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PubMed1981

The histochemical localization of cytochrome oxidase in the dentate gyrus of the rat hippocampus.

In the dentate gyrus of the rat's hippocampal formation, the activity of an oxidative enzyme, cytochrome oxidase, has been localized mostly to the molecular layer with histochemical methods that utilize diaminobenzidine. The electron microscopic localization of cytochrome oxidase indicated that mitochondria within granule cell dendrites were very reactive while those within the somata and mossy fiber terminals of this neuronal type were less reactive. Caution must be used when predicting the relative physiological activities of neurons with this method because differential activities of this enzyme occur within separate parts of the same neuronal population.

Animals↗
PubMed1990

Electron cryo-microscopic analysis of crystalline cytochrome oxidase.

The structure of cytochrome oxidase from beef heart mitochondria has been analysed by cryo-electron microscopy of vesicle crystals of the space group p22(1)2(1), with cell dimensions a = 102 A, b = 123 A, gamma = 90 degrees. Several methods of specimen preparation were applied to the vesicular two-dimensional crystals in the electron microscope, to ensure that the structure was preserved to the maximum resolution. The two most informative density maps were from specimens embedded in ice and from negative staining in a 1:1 mixture of glucose and uranyl acetate. The three-dimensional structure of the ice-embedded molecule shows a single, well resolved, but convoluted density, which represents in size and shape one cytochrome oxidase dimer. At the bottom of the molecule, a substantial part of the protein is embedded in the lipid bilayer of the vesicle. The molecule then extends upwards, out of the bilayer, into the internal space within the vesicle. Here, the structure first passes through a region within the molecule containing a hollow cavity that lies roughly at the centre of mass of the dimer, and then branches into two well-resolved halves at some distance from the membrane. The negatively stained structure, in contrast, shows a stain-excluding region in the centre of the vesicle at the level of the cavity in the ice-embedded structure, but otherwise has a similar overall external shape. In addition, there is a small rotation of the whole molecule by approximately 25 degrees relative to the orientation of ice-embedded specimens. We interpret these differences to mean that the central cavity seen in the ice-embedded structure is too small to allow the stain to penetrate during the drying process and that the drying process causes the rotation. The structures described here are consistent with one another and allow an interpretation at higher resolution than from previous work.

Animals↗
PubMed2004

Nitrogen disruption of synaptoneurosomes: an alternative method to isolate brain mitochondria.

Mitochondria are known to be localized in synaptic and non-synaptic compartments in the brain. Synaptoneurosomes, which contain high numbers of mitochondria, may act as a major contaminant of currently used isolation techniques. Currently, there is no method employed to successfully disrupt synaptoneurosomes and isolate both synaptic and non-synaptic mitochondria without structural or functional damage. A novel method is reported here for disruption of synaptoneurosomes and isolation of total brain mitochondria from synaptic and non-synaptic sources using a nitrogen decompression technique. Nitrogen gas was dissolved into crude mitochondrial preparations and maintained under constant, moderate pressure. After a short incubation, the pressure was released causing the nitrogen to come out of solution as growing bubbles, which ruptures cellular and synaptoneurosomal membranes. Mitochondria isolated using this rapid technique were bioenergetically competent and exhibited functional characteristics comparable to mitochondria isolated using traditional techniques. This nitrogen decompression technique will allow for further characterization of synaptic pools of mitochondria, which are almost exclusively neuronal in origin.

Animals↗
PubMed2003

Structural and biochemical evidence of mitochondrial depletion in pigs with hypertrophic cardiomyopathy.

Pig hearts with naturally occurring hypertrophic cardiomyopathy (HCM) were isolated to investigate the effects of mitochondrial deficiency at biochemical and molecular levels. Enzyme activities of mitochondrial-encoded cytochrome c oxidase and NADH dehydrogenase in the HCM hearts (n=12) were lower than that in the controls (n=12) by 41+/-29% (P<0.01) and 43+/-21% (P<0.001), respectively. Additionally, Southern blot analysis was conducted to quantify the relative amount of mitochondrial DNA (mtDNA) from the HCM and controls. The relative amount of mtDNA in the HCM hearts was significantly 57+/-19% (P<0.001) lower than that in the controls. Both mitochondrial enzyme deficiency and mtDNA depletion were significantly correlated with the degree of cardiac hypertrophy judged based on the ratio of heart/body weight. In conclusion, our results reveal that a secondary effect of tissue-specific mtDNA depletion and mitochondrial dysfunction is in response to the HCM.

Animals↗
PubMed1987

Quantitative cytochemical analysis of cytochrome oxidase and succinate dehydrogenase activity in spinal neurons.

This paper describes cytophotometric determinations of cytochrome oxidase (COX) and succinate dehydrogenase (SDH) activities in neurons in 3 areas of the spinal motor column of the teleost fish Brachydanio rerio (the Zebrafish). Purpose of this investigation was to analyse the correlation between the oxidative metabolic capacity of motoneurons with their activity patterns. The spatial organization of the spinal cord of the zebrafish allows such an analysis, because the motoneurons which innervate different muscle fiber types (slow tonic red and fast phasic white, respectively) occupy separate areas of the motor column (Van Raamsdonk et al. 1983). We analysed the COX and SDH activities on serially sectioned neurons, We found large variations in the ratio of COX/SDH activity: the ratio was high for large neurons (in the "white" area) and low for small neurons (in the "red" area). These findings were contrary our expectations, because COX as well as SDH activity have been proposed as indicators for neuronal activity if both activities are reliable indicators, then their ratio should be constant. In addition, COX and SDH activities were analysed on serially sectioned anterior horn neurons of the cat spinal cord. In contrast to the situation in fish, we observed a statistically significant proportionality between COX and SDH activities. We conclude that the histochemical reactions for COX or SDH activity have no general validity as markers for the same type of neuronal activity.

Animals↗
PubMed1973

Changes in enzyme activities and distributions during glucose de-repression and respiratory adaptation of anaerobically grown Saccharomyces carlsbergensis.

1. During anaerobic glucose de-repression the respiration rate of whole cells of Saccharomyces carlsbergensis remained constant and was insensitive to antimycin A but was inhibited by 30% by KCN. Aeration of cells for 1 h led to increased respiration rate which was inhibited by 80% by antimycin A or KCN. 2. Homogenates were prepared from sphaeroplasts of anaerobically grown, glucose de-repressed cells and the distribution of marker enzymes was investigated after zonal centrifugation on sucrose gradients containing MgCl(2). These homogenates contained no detectable cytochrome c oxidase or catalase activity. The complex density distributions of NADH- and NADPH-cytochrome c oxidoreductases and adenosine triphosphatase(s) [ATPase(s)] were very different from those of anaerobically grown, glucose-repressed cells. 3. The specific activity of total ATPase was lowered and sensitivity to oligomycin decreased from 58 to 7% during de-repression. 4. Cytochrome c oxidase and catalase activities were detectable in homogenates of cells after 10min aeration. Zonal centrifugation indicated complex, broad sedimentable distributions of all enzyme activities assayed; the peaks of activity were at 1.27g/ml. 5. Centrifugation of homogenates of cells adapted for 30min and 3 h indicated a shift of density of the major sedimentable peak from 1.25g/ml (30min) to 1.235g/ml (3 h). After 30min adaptation a minor zone of oligomycin-sensitive ATPase and 15% of the total cytochrome c oxidase activities were detected at rho=1.12g/l; these particles together with those of higher density containing cytochrome c oxidase, ATPase and NADH-cytochrome c oxidoreductase activities were all sedimented at 10(5)g-min. 6. Electron microscopy indicated that the mitochondria-like structures of anaerobically grown, glucose-de-repressed cells were similar to those of repressed cells. After 10min of respiratory adaptation highly organized mitochondria were evident which resembled the condensed forms of mitochondria of aerobically grown, glucose-de-repressed cells. High-density zonal fractions of homogenates of cells after adaptation also contained numerous electron-dense vesicles 0.05-0.2mum in diameter. 7. The possibility that the ;promitochondria' of anaerobically grown cells may not be the direct structural precursors of fully functional mitochondria is discussed.

Acid Phosphatase↗
PubMed1987

Dynamics of proteoliposome formation. Intermediate states during detergent dialysis.

1. The intermediate structures formed during dialysis of mixtures of cholate, phospholipid and cytochrome c oxidase were analysed by gel chromatography and electron microscopy. Measurements of trapped phosphate and the degree of respiratory control were used to assess the integrity of the vesicular structures formed. Protein orientation in the bilayer was monitored by the accessibility of cytochrome c to cytochrome c oxidase. 2. The results indicate that proteoliposome formation by the detergent-dialysis procedure takes place in three distinct stages. In the first stage, cholate/phospholipid and cholate/phospholipid/protein micelles coexist in solution and grow in size as the detergent is slowly removed. At a detergent/phospholipid molar ratio of about 0.2, micelle fusion results in the formation of large bilayer aggregates permeable to both phosphate and cytochrome c. It is at this stage that cytochrome c oxidase is incorporated into the bilayer. In the final stage of dialysis the bilayer sheets fragment into small unilamellar vesicles. 3. The orientation of membrane protein in the final vesicles appears to be determined by the effect of protein conformation on the initial curvature of the bilayer sheets during the fragmentation process.

Cholic Acid↗
PubMed1995

Homology between mitochondriogenesis in the avian and amphibian oocyte.

Cytochrome oxidase cytochemistry was used to unequivocally identify the spread of mitochondria during oogenesis in the adult Japanese quail. This enabled us to compare their distribution with the distribution in the Xenopus laevis oocyte (Tourte et al, 1984). In the quail the paranuclear mitochondrial cloud initially disperses homogeneously but afterwards segregates into 2 populations: (i) a population localized in the basophilic cortical layer (surrounding the vegetal pole); and (ii) clusters of mitochondria distributed geometrically around the germinal vesicle in the animal pole. The mitochondria in these clusters have a high cytochrome oxidase activity, which reflects their functionality. This perinuclear crown of mitochondrial clusters actively replicates mtDNA in both animal species and builds up most of the stock of the mitochondria in the full-grown oocyte. Our study suggests that the perinuclear group of mitochondria will segregate in the somatic cells of the future embryo, whilst the original subcortical group will become localized in the primordial germ cells.

Animals↗
PubMed1972

Isolation and characterization of the sarcoplasmic reticulum of skeletal muscle.

The sarcoplasmic reticulum (SR) of rabbit skeletal muscle was studied after isolation of a vesicle fraction and of vesicular subfractions by means of differential and density gradient centrifugations. The different fractions were examined electron microscopically by negative and positive staining; their content in protein and phospholipid and their ability to bind Ca(++) were determined. After homogenization, differential centrifugation yielded a "sarcovesicular fraction" (SVF) which was mainly composed of numerous vesicles of different types mixed with fibrous proteins and mitochondrial fragments. This SVF contained 2% of the protein and 25% of the phospholipid of the initial tissue extract. It had a high Ca(++) binding activity that was preserved for several days by storage in the presence of oxalate. After centrifugations of the SVF on sucrose density gradients, two vesicular subfractions were obtained which were characterized by different sedimentation rates, isopycnic banding, morphology, and composition in protein and phospholipid. (a) The low-density subfraction (rho 1.10-1.12) contained a heterogeneous population of membranous structures: thick- and thin-walled vesicles, tubular formations, triads, and plasma membranes. Its content in protein and phospholipid was very low. (b) The high-density subfraction (rho 1.13-1.17) was a very pure subfraction composed only of thin-walled vesicles. Its content in phospholipid was high and the ratio of phospholipid-phosphorus to protein was about 20. The calcium-binding activity found in the total SVF was recovered only in this latter homogeneous subfraction. The origin of these two subfractions from the SR is discussed.

Animals↗
PubMed1973

Mitochondrial biogenesis during differentiation of Artemia salina cysts.

Mitochondria isolated from cysts of Artemia salina (brine shrimp) were found to be devoid of cristae and to possess a low respiratory capability. Hydration of the cysts induces marked biochemical and morphological changes in the mitochondria. Their biogenesis proceeds in two stages. The first stage is completed within 1 h and is characterized by a rapid increase in the respiratory capability of the mitochondria, their cytochrome oxidase, cytochrome b, cytochrome c and perhaps some morphological changes. In the second stage there is an increase in the protein-synthesizing capacity of the mitochondria as well as striking changes in mitochondrial morphology leading to the formation of cristae.

Animals↗