O ( 2 ) ( or superoxide ) is required for activation of SOD 1 by CCS . ^^^ Dose response studies with a translational blocking agent demonstrate that the cellular oxidative response to O ( 2 ) is multitiered : existing apo pools of SOD 1 are activated by CCS in the early response , followed by increasing expression of SOD 1 protein with persistent oxidative stress . ^^^ This CCS function provides oxidant responsive posttranslational regulation of SOD 1 activity and may be relevant to a wide array of physiological stresses that involve a sudden elevation of oxygen availability . . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The structure is compared with that of the oxidized S S form as well as with that of the yeast SOD 1 complexed with its copper chaperone , CCS . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Recently , we have reported that copper chaperone for Cu / Zn superoxide dismutase ( CCS ) protein level is increased in tissues of overtly Cu deficient rats and proposed CCS as a novel biomarker of Cu status . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Transduced human copper chaperone for Cu , Zn SOD ( PEP 1 CCS ) protects against neuronal cell death . ^^^ SOD activity is dependent upon bound copper ions supplied by its partner metallochaperone protein , copper chaperone for SOD ( CCS ) . ^^^ Moreover , transduced PEP 1 CCS markedly increased endogenous SOD activity in the cells . ^^^ These results suggest that CCS is essential to activate SOD , and that transduction of PEP 1 CCS provides a potential strategy for therapeutic delivery in various human diseases including stroke related to SOD or ROS . . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| The intracellular copper SODs of eukaryotes ( SOD 1 ) can obtain copper post translationally , by way of interactions with the CCS copper chaperone . ^^^ CCS also oxidizes an intrasubunit disulfide in SOD 1 . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| In the present study , we investigated the chronological alterations in SOD 1 and its copper chaperone ( chaperone for superoxide dismutase , CCS ) immunoreactivities and their neuroprotective effects against neuronal damage in the gerbil hippocampus after 5 min of transient forebrain ischemia . ^^^ SOD 1 and CCS immunoreactivities were significantly increased in the stratum pyramidale of the CA 1 region at 24 and 12 h after ischemic insult , respectively . ^^^ At 24 h after ischemic insult , the SOD 1 and CCS immunoreactivities were colocalized in the CA 1 pyramidal cells of the stratum pyramidale . ^^^ To elucidate the effects of CCS or CCS / SOD1 , we constructed the expression vectors PEP 1 SOD and PEP 1 CCS . ^^^ In addition , the SOD activity in the PEP CCS or PEP CCS / SOD1 treated group was maintained by 10 days after ischemic insult . ^^^ |
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| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| Activation of CuZn SODs in eukaryotic cells occurs post translationally and is generally dependent on the copper chaperone for SOD 1 ( CCS ) , which inserts the catalytic copper cofactor and catalyzes the oxidation of a conserved disulfide bond that is essential for activity . ^^^ As was found for mammalian SOD 1 , wSOD 1 exhibits a requirement for reduced glutathione in CCS independent activation . ^^^ |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14618 and P00441 |
Pubmed |
SVM Score :0.0 |
| NA |
|