Raised Cerebrospinal-Fluid Copper Concentration in Parkinson's Disease

Pall, Hardev; Blake, D R; Gutteridge, John M.C.; Williams, Adrian; Lunec, Joseph; Hall, Michael R.; Taylor, Ann E.

doi:10.1016/s0140-6736(87)90827-0

Cited by 210 publications

(144 citation statements)

References 26 publications

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“…The extremely low levels of activity suggest that this protein likely plays no direct metabolic role in the biodegradation of catecholamines. However, the insensitivity of the Cu-S100B reaction to SOD, an antioxidative mechanism employed by the cell, may implicate this type of oxidative mechanism in the slow progression of neurodegenerative diseases (17).…”

Section: Resultsmentioning

confidence: 99%

Catecholase Activity Associated with Copper-S100B

et al. 2003

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This study addresses the spectroscopic properties and reactivity associated with the copperloaded form of S100B isolated from bovine brain. Copper(II)-S100B displays EPR features typical of a type II copper center and is shown here to exhibit catecholase activity, the two-electron oxidation of catechols. The steady-state kinetics associated with the oxidation of several catecholamines has been probed in order to further characterize this activity. The evidence provided indicates that the catecholase chemistry is copper initiated. Superoxide dismutase has no effect on the rates of catecholamine oxidation catalyzed by Cu-S100B, establishing that superoxide is not produced during this reaction, ruling out an autoxidative mechanism. Addition of catalase to the Cu-S100B reaction with catechols reduces the amount of oxygen consumed by 50%, demonstrating that peroxide is released during this reaction. The release of peroxide is mechanistically distinct from the type III dinuclear copper proteins, catechol oxidase and tyrosinase.

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Section: Resultsmentioning

confidence: 99%

Catecholase Activity Associated with Copper-S100B

et al. 2003

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“…In this regard, a recent finding should be noted that ␤A4 amyloid precursor protein reduces Cu 2ϩ to Cu 1ϩ and possibly contributes to neurodegeneration in Alzheimer's disease through generation of reactive oxygen species (24). It is also reported that the copper level of the cerebrospinal fluid is significantly elevated in patients of Parkinson's disease (25). Therefore, it seems likely that S100b protein intervenes the pathogenic processes of these diseases.…”

Section: Discussionmentioning

confidence: 99%

“…ischemia-reperfusion injury (2), fulminant hepatic inflamation in Wilson's disease (3), Parkinson's disease (4), and rheumatoid arthritis (5). Sequestration of copper ions is also important for prevention of L-ascorbate oxidation that is extremely accelerated by free copper ions (6,7).…”

mentioning

confidence: 99%

Identification of S100b Protein as Copper-binding Protein and Its Suppression of Copper-induced Cell Damage

Nishikawa

Lee

Shiraishi

et al. 1997

Journal of Biological Chemistry

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We have isolated from bovine brain a protein with a high capacity to inhibit the copper ion-catalyzed oxidation of L-ascorbate and identified it as S100b protein, an EF-hand calcium-binding protein, by sequencing its proteolytic peptides. Copper binding studies showed that this protein has four copper-binding sites per dimeric protein molecule with a dissociation constant of 0.46 M and that in the presence of L-ascorbate, copper ions bind to a total of six binding sites with a great increase in affinity. Furthermore, we examined whether S100b protein can prevent copper-induced cell damage. Bovine S100b protein was found to suppress dose-dependently the hemolysis of mouse erythrocytes induced by CuCl 2 . We transformed Escherichia coli cells with pGEX-5X-3 vector containing a cDNA for rat S100b protein, so that this protein could be expressed as a fusion protein with glutathione S-transferase. The transformed cells were demonstrated to be markedly resistant to a treatment with CuCl 2 plus H 2 O 2 as compared with the control cells expressing glutathione S-transferase alone. These results indicate that S100b protein does suppress oxidative cell damage by sequestering copper ions.

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“…Therefore, our developed pyoverdine-based biosensor could be utilized to detect copper ion in polluted water samples. Additionally, the concentration of cop- per ion in cerebrospinal fluid would rise in patients of Parkinson's disease [38]. Therefore, our pyoverdine-based biosensor could also be used in disease prediction.…”

Section: Applications Of the Biosensor To Spiked Samplesmentioning

confidence: 99%

A sensitive fluorescent biosensor for the detection of copper ion inspired by biological recognition element pyoverdine

Yin

Wang

et al. 2016

Sensors and Actuators B: Chemical

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a b s t r a c tThe environmental copper pollution seriously threatens the health of organisms and the safety of ecosystem. Therefore, the development of a simple and sensitive method to detect copper ion is very important. In this study, we have developed a fluorescent biosensor based on biological recognition element pyoverdine to selectively detect copper ion. The fluorescence of pyoverdine is quenched obviously after binding with copper ion. A good linearity within the range of 0.2-10 M (R = 0.997) is attained and the detection limit is 50 nM. The biosensor has been successfully utilized for the detection of copper ion in drinking water, seawater and bio-samples and the results agree well with those obtained by the inductively coupled plasma mass spectrometry. Therefore, the established biosensor is a creditable method to detect copper ion with high sensitivity and selectivity, which can be utilized as a powerful tool to monitor copper pollution in the environment.

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Raised Cerebrospinal-Fluid Copper Concentration in Parkinson's Disease

Cited by 210 publications

References 26 publications

Catecholase Activity Associated with Copper-S100B

Catecholase Activity Associated with Copper-S100B

Identification of S100b Protein as Copper-binding Protein and Its Suppression of Copper-induced Cell Damage

A sensitive fluorescent biosensor for the detection of copper ion inspired by biological recognition element pyoverdine

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