Increased histaminase activity in the atrophic muscle of denervated frog.

Sciatic denervation for 1 month in the frog Rana hexadactyla resulted in progressive atrophy of the gastrocnemius muscle without any change in the total DNA content of the whole muscle. Histamine content of the muscle decreased; glutamic and acid content increased and histidine level remained unaltered on denervation. Histaminase activity localized in the muscle decreased; glutamic acid content increased and histidine level remained unaltered on denervation. Histaminase activity localized in the muscle mitochondria increased on denervation. The histidine-degrading enzymes, histidine ammonia lyase, urocanate hydratase and imidazol-5yl lactate dehydrogenase, are localized in the sarcoplasm of the muscle and their activities are not altered on denervation. The histidine decarboxylase activity localized in the mitochondria is not altered on denervation. The reduction in the histamine content of the atrophied muscle may be due to increased mitochondrial histaminase activity but not due to increased decarboxylation of histidine. The loss of 'trophic influence' due to denervation may be manifested in the impairment of mitochondrial histaminase activity.     

Cytochrome c oxidase in prokaryotes

Abstract Several heme aa ₃-type cytochrome c oxidases, purified from the cytoplasmic membranes of bacteria, are able to catalyze the same reactions as the structurally far more complex eukaryotic enzyme, i.e., electron transport from cytochrome c to oxygen coupled to proton translocation. However, these oxidases show a very simple subunit pattern, and moreover, individual polypeptides even have homologous amino-acid sequences. This review summarizes the present data on purified bacterial cytochrome c oxidases and relates these findings to results obtained with the mitochondrial enzymes.     

Cytochrome oxidase in health and disease

Yeast and bovine cytochrome c oxidases (COX) are composed of 12 and 13 different polypeptides, respectively. In both cases, the three subunits constituting the catalytic core are encoded by mitochondrial DNA. The other subunits are all products of nuclear genes that are translated on cytoplasmic ribosomes and imported through different transport routes into mitochondria. Biogenesis of the functional complex depends on the expression of all the structural and more than two dozen COX-specific genes. The latter impinge on all aspects of the biogenesis process. Here we review the current state of information about the functions of the COX-specific gene products and of their relationship to human COX deficiencies.     

Cytochrome oxidase activity in bone tissue

Cytochrome oxidase activity was studied in articular and epiphyseal cartilage, in bone tissue and in callus. Changes in the activity of the enzyme were observed after ischaemic condition. Activity was the highest in the epiphyseal cartilage while in the other structures it decreased in the order of articular cartilage, chondroid tissue, newly formed woven bone, connective tissue cells, immature, preexisting lamellar bone tissue. It is assumed that differences in enzyme activity are due to differences in metabolic rate. The higher the activity of a structure in the intact state, the more marked was its decrease upon ischaemia. This implies that cells of higher metabolic rate are more sensitive to ischaemia.     

Cytochrome oxidase and ascorbic acid oxidase activities in cereal plants

Cytochrome oxidase and ascorbic acid oxidase activities were investigated in rye, wheat, barley and oat plants. The variations in the activity of both enzymes was followed in the course of the initial 28 days of growth, as well as at the phase of milk ripeness, namely in the cytoplasmic and mitochondrial cell fractions of roots, leaves and spikes. Both enzymes were active in all measurements. Cytochrome oxidase mostly exhibited a higher activity than ascorbio acid oxidase. The activity of the former enzyme was substantially higher in the mitochondrial fraction of leaves, roots and spikes of the four experimental plants in comparison with the cytoplasmic fraction. On the contrary, the ascorbic acid oxidase activity varied in both cell fractions according to the plant species, organ and growth phase. The variations in the activity of both enzymes exhibited on the whole a course similar to that of the respiration rate. During the first 14 to 21 days of growth the enzyme activities increased up to the maximum. This was thon followed at first by a rapid, later on by a slow decrease. The course of variations in the enzyme activities was, with certain exceptions, alike in all the four plant species investigated.     

Cytochrome c oxidase dysfunction in oxidative stress

Cytochrome c oxidase (CcO) is the terminal oxidase of the mitochondrial electron transport chain. This bigenomic enzyme in mammals contains 13 subunits of which the 3 catalytic subunits are encoded by the mitochondrial genes. The remaining 10 subunits with suspected roles in the regulation, and/or assembly, are coded by the nuclear genome. The enzyme contains two heme groups (heme a and a3) and two Cu(2+) centers (Cu(2+) A and Cu(2+) B) as catalytic centers and handles more than 90% of molecular O(2) respired by the mammalian cells and tissues. CcO is a highly regulated enzyme which is believed to be the pacesetter for mitochondrial oxidative metabolism and ATP synthesis. The structure and function of the enzyme are affected in a wide variety of diseases including cancer, neurodegenerative diseases, myocardial ischemia/reperfusion, bone and skeletal diseases, and diabetes. Despite handling a high O(2) load the role of CcO in the production of reactive oxygen species still remains a subject of debate. However, a volume of evidence suggests that CcO dysfunction is invariably associated with increased mitochondrial reactive oxygen species production and cellular toxicity. In this paper we review the literature on mechanisms of multimodal regulation of CcO activity by a wide spectrum of physiological and pathological factors. We also review an array of literature on the direct or indirect roles of CcO in reactive oxygen species production.     

Cytochrome oxidase histochemistry in the rat hippocampus

Summary The diaminobenzidine (DAB) method was adapted for the microphotometric determination of cytochrome c oxidase (cyt ox) in the rat hippocampus. The qualitative and quantitative investigations at the light microscopic level showed that acetone and cytochrome c pretreatment of cryostat sections resulted in a significant increase of demonstrable cyt ox activities. The final incubation medium consisted of 7.5 mM DAB, 2% polyvinylalcohol (PVA) and 6% dimethyl sulfoxide in 0.1 M Hepes buffer; final pH 7.5. PVA was used to keep DAB and artificially oxidized DAB in solution. In the kinetic and endpoint measurements a linear response of the reaction with highest slope was observed only in the initial 5–6 min of reaction. Thereafter the slope decreased. Ultracytochemical demonstrations, which were performed as a topochemical control, showed reaction product only in mitochondria (cristae and intermembranous space). In contrast to vibrotome sections all mitochondria reacted positively in cryostat sections of aldehyde-fixed hippocampi. The enhancement of reaction after acetone pretreatment of cryostat sections (light microscopic level) and after a freezing step in ultracytochemistry is discussed in connection with diffusion problems of DAB through mitochondrial membranes.Dedicated to Professor Dr. G. Lang on the occasion of his 65th birthdaySupported by the Deutsche Forschungsgemeinschaft (Ku 541/2-1)     

Cytochrome oxidase as a proton pump

The general structure of cytochrome oxidase is reviewed and evidence that the enzyme acts as a redox-linked proton pump outlined. The overall H⁺/e ^– stoichiometry of the pump is discussed and results [Wikström (1989),Nature 338, 293] which suggest that only the final two electrons which reduce the peroxide adduct to water are coupled to protein translocated are considered in terms of the restrictions they place on pump mechanisms. Direct and indirect mechanisms for proton translocation are discussed in the context of evidence for redox-linked conformational changes in the enzyme, the role of subunit III, and the nature of the Cu_A site.