Respiratory chain enzyme activity and iron metabolism dysfunction in Parkinsonism

2002 ◽  
Vol 12 ◽  
pp. 382
Author(s):  
M.F. Borae ◽  
S.A. Hadi
Keyword(s):  
Enzyme Activity ◽  
Respiratory Chain ◽  
Iron Metabolism ◽  
Respiratory Chain Enzyme ◽  
Respiratory Chain Enzyme Activity

scholarly journals Measurement of Respiratory Chain Enzyme Activity in Human Renal Biopsy Specimens

2017 ◽  
Vol 6 (9) ◽  
pp. 90 ◽  
Author(s):  
Arun Ghose ◽  
Christopher Taylor ◽  
Alexander Howie ◽  
Anapurna Chalasani ◽  
Iain Hargreaves ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Renal Biopsy ◽  
Respiratory Chain ◽  
Respiratory Chain Enzyme ◽  
Biopsy Specimens ◽  
Respiratory Chain Enzyme Activity

Placental ceruloplasmin homolog is regulated by iron and copper and is implicated in iron metabolism

2002 ◽  
Vol 282 (3) ◽  
pp. C472-C478 ◽  
Author(s):  
Ruth Danzeisen ◽  
Cedric Fosset ◽  
Zehane Chariana ◽  
Kenneth Page ◽  
Samuel David ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Subcellular Localization ◽  
Iron Metabolism ◽  
Brush Border ◽  
Oxidase Activity ◽  
Perinuclear Region ◽  
Protein Levels ◽  
Bewo Cells ◽  
Membrane Bound ◽  
Choriocarcinoma Cell Line

We previously reported an endogenous, membrane-bound Cu oxidase with homology to ceruloplasmin in BeWo cells, a placental choriocarcinoma cell line. In this previous study, ceruloplasmin immunoreactivity was localized to the perinuclear region and non-brush-border membranes. Here, we show that azide-sensitive oxidase activity is enriched in the same fractions, correlating subcellular localization of enzyme activity with ceruloplasmin immunoreactivity. Expression of the placental Cu oxidase is inversely proportional to Fe status and directly proportional to Cu status at enzyme and protein levels. To identify a role for the Cu oxidase, cells were exposed to59Fe-transferrin for 18 h in an environment of 20% O2or 5% O2. At 5% O2, Cu-deficient cells retain significantly more59Fe than control cells. This excess in59Fe accumulation is caused by a significant decrease in59Fe release. These results indicate that downregulation of the placental Cu oxidase in BeWo cells impairs Fe release. This effect is only apparent in an environment of limited O2.

Respiratory chain enzyme activities in lymphocytes from untreated patients with Parkinson disease

1993 ◽  
Vol 39 (4) ◽  
pp. 667-669 ◽  
Author(s):  
N Barroso ◽  
Y Campos ◽  
R Huertas ◽  
J Esteban ◽  
J A Molina ◽  
...  
Keyword(s):  
Parkinson Disease ◽  
Respiratory Chain ◽  
Enzyme Activities ◽  
Complex I ◽  
Matched Control ◽  
Noninvasive Method ◽  
Respiratory Chain Enzyme ◽  
Complex Iv ◽  
Control Subjects ◽  
Combined Defects

Abstract Respiratory chain enzyme activities were studied in lymphocytes from patients with Parkinson disease (PD) (n = 16) and age-matched control subjects (n = 15). The patients had received no therapy before the study was conducted. Complex I, III, and IV activities were significantly lower (P < 0.05) in patients than in control subjects. A complex I defect was found in one patient, whereas complex IV was defective in another. Two patients had combined defects of both complexes. The use of lymphocytes for investigating the respiratory chain enzymes provides an easy, noninvasive method to assess mitochondrial function in patients with PD. Furthermore, our study supports the hypothesis that a biochemical defect in the respiratory chain may be involved in the pathogenesis of PD.

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