Glutathione peroxidase in early and advanced Parkinson's disease.

Johannsen, Peter; Velander, G; Mai, Jesper; Thorling, Eivind B.; Dupont, E.

doi:10.1136/jnnp.54.8.679

Cited by 39 publications

(15 citation statements)

References 18 publications

(2 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In the early stages no alterations can be detected in the activities of SOD and catalase, while later a reduction of these enzymes can be observed in the RBC [7,8]. Glutathione peroxidase displays similar changes [6]. The decreased activities of these enzymes in the RBC are presumably a consequence of the progression of the disease.…”

Section: Discussionmentioning

confidence: 94%

See 1 more Smart Citation

Kynurenine metabolism in plasma and in red blood cells in Parkinson's disease

Hartai

Klivényi

Janáky

et al. 2005

Journal of the Neurological Sciences

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 94%

“…Decreased levels of vitamin C [3] and GSH [4,5] have been reported in the plasma and lower GSH peroxidase [6] and superoxide dismutase (SOD) levels [7,8] have been measured in the RBC in PD. These data suggest alterations can be detected in the plasma and RBC in PD.…”

Section: Introductionmentioning

confidence: 99%

Kynurenine metabolism in plasma and in red blood cells in Parkinson's disease

Hartai

Klivényi

Janáky

et al. 2005

Journal of the Neurological Sciences

View full text Add to dashboard Cite

“…2% of the body mass in humans, it is responsible for approximately 20% of total body oxygen consumption. [4][5][6] As a consequence of the high oxygen demand, the brain tissue inevitably induces the generation of large amounts of reactive oxygen species, which are thought to be associated with the onset and/or progression of neurodegenerative diseases such as Alzheimer's disease [7][8][9] and Parkinson's disease, [10][11][12] due to the reactive oxygen species-mediated injury from the early stages of the illnesses. Numerous papers have pointed out that decreases in the GPx activity in the brain are associated with these neurodegenerative diseases.…”

mentioning

confidence: 99%

A Comprehensive Analysis of Selenium-Binding Proteins in the Brain Using Its Reactive Metabolite

Yoshida

Hori

Ura

et al. 2016

CHEMICAL & PHARMACEUTICAL BULLETIN

View full text Add to dashboard Cite

The intracellular metabolism of selenium in the brain currently remains unknown, although the antioxidant activity of this element is widely acknowledged to be important in maintaining brain functions. In this study, a comprehensive method for identifying the selenium-binding proteins using PenSSeSPen as a model of the selenium metabolite, selenotrisulfide (RSSeSR, STS), was applied to a complex cell lysate generated from the rat brain. Most of the selenium from L-penicillamine selenotrisulfide (PenSSeSPen) was captured by the cytosolic protein thiols in the form of STS through the thiol-exchange reaction (R-SH PenSSeSPen→R-SSeSPen PenSH). The cytosolic protein species, which reacted with the PenSSeSPen mainly had a molecular mass of less than 20 kDa. A thiol-containing protein at m/z 15155 in the brain cell lysate was identified as the cystatin-12 precursor (CST12) from a rat protein database search and a tryptic fragmentation experiment. CST12 belongs to the cysteine proteinase inhibitors of the cystatin superfamily that are of interest in mechanisms regulating the protein turnover and polypeptide production in the central nervous system and other tissues. Consequently, CST12 is suggested to be one of the cytosolic proteins responsible for the selenium metabolism in the brain.

show abstract

“…Depletion of glutathione (Tazhibaev and Tishchenko, 1992) 8. Impairment of Ca metabolism (Kakkar et al, 1993) (Agid, 1991;Johannsen et al, 1991;Lafon-Gazal et al, 1993;Olanov, 1992;Riederer and Lange, 1992) a 2. Excess of free iron (Aim et al, 1994;Ben-Shachar et al, 1992;Kontoghiorghes et al, 1993;Temlett et al, 1994) a 3.…”

Section: Resultsmentioning

confidence: 97%