Decrease in cytochrome c oxidase activity detected cytochemically in the placental trophoblast of patients with pre-eclampsia

Matsubara, Shigeki; Minakami, Hisanori; Sato, Ikuo; Saito, Takuma

doi:10.1016/s0143-4004(97)80059-8

Cited by 52 publications

(36 citation statements)

References 11 publications

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“…The function of placental cells is dependent on energy supplied by the mitochondria. Changes in the function and activities of placental Mt respiratory chain enzymes of preeclamptic patients noted in the present study are in accordance with an increased Mt dysfunction since respiratory complexes are critical for the maintenance of cellular energy (39,40). Under conditions of highenergy demand, such as during oxidative stress, the placenta may experience energy shortages due to inability of the mitochondria to produce ATP.…”

Section: Discussionsupporting

confidence: 79%

Preeclamptic placental stress and over expression of mitochondrial HSP70

Perumal

Lavanya

Uthra

2009

Clinical Chemistry and Laboratory Medicine

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Background: Evidence is accumulating that mitochondrial (Mt) oxidative stress plays a role in the pathogenesis of preeclampsia. The current study analyzes the stress levels, energy status and associated enzymatic alteration in placental mitochondria of preeclamptic (ns30) and normotensive (ns35) subjects. Methods: Total Mt stress was measured using dichlorofluorescin (DCFH) oxidant analysis, malondialdehyde (MDA) concentrations, protein carbonyl (PC) concentrations and measurement of nitrite ( ) and

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Section: Discussionsupporting

confidence: 79%

Preeclamptic placental stress and over expression of mitochondrial HSP70

Perumal

Lavanya

Uthra

2009

Clinical Chemistry and Laboratory Medicine

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“…There were no findings, such as phagosomal formation, fusion of lysosomes to the phagosomes/plasma membranes, or the appearance of the acid phosphatase to the phagosomal membranes, which we have shown to be the histochemical signs of phagocytosis (Matsubara et al 2000a). CCO labelings were observed in the mitochondria in their intermembrane spaces and intracristal spaces (Figures 2b, b'), which agreed well with our previous observations in other cells (Matsubara et al 1997b;Matsubara et al 2000b). Mitochondria, highlighted by CCO stainings, were present all throughout the cytoplasm, and there were no CCO-negative mitochondria (Figures 2b, b').…”

Section: Enzymehistochemistry (Figures 2a-c)supporting

confidence: 91%

Human amniotic epithelial cells are morphologically homogeneous: enzymehistochemical, tracer, and freeze-substitution fixation study

Iwasaki

Matsubara²,

Tajima³

et al. 2009

Eur J Histochem

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We examined the fine subcellular morphology of human amniotic epithelial cells and attempted to answer the question as to whether amniotic epithelial cells consist of heterogeneous or homogeneous cells, which has long been controversial. Study subjects were fetal membranes from pregnant women (n=18) who abdominally gave birth to healthy infants at term (37.9±0.7 weeks of gestation, mean±sd). The methods employed were transmission electron microscopy, enzymehistochemistry, tracer permeability analysis, and freeze-substitution fixation. The labelings for acid phosphatase, cytochrome c oxidase, and CA ++ ATPase were seen in the lysosomes, mitochondria, and lateral plasma membranes, respectively. The staining distribution pattern of these three enzymes and the morphology of the organelle highlighted by these enzymehistochemistry did not differ among cells. Freeze-substitution fixation revealed that intercellular spaces in the amniotic epithelial cells were narrower than previously thought, but the tracers (horse radish peroxidase and lanthanum nitrate) fully entered these spaces. There were no variations in the tracer permeability among cells. All cells from freeze-substitution fixation exhibited the same morphological features. From these morphological viewpoints, we conclude that human term amniotic epithelial cells consist of a homogeneous cell population.

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“…In brief, sections of 40 µm thickness were incubated in the following reaction media: cerium medium [100 mM TRIS-maleate buffer (pH 8.0), 1 mM beta-glycerophosphate, 2 mM CeCl 3 ; Robinson and Karnovsky 1983] for ALPase, cerium medium [100 mM acetate buffer (pH 5.0), 1 mM beta-glycerophosphate, 2 mM CeCl 3 ; Robinson and Karnovsky 1983] for ACPase, cerium medium [80 mM cacodylate buffer (pH 6.7), 3.7 mM glucose-6-phosphate, 3.6 mM CeCl 3 , 1 mM bromotetramisole; Asaka et al 1991] for G6Pase, and diaminobenzidine medium [100 mM phosphate buffer (pH 7.4), 1 mg/ml cytochrome c, 0.5 mg/ml diaminobenzidine, 0.1 mg/ml catalase; Seligman et al 1968] for CCO. A series of previous studies done by our group demonstrated that these conditions were the most suitable for the detection of each placental enzyme activity, with adequate preservation of the placental ultrastructure (Matsubara et al 1987b(Matsubara et al , 1997b(Matsubara et al , 1999a. To confirm the specific detection of each enzyme activity, a series of cytochemical control experiments was performed, as previously described (Matsubara et al 1987b(Matsubara et al , 1997b(Matsubara et al , 1999a.…”

Section: Methodsmentioning

confidence: 98%

“…A series of previous studies done by our group demonstrated that these conditions were the most suitable for the detection of each placental enzyme activity, with adequate preservation of the placental ultrastructure (Matsubara et al 1987b(Matsubara et al , 1997b(Matsubara et al , 1999a. To confirm the specific detection of each enzyme activity, a series of cytochemical control experiments was performed, as previously described (Matsubara et al 1987b(Matsubara et al , 1997b(Matsubara et al , 1999a. Sections were postfixed in cold 1% buffered osmium tetroxide for 60 min, dehydrated, and embedded in epoxy resin.…”

Section: Methodsmentioning

confidence: 99%

Enzyme histochemistry on human placental trophoblasts: the effect of fixation delay on enzyme activity

Matsubara

Tajima

Sato

2000

Histochem Cell Biol

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We examined the effect of time delay in tissue fixation on enzyme histochemically detectable enzyme activity and its localization in term human placental trophoblasts. Four placental enzymes, alkaline phosphatase, acid phosphatase, glucose-6-phosphatase, and cytochrome c oxidase, were studied. A fixation delay of 15 min did not markedly alter the activity or distribution pattern of the four enzymes, excepted for a slight reduction in cytochrome c oxidase activity and the appearance of dilated endoplasmic reticula positive for glucose-6-phosphatase. A fixation delay of 60 min abolished cytochrome c oxidase activity, but the activities of the other three enzymes remained positive. When the placental tissue was stored at 4 degrees C without cutting for 24 h before fixation, cell degeneration occurred. However, alkaline phosphatase activity was still clearly demonstrable. In enzyme histochemistry, ,,immediate" fixation is superior, but even if this cannot be performed, the placentas, especially when they are from patients with rare disorders, should not be discarded. Observations made here will be useful for clinician's attempting enzyme histochemistry in organs other than the placenta.

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Decrease in cytochrome c oxidase activity detected cytochemically in the placental trophoblast of patients with pre-eclampsia

Cited by 52 publications

References 11 publications

Preeclamptic placental stress and over expression of mitochondrial HSP70

Preeclamptic placental stress and over expression of mitochondrial HSP70

Human amniotic epithelial cells are morphologically homogeneous: enzymehistochemical, tracer, and freeze-substitution fixation study

Enzyme histochemistry on human placental trophoblasts: the effect of fixation delay on enzyme activity

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