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PubMed1977

Thermosensitive respiratory deficiency in yeast associated with specific effects on particulate cytochrome oxidase.

A mutant of Saccharomyces cerevisiae, unable to grow at the expense of non fermentable carbon sources at 37 degrees C, has been selected; at 25 degrees C the mutant strain behaves like the parental wild strain. Evaluations of respiration rates during aerobic growth at restrictive temperature on one hand, enzymatic and/or spectral evaluations of the individual components of the respiratory chain on the other hand show that the respiratory deficiency is specifically correlated with a reduced level of cytochrome oxidase. The decrease of enzyme activity is the direct consequence of a lowering of hemoprotein (a,a3) concentration. Temperature-activity relationship of cytochrome oxidase elaborated at the permissive temperature by the mutant strain is modified as far as the particulate enzyme is concerned, but no difference is observed after partial solubilization of the enzyme by non ionic surfactant. Genetic analysis shows that the mutant phenotype results from a nuclear gene mutation.

Aerobiosis↗
PubMed1994

Cortical cytochrome oxidase activity is reduced in Alzheimer's disease.

A defect in energy metabolism may play a role in the pathogenesis of neurodegenerative diseases, such as Alzheimer's disease. In the present study, we examined the activities of the enzymes that catalyze oxidative phosphorylation in frontal, temporal, parietal, and occipital cortex from Alzheimer's disease patients and age-matched controls. Complex I and complex II-III activities showed a small decrease in occipital cortex, but were unaffected in the other cortical areas. The most consistent change was a significant decrease of cytochrome oxidase (complex IV) activity of 25-30% in the four cortical regions examined. These results provide further evidence of a cytochrome oxidase defect in Alzheimer's disease postmortem brain tissue. A deficiency in this key energy-metabolizing enzyme could lead to a reduction in energy stores and thereby contribute to the neurodegenerative process.

Alzheimer Disease↗
PubMed2000

Alleviation of brain injury-induced cerebral metabolic depression by amphetamine: a cytochrome oxidase histochemistry study.

Measurements of oxidative metabolic capacity following the ablation of rat sensorimotor cortex and the administration of amphetamine were examined to determine their effects on the metabolic dysfunction that follows brain injury. Twenty-four hours after surgery, rats sustaining either sham operations or unilateral cortical ablation were administered a single injection of D-amphetamine (2 mg/kg; i.p.) or saline and then sacrificed 24 h later. Brain tissue was processed for cytochrome oxidase histochemistry, and 12 bilateral cerebral areas were measured, using optical density as an index of the relative amounts of the enzyme. Compared with that of the control groups, cytochrome oxidase in the injured animals was significantly reduced throughout the cerebral cortex and in 5 of 11 subcortical structures. This injury-induced depression of oxidative capacity was most pronounced in regions of the hemisphere ipsilateral to the ablation. Animals given D-amphetamine had less depression of oxidative capacity, which was most pronounced bilaterally in the cerebral cortex, red nucleus, and superior colliculus; and in the nucleus accumbens, caudateputamen, and globus pallidus ipsilateral to the ablation. The ability of D-amphetamine to alleviate depressed cerebral oxidative metabolism following cortical injury may be one mechanism by which drugs increasing noradrenaline release accelerate functional recovery in both animals and humans.

Amphetamine↗
PubMed1991

Organization of the superior olivary complex in the guinea pig. I. Cytoarchitecture, cytochrome oxidase histochemistry, and dendritic morphology.

The superior olivary complex is a prominent component of the auditory system. It consists of the lateral and medial superior olivary nuclei and a large number of smaller cell groups known as the periolivary nuclei, which are sources of both ascending and descending projections. The goal of this study was to establish criteria for identifying the periolivary nuclei in the guinea pig. Use of Nissl stains, the Golgi impregnation technique, and cytochrome oxidase histochemistry allowed us to distinguish eleven periolivary nuclei on the basis of differences in the types of cells they contain, in the distribution of cell types, and in the cytochrome oxidase staining characteristics of both the cells and the neuropil. The nuclei, named according to their position with respect to the lateral and medial superior olivary nuclei, can be divided into four groups: (1) a lateral group comprising the lateral nucleus of the trapezoid body and the anterolateral and posteroventral periolivary nuclei, (2) a dorsal group comprising the dorsal and dorsolateral periolivary nuclei, (3) a ventral group comprising the ventral nucleus of the trapezoid body and the anteroventral, ventromedial and rostral periolivary nuclei, and (4) a medial group comprising the medial nucleus of the trapezoid body and the superior paraolivary nucleus. Cytological distinctions among the periolivary nuclei are consistent with other evidence that they serve different functions and highlight the need for detailed study of their connections, immunocytochemistry and physiological response properties.

Animals↗
PubMed1993

Laminar organization of acetylcholinesterase and cytochrome oxidase in the lateral geniculate nucleus of prosimians.

Hess and Rockland [Hess and Rockland (1983) Brain Res. 289, 322-325] proposed that the distribution of acetylcholinesterase within the lateral geniculate nucleus might correlate with the daily activity patterns shown by primates. In diurnal primates, the magnocellular laminae show a greater acetylcholinesterase reaction product. In nocturnal primates, the parvocellular laminae are more heavily stained. We have examined the laminar distribution of acetylcholinesterase and cytochrome oxidase in the lateral geniculate nucleus of a series of rare prosimian primates. In all prosimians examined, the most dense acetylcholinesterase reaction product is seen in the parvocellular layers of the lateral geniculate nucleus. Heavy cytochrome oxidase activity is seen in both the magnocellular and parvocellular layers, but not the koniocellular layers of the prosimian lateral geniculate nucleus. We have also employed a polyclonal antibody to choline acetyltransferase to examine the laminar organization or cholinergic activity in the Galago (Bushbaby) lateral geniculate nucleus. We report that choline acetyltransferase immunoreactivity does not correlate with acetylcholinesterase activity in the prosimian lateral geniculate nucleus. Although the lateral geniculate nucleus is more immunoreactive than most other thalamic structures and although the intercalated koniocellular laminae demonstrate somewhat lighter choline acetyltransferase immunoreactivity, no great difference in staining intensity is seen between the parvocellular and magnocellular laminae. In addition, we examined the phenotype of known inputs to assess the laminar specificity of cholinergic projections to the bushbaby lateral geniculate nucleus. Layer VI of primary visual cortex, which is known to be a source of acetylcholinesterase in the parvocellular layers, does not contain cholinergic cells, nor does the pretectal nucleus, which projects mainly to the parvocellular layers. The parabigeminal nucleus is cholinergic; however, this nucleus is known to project to the koniocellular layers, along with the non-cholinergic superior colliculus. Finally, the pedunculopontine tegmental nucleus, which provides a strong input to many regions of the thalamus, including the lateral geniculate nucleus, is cholinergic. The laminar organization of its input to the lateral geniculate nucleus is not known. Increased acetylcholinesterase reaction product within the parvocellular layers of the lateral geniculate nucleus is common to all strepsirhine primates. The pattern is also seen in the only two nocturnal haplorhine primates, Tarsius and Aotus (owl monkey). The relation of this increased acetylcholinesterase activity to cholinergic function remains unclear.(ABSTRACT TRUNCATED AT 400 WORDS)

Acetylcholinesterase↗
PubMed1998

Cytochrome oxidase and NADPH-diaphorase on the afferent relay branch of the optokinetic reflex in the opossum.

In the present study, histochemical techniques combined with more conventional anatomical methods were used to refine the identification of the nucleus of the optic tract and the nuclei of the accessory optic system in the opossum. The distribution of the enzyme cytochrome oxidase (CO) was examined in the cells and the neuropil of the opossum's mesodiencephalic region. Strong CO labeling was present in the nucleus of the optic tract (NOT)-dorsal terminal nucleus (DTN). Alternate sections, taken from animals that had received bilateral injections of horseradish peroxidase centered in the region of the inferior olive, were subjected to assays for CO and horseradish peroxidase. The region occupied by CO-labeled cells in the NOT-DTN superimposed with the one defined by retrogradely labeled cells. Cell counts along the NOT-DTN anteroposterior axis revealed that although the olivary and CO-positive cells were confined within similar boundaries, the latter are up to twofold more numerous than the former. As revealed by cytochrome oxidase histochemistry, the outlines of the NOT-DTN, the other pretectal nuclei and the nuclei belonging to the accessory optic system coincided with those revealed by the histochemistry for nicotinamide dinucleotide phosphate diaphorase (NADPH-d). After an intraocular injection of cholera toxin beta subunit and alternate sections processing for NADPH-d and CO, the distribution of labeled retinal terminal fields in the mesodiencephalic region was shown to be coincident with regions of high levels of histochemical labeling. These results are discussed in the light of previous anatomofunctional assessments of the pretectum and accessory optic system.

Animals↗
PubMed1992

Area 3a in the cat. I. A reevaluation of its location and architecture on the basis of Nissl, myelin, acetylcholinesterase, and cytochrome oxidase staining.

Current knowledge on the anatomy of area 3a of the cat mainly derives from the cyto- and myeloarchitectonic study of Hassler and Muhs-Clement (J Hirnforsch 6:377, 1964). Previous investigations in the cat had failed to identify a cortical region comparable to monkey's area 3a. In the present study, Nissl, myelin, acetylcholinesterase, and cytochrome oxidase staining techniques were applied to coronal and sagittal serial sections of the cat brain. Area 3a appears as a slender band of cortex between areas 4 and 3b, and in Nissl-stained sections it is mainly characterized by an attenuated granular layer IV, overlying a thin layer V with pyramidal cells of various sizes, including a few large ones. These cytoarchitectonic features are sufficient to differentiate area 3a from neighboring areas, although the borders between them are not sharp in many cases. After the Nissl staining, the acetylcholinesterase staining proved to be the most helpful in defining the structure and borders of area 3a. Acetylcholinesterase staining was dense in layer I (in contrast with a lighter staining of outer layer I in area 4), and light in layers II and IIIa, changing to moderate in IIIc and IV (a pattern which is accentuated in area 3b). Myelin and cytochrome oxidase techniques also yielded differential staining patterns of area 3a and neighboring areas 4 and 3b, although the borders were not easily drawn with these techniques. Whereas our cyto- and myeloarchitectonic findings were comparable to those of Hassler and Muhs-Clement ('64) and applied well to area 3a in the convexity of the hemisphere, we found that most of the area 3a described by these authors in the medial face of the hemisphere had a number of distinguishing architectonic (as well as connectional and physiological) features which enabled us to define it as a separate area (7m). The techniques we used to delineate area 3a are compatible with most current procedures of histo- and immunohistochemical staining of the brain, and may also provide valuable supporting data for electrophysiological studies.

Acetylcholinesterase↗
PubMed2002

Conductive hearing loss results in changes in cytochrome oxidase activity in gerbil central auditory system.

Conductive hearing loss (CHL) restricts auditory input to an intact peripheral auditory system. Effects of deprivation on the central auditory system (CAS) have been debated, although a number of studies support the hypothesis that CHL can cause modification of CAS structure and function. The present study was designed to test the hypothesis that unilateral CHL results in a decrease in cytochrome oxidase (CO) activity in CAS nuclei that receive major afferent input from the affected ear. Gerbils at postnatal day 12 (P21) or 6-8 weeks underwent left unilateral CHL (malleus removal), cochlear ablation, or a sham surgical procedure. After a survival time of 48 hours or 3 weeks, animals were sacrificed and tissue was processed for cytochrome oxidase histochemistry. Optical density (OD) measurements were made from individual neurons in the anteroventral cochlear nucleus (AVCN) and from medial and lateral dendritic fields in the medial superior olivary nucleus (MSO), the lateral superior olivary nucleus, and the inferior colliculus. The width of the CO-stained neuropil in MSO was also measured as an estimate of dendritic length. OD measures were corrected to neutral areas of the brain. Cochlear ablation caused significant decreases in CO activity in left lower brainstem nuclei, particularly in adult animals. Following CHL, a significant decrease in CO activity was observed in the ipsilateral AVCN and a significant increase was observed in the contralateral AVCN. Cochlear ablation resulted in decreased width of MSO neuropil containing dendrites that receive primary input from the ablated ear. CHL resulted in a significant increase in the width of MSO neuropil on both sides of the brain in the P21 animals that survived 3 weeks but not in P21 animals that survived only 48 hours or in the adult animals. Unilateral CHL is associated with changes in CO activity in the AVCN and may affect MSO dendritic length in younger animals.

Animals↗
PubMedDate not supplied

The stoichiometry of H+ pumping in cytochrome oxidase and the mechanism of uncoupling.

It is suggested that loose coupling in free energy transducing organelles is due partly to leaks through the phospholipid bilayer (extrinsic uncoupling) and partly to "slipping" of the proton pumps (intrinsic uncoupling). The flow ratio of the redox pumps (JH/JO) measured at level flow is not affected by extrinsic uncoupling, but it will be lower the higher the extent of intrinsic uncoupling. During operation of cytochrome oxidase with ferrocyanide or N,N,N',N'-tetraphenyl-p-phenylenediamine as substrates, the rate of resting respiration depends on substrate concentration and does not exhibit control by delta muH; the available data strongly suggest that the enzyme is intrinsically uncoupled to a high and variable (substrate concentration-dependent) extent. It is concluded that flow ratios (at level flows) provide underestimates of the cytochrome oxidase pump stoichiometry.

Biological Transport↗
PubMed1979

Photoreductive titration of the resonance Raman spectra of cytochrome oxidase in whole mitochondria.

A photoreductive titration of the resonance Raman (RR) spectra of cytochrome c oxidase in whole mitochondria was recorded by exploiting the preferential enhancement of the Raman signals of reduced cytochrome oxidase excited at 441.6 nm. When the sample was cooled to about--10 degrees C, it was possible to slow down the photoreductive effect of the laser and to record RR spectra at various states of reduction. Compared to the earliest recorded scan (most oxidized), the dithionite-reduced sample shows the appearance of new bands at 216, 363, 560, and 1665 cm-1. At intermediate stages of photoreduction, the 216- and 560-cm-1 bands appear before the 363- and 1665-cm-1 bands; photoreduction induces full intensity in the former bands, whereas the latter bands are photoreduced to 50% of the dithionite-reduced intensity. The relative intensities of a doublet at 1609--1623 cm-1 are affected by reduction: the band at 1609 cm-1 is weaker in the earlier scans; in later scans this band has grown to equal intensity with the 1623-cm-1 band. We conclude that this reductive titration of the RR spectrum of cytochrome c oxidase reflects three states in its reduction. The behavior of the doublet at 1609--1623 cm-1 suggests that the two hemes are nonequivalent but interacting. The band at 216 cm-1 may be indicative of an iron-copper interaction that is affected by the presence of external ligands.

Animals↗
PubMed1993

An interdigitated columnar mosaic of cytochrome oxidase, zinc, and neurotransmitter-related molecules in cat and monkey visual cortex.

There is considerable physiological evidence for the compartmentalization of mammalian visual cortex into functional columnar modules, representing features of visual information processing such as eye and orientation specificity. However, anatomical markers of visual cortical compartmentalization have been described only for primate visual cortex. In this report, we describe an interdigitated mosaic of four neuroactive molecules which demarcate two distinct columnar systems in the kitten visual cortex. Serotonin 1C receptors and synaptic zinc were found to demarcate columns within layer IV of kitten visual cortex, which were interdigitated with a second, patchy system characterized by increased levels of cytochrome oxidase and acetylcholinesterase. In primate visual cortex, as well as in the kitten, synaptic zinc was periodically distributed in a manner precisely complementary to cytochrome oxidase. These findings provide an anatomical framework on which unifying hypotheses of the functional organization of columnar systems in mammalian visual cortex can be built.

Acetylcholinesterase↗
PubMed1995

Triplet-state quenching in complexes between Zn-cytochrome c and cytochrome oxidase or its CuA domain.

The quenching of the triplet state of Zn-cytochrome c in electrostatic complexes with cytochrome oxidase and its soluble CuA domain has been studied by laser flash photolysis. The triplet state of free Zn-cytochrome c decayed with a rate of about 200 s-1. With the oxidase, biphasic decay with rate constants of 2 x 10(5) and 2 x 10(3) s-1, respectively, was observed. At high ionic strength (I = 0.2) the decay was the same as with free Zn-cytochrome c. The quenching was also eliminated by reduction of the oxidase. The decay rate in the complex with the CuA domain was 4 x 10(4) s-1. The results are interpreted in terms of rapid electron transfer to CuA and a slower one to cytochrome a. No electron transfer products were detected, because the backward reaction is faster than the forward one. This can be explained by the high driving force (1.1 eV) for the forward electron transfer, taking the system into the inverted Marcus region. The distance in the electrostatic complex between cytochrome c and the electron acceptor, presumed to be CuA, is calculated to be 16 A.

Animals↗
PubMed1986

Isolation and characterization of human heart cytochrome c oxidase.

Cytochrome c oxidase was isolated from human hearts and separated by SDS gel electrophoresis. The identity of polypeptide bands with known subunits was demonstrated by immunoblotting with monospecific antisera to rat liver cytochrome c oxidase subunits. The polarographically determined kinetics of cytochrome c oxidation were similar to those reported for the bovine heart enzyme.

Animals↗
PubMed1997

Spatio-temporal frequency domains and their relation to cytochrome oxidase staining in cat visual cortex.

Spatial and temporal frequencies are important attributes of the visual scene. It is a long-standing question whether these attributes are represented in a spatially organized way in cat primary visual cortex. Using optical imaging of intrinsic signals, we show here that grating stimuli of different spatial frequencies drifting at various speeds produce distinct activity patterns. Rather than observing a map of continuously changing spatial frequency preference across the cortical surface, we found only two distinct sets of domains, one preferring low spatial frequency and high speed, and the other high spatial frequency and low speed. We compared the arrangement of these spatio-temporal frequency domains with the cytochrome oxidase staining pattern, which, based on work in primate striate cortex, is thought to reflect the partition of the visual cortex into different processing streams. We found that the cytochrome oxidase blobs in cat striate cortex coincide with domains engaged in the processing of low spatial and high temporal frequency contents of the visual scene. Together with other recent results, our data suggest that spatiotemporal frequency domains are a manifestation of parallel streams in cat visual cortex, with distinct patterns of thalamic inputs and extrastriate projections.

Animals↗
PubMed2005

Porin and cytochrome oxidase containing contact sites involved in the oxidation of cytosolic NADH.

Cytochrome c (cyto-c) added to isolated mitochondria promotes the oxidation of extra-mitochondrial NADH and the reduction of molecular oxygen associated to the generation of an electrochemical membrane potential available for ATP synthesis. The electron transport pathway activated by exogenous cyto-c molecules is completely distinct from the one catalyzed by the respiratory chain. Dextran sulfate (500 kDa), known to interact with porin (the voltage-dependent anion channel), other than to inhibit the release of ATP synthesized inside the mitochondria, greatly decreases the activity of exogenous NADH/cyto-c system of intact mitochondria but has no effect on the reconstituted system made of mitoplasts and external membrane preparations. The results obtained are consistent with the existence of specific contact sites containing cytochrome oxidase and porin, as components of the inner and the outer membrane respectively, involved in the oxidation of cytosolic NADH. The proposal is put forward that the bi-trans-membrane electron transport chain activated by cytosolic cyto-c becomes, in physio-pathological conditions: (i) functional in removing the excess of cytosolic NADH; (ii) essential for cell survival in the presence of an impairment of the first three respiratory complexes; and (iii) an additional source of energy at the beginning of apoptosis.

Adenosine Triphosphate↗
PubMed2000

Redox status of cytochrome oxidase in darkened leaf of C4 crop plants.

Light is essential for growth, development and various metabolic processes in plant. One-third of the whole intact leaf blades of pearlmillet and maize were covered (treated leaf) with a black opaque plastic sheet at the middle region for 15 days. The leaf samples were taken from three regions: basal, middle and distal; from treated and parallel untreated leaves (control). Oxygen uptake was measured from all the three regions by taking randomized leaf discs. Oxygen uptake was nearly the same in all the regions of treated and parallel untreated leaf in pearlmillet and maize. Carbon monoxide used at 0.5 mM concentration with pearlmillet inhibited oxygen uptake slightly (22%) in covered leaf blade, whereas the inhibition with maize leaf at 1.12 mM CO was significantly higher (45%). However, CO did not inhibit oxygen uptake in untreated leaf from pearlmillet and maize. In contrast. cyanide brought about 33%, inhibition in oxygen uptake at 0.25 mM with pearlmillet and 60%, with maize at 0.4 mM, irrespective of the fact whether a portion of the leaf blade was covered or not with an opaque sheet. The results indicate that removing light from a portion of the leaf blade alters the redox state of the whole leaf in terms of an increase in the level of the ferrocytochrome a3 component of cytochrome c oxidase (cytochrome aa3).

Carbon Monoxide↗