Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A histochemical analysis of mitochondrial enzyme activity was carried out in 103 human diaphragmatic skeletal muscles from 49 subjects of different ages, obtained either at the time of abdominal surgery or at necropsy. Evidence of respiratory failure (cytochrome oxidase negativity) was seen in occasional fibres from the fourth decade on with an approximate 10-fold increase between the fourth and ninth decade (0.16% to 2.85%). A similar incidence of mitochondrial failure in CNS neurones to that documented in skeletal muscle could easily account for attrition of 25% of neurones over a 50-year period as reported in the literature. Possible theoretical relationships between morphological markers of mitochondrial failure and cell attrition are explored. While the projections from muscle to neurone are somewhat speculative, it is clear that if a similar extent of mitochondrial pathology exists in the brain to that documented in skeletal muscle, this could easily account for neuronal loss in the ageing brain.
Mutat Res 1992 Sep
PMID:Respiratory chain failure in adult muscle fibres: relationship with ageing and possible implications for the neuronal pool. 138 55

Previous studies on mitochondrial targeting presequences have indicated that formation of an amphiphillic helix may be required for efficient targeting of the precursor protein into mitochondria, but the structural details are not well understood. We have used CD and NMR spectroscopy to characterize in detail the structure of a synthetic peptide corresponding to the presequence for the beta-subunit of F1-ATPase, a mitochondrial matrix protein. Although this peptide is essentially unstructured in water, alpha-helix formation is induced when the peptide is placed in structure-promoting environments, such as SDS micelles or aqueous trifluoroethanol (TFE). In 50% TFE (by volume), the peptide is in dynamic equilibrium between random coil and alpha-helical conformations, with a significant population of alpha-helix throughout the entire peptide. The helix is somewhat more stable in the N-terminal part of the presequence (residues 4-10), and this result is consistent with the structure proposed previously for the presequence of another mitochondrial matrix protein, yeast cytochrome oxidase subunit IV. Addition of increasing amounts of TFE causes the alpha-helical content to increase even further, and the TFE titration data for the presequence peptide of the F1-ATPase beta-subunit are not consistent with a single, cooperative transition from random coil to alpha-helix. There is evidence that helix formation is initiated in two different regions of the peptide. This result helps to explain the redundancy of the targeting information contained in the presequence for the F1-ATPase beta-subunit.
Biochim Biophys Acta 1992 Sep 04
PMID:Conformational analysis of a mitochondrial presequence derived from the F1-ATPase beta-subunit by CD and NMR spectroscopy. 139 Sep 13

The protective effect of a new oligomeric derivative of prostaglandin B2, known as OC-5186, was evaluated using time-sharing spectrofluorometry in the cold-preserved rat liver. Experiments were divided into three groups: in group A, a 5000 ng dose of OC-5186 was administered via the peripheral vein, 1000 ng via the portal vein, and 200 ng/ml in University of Wisconsin (UW) solution; in group B, the OC-5186 dosage was ten times greater than that in group A; in group C (control group), liver procurement and storage were performed without OC-5186. At 0, 12, and 24 h after cold preservation at 4 degrees C, the liver was perfused for 30 min at 12 degrees C with oxygenized Krebs-Henseleit solution, after which the perfusate was switched to deoxygenized Krebs-Henseleit solution. Time sharing spectrofluorometry was used to follow NADH fluorescence at 450 nm with a 360-nm excitation wavelength, as well as the reflectance of cytochrome aa3 with 605 minus 620 nm from oxidation to reduction. Rate constants of NADH fluorescence and cytochrome aa3 reflectance were used as indices of integrity of the mitochondrial respiratory chain. In group C, the rate constant of NADH fluorescence decreased significantly (P < 0.05) from the control value of 8.31 +/- 0.21 x 10(-3) (sec-1) to 4.97 +/- 0.15 x 10(-3) and 5.58 +/- 0.16 x 10(-3) (mean +/- SEM) at 12 and 24 h after cold preservation, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
Transpl Int 1992 Sep
PMID:Protective effect of a prostaglandin oligomer on liver mitochondria in situ: time-shared measurements of fluorescence and reflectance in the cold-preserved rat liver. 141 8

During earlier fat cell studies we noticed that homogenates of white fat cells became more brown with training, a fact that might reflect an increased content of mitochondria. This raised the question whether training (as is the case in muscle) increases the oxidative capacity in fat cells. Groups of 8-12 rats were swim trained for 10 wk or served as either sedentary, sham swim-trained, or cold-stressed controls. White adipose tissue was removed, and the activities of the respiratory chain enzyme cytochrome-c oxidase (CCO) and of the enzyme malate dehydrogenase (MDH), which participates in the tricarboxylic acid cycle as well as in the mitochondrial malate-aspartate and acetyl-group shuttles, were determined. The CCO and MDH activities expressed per milligram protein were increased in male rats 4.4- and 2.8-fold, respectively, in the swim-trained compared with the sham swim-trained rats (P less than 0.05). In female rats the CCO activity expressed per milligram protein was increased 4.5-fold in the trained compared with the sedentary control rats (P less than 0.01). Neither cold stress nor sham swim training increased CCO or MDH activities in white adipose tissue (P greater than 0.05). In conclusion, in rats, intensive endurance training induces an increase in mitochondrial enzyme activities in white adipose tissue as is seen in skeletal muscle.
Am J Physiol 1991 Sep
PMID:Increased activities of mitochondrial enzymes in white adipose tissue in trained rats. 165 28

Thioridazine interacts with purified cardiac cytochrome oxidase altering both the activity of the enzyme and the optical spectrum of the drug. Cytochrome oxidase activity, as measured by oxidation of cytochrome c, exhibits a biphasic response to changing drug concentration. Lower concentrations of thioridazine increased cytochrome oxidase activity up to 20% at 65 microM and higher concentrations inhibit activity until almost complete inhibition is observed. Both the activation and the inhibition of cytochrome oxidase by thioridazine follow Michaelis-Menton kinetics with Vmax changing but Km remaining constant. The analysis of the 2 nm shift in the UV absorption spectrum of the thioridazine suggest that the binding of thioridazine to cytochrome oxidase involves multiple (535) binding sites on the enzyme with an average dissociation constant of 20 microM.
Biochem Biophys Res Commun 1991 Sep 16
PMID:The interaction of thioridazine with cardiac cytochrome oxidase; enzyme activity and drug binding studies. 165 98

Neuron L7 of the marine mollusc, Aplysia californica, is unique in that it innervates five different target tissues in the animal. We show that when L7 is grown in vitro with two of these targets, that is, muscle cells isolated from the auricle or the gill vein, newly formed L7 neurites contact the muscle cells. Chemical synapses are formed since intracellular stimulation of L7 elicits contraction of individual muscle cells. Interestingly, auricle muscles are also innervated by neuron RBhe and co-cultures of RBhe and auricle muscle cells also exhibit synapse formation. To explore the molecular basis for synaptogenesis between L7 and its targets, it would be useful to quantify the extent of synapse formation in vitro, that is, to determine how many muscle cells can be innervated by a single L7. We show that this can be attained by staining for cytochrome oxidase activity. Cultures of auricle and gill vein muscles were exposed to the appropriate neurotransmitter in order to elicit contraction. The cells were then fixed and stained. In both cases, only cells that contracted were stained and electron microscopy showed reaction product associated with the cristae of mitochondria. When this procedure was applied to cultures of L7 and muscle cells, 38 +/- 2.8% (S.E.M.; n = 7) of the cells on the neurites were stained and therefore responded to L7 stimulation. Thus, part of the L7-RBhe circuit can be assembled in vitro and the extent of synaptogenesis can be accurately quantitated.
J Neurobiol 1991 Sep
PMID:Cytochrome oxidase activity as a measure of synaptogenesis by multifunctional neuron L7 of Aplysia. 165 72

Metabolism of methanol, methyl ethers, esters and amides give rise to formic acid. This acid is an inhibitor of the mitochondrial cytochrome oxidase causing histotoxic hypoxia. Formic acid is a weaker inhibitor than cyanide and hydrosulphide anions. The body burden of formate in methanol poisoning is high enough to cause acidosis, and other clinical symptoms. Part of the protons can be attributed to formic acid whereas the most significant acid load results from the hypoxic metabolism. The acidosis causes e.g. dilatation of cerebral vessels, facilitation of the entry of calcium ions into cells, loss of lysosomal latency and deranged production of ATP. The latter effect seems to impede parathormone-dependent calcium reabsorption in the kidney tubules. Besides, urinary acidification is affected by formic acid. Its excretion causes continuous recycling of the acid by the tubular cell Cl-/formate exchanger. This sequence of events may partially explain an accumulation of formate in urine. Occupational exposure to vapours of methanol and formic acid can be quantitatively monitored by urinary formic acid determinations. Formic acid toxicity may prove a suitable model for agents causing histotoxic hypoxia.
Pharmacol Toxicol 1991 Sep
PMID:Methanol and formic acid toxicity: biochemical mechanisms. 166 61

Recently the pH gradient evoked by a K+ diffusion potential was shown to translocate a synthetic monobasic amphipathic hexapeptide across the bilayer of lipid vesicles (De Kroon, A.I.P.M., Vogt, B., Van 't Hof, R., De Kruijff, B. and De Gier, J. (1991) Biophys. J. 60, in press). Here this observation is extended by studying the effect of a membrane potential on a set of bioactive peptides. The panel of peptides comprises the toxin mastoparan X, a tryptophan-containing analogue of the presequence of the mitochondrial protein cytochrome oxidase subunit IV (preCoxIV(1-25)W18), and the regulatory peptides ACTH(1-24), alpha-MSH, ACTH(1-10), dynorphin A, bombesin, and LHRH. The interaction of these peptides with phospholipid vesicles has been measured using the intrinsic tryptophan residue as fluorescent probe. In the absence of a K+ diffusion potential only mastoparan X and the presequence show considerable binding to vesicles consisting of phosphatidylcholine (PC). In contrast, under these conditions all peptides display affinity for vesicles consisting of the acidic phospholipid cardiolipin (CL), the extent of which depends on the net positive charge of the peptide. Application of a K+ diffusion potential to large unilamellar vesicles (LUV) consisting of PC results in a time dependent tryptophan fluorescence increase for mastoparan X, which is accelerated upon incorporating increasing amounts of CL into the LUV. A similar fluorescence increase in response to a K+ diffusion potential was observed for the above model peptide. Yet the mechanism resulting in the fluorescence increase of mastoparan X is completely different from that of the hexapeptide. Binding experiments indicate that a membrane potential-induced enhanced binding of the peptide to the outer surface of the vesicles contributes to the fluorescence increase. PreCoxIV(1-25)W18, dynorphin A, and ACTH(1-24) show fluorescence responses upon applying a membrane potential that are consistent with that of mastoparan X, whereas the other peptides tested do not respond up to a LUV CL content of 50%. The results tentatively suggest that the membrane potential only affects a peptide when it has the ability to adopt a stable membrane bound conformation.
Biochim Biophys Acta 1991 Sep 30
PMID:The effect of a membrane potential on the interaction of mastoparan X, a mitochondrial presequence, and several regulatory peptides with phospholipid vesicles. 168 Mar 97

The lateral magnocellular nucleus (LM) contains the largest neurons in the rabbit thalamus, yet its cortical connections have not been described. This study evaluates the architecture, cingulate cortical connections, and spontaneous rate of neuronal discharges in LM. At its maximal mediolateral extent in coronal sections, LM underlies the laterodorsal and lateroposterior nuclei. It has a short medial and long lateral limb, both of which have high levels of cytochrome oxidase activity. On the basis of horseradish peroxidase and fluorescent dye injections, LM projects primarily to area 29 and posterior area 24. Projections to area 29d are topographically organized so that the medial limb of LM projects to rostral area 29d, mid levels of LM where the limbs join project to midlevels of area 29d and lateral parts of the lateral limb project to posterior area 29d. It is mainly the midportion of the lateral and medial limbs that projects to areas 29b and 29c. The anterior parts of these areas receive input from dorsal parts of LM, whereas posterior levels of these areas receive input from ventral LM. The midregion of LM also projects to caudal area 24. Injections of 3H-amino acids into area 29d anterogradely label neuronal processes in LM. Finally, single unit electrophysiological recordings from LM in halothane-anesthetized rabbits showed a unique pattern of spontaneous discharges. Over 70% of the LM neurons cycled through a number of different phases with a mean +/- S.E.M. peak discharge rate of 31 +/- 4.7 Hz. This high rate contrasts with the 17.6 +/- 3.2 Hz rate for neurons that maintained a constant rate of discharge and the 7.5 +/- 1.3 Hz rate of discharges for neurons in nuclei dorsal and ventral to LM. LM neurons are large, have high levels of cytochrome oxidase and spontaneous activity, and project extensively to the posterior cingulate cortex. These features suggest that LM neurons are highly active metabolically and may be fast conducting efferents to cingulate cortex.
J Comp Neurol 1990 Sep 01
PMID:Lateral magnocellular thalamic nucleus in rabbits: architecture and projections to cingulate cortex. 169 39

The first mitochondrial-encoded gene of an archegoniate has been identified, cloned and sequenced. The cytochrome oxidase III gene (cox3) of the moss Physcomitrella patens consists of a 618 bp open reading frame with high homology (around 72%) to known cox3 sequences of higher plants. Nevertheless, it is a quarter shorter than these. The cox3 gene of P. patens contains no introns and reveals a G + C-content of 41.3%. The region containing the cox3 gene exists as a single copy in the mitochondrial genome as shown by restriction mapping. In the 5' flanking sequence a putative ribosome binding site and a putative secondary structure were found. Two main transcripts of 2.4 kb and 2.6 kb were detected indicating a complex mitochondrial transcription pattern possibly due to co-transcription. Additional open reading frames were found downstream from, as well as upstream of, the cox3 gene. In Western blots a polyclonal cox3 antibody from yeast detected one single band with an apparent molecular weight of 22 kDa.
Curr Genet 1991 Sep
PMID:The first analysed archegoniate mitochondrial gene (COX3) exhibits extraordinary features. 171 13


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