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  • 1
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The oxidative response to phagocytosis by chicken polymorphonuclear leucocytes was investigated as compared to guinea pig polymorphonuclear leucocytes. The polymorphs from both species respond to phagocytosis with an increased oxygen consumption, an increased generation of O2 − and H2O2, and an increased oxidation of glucose through the hexose monophosphate shunt. The rate of oxygen consumption, and generation of O2 − and H2O2 by phagocytosing chicken polymorphonuclear leucocytes is considerably lower than with phagocytosing guinea pig polymorphonuclear leucocytes. By contrast, the extent of hexose monophosphate shunt stimulation in chicken polymorphs is comparable to that of guinea pig polymorphs. Evidence is presented suggesting that H2O2 is preferentially degraded in chicken cells through the glutathione cycle, whereas catalase and myeloperoxidase are the two main H2O2 degrading enzymes in guinea pig cells. The 20,000 g fraction of the postnuclear supernatant of chicken polymorphs contains a cyanide-insensitive NADPH oxidizing activity which is stimulated during phagocytosis. Similar properties for the NADPH oxidizing activity of guinea pig polymorphs have been previously reported. It is concluded that the metabolic burst of phagocytosing chicken polymorphonuclear leucocytes is qualitatively similar to that of guinea pig polymorphonuclear leucocytes, but the latter cells are more active in all the biochemical parameters that have been measured. The difference in the H2O2 degradation pathways between the two species is accounted for by the lack of myeloperoxidase and catalase in chicken polymorphs.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The effects of several known inhibitors and activators of peroxidase-catalyzed reactions have been studied on the NADPH oxidase activity of granules isolated from polymorphonuclear leukocytes at rest or during phagocytosis. Redogenic substances, such as ascorbate or hydroquinone, and superoxide dismutase, which are known to inhibit peroxidase-catalyzed reactions, also inhibited the NADPH oxidase activity of granules. Oxidogenic substances, such as guaiacol or resorcinol, and manganese, which are known to stimulate peroxidase-catalyzed reactions, also activated the NADPH oxidase activity of granules. Cyanide, an inhibitor of peroxidase-catalyzed reactions, inhibited the NADPH oxidase activity of granules isolated from resting leukocytes but only slightly affected that of granules isolated from phagocytosing cells, as previously reported. A list of the properties of the NADPH oxidase activity of granules and of peroxidase oxidase activity is given. The arguments in favor of and those against a possible identity of the two activities are discussed.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The protease inhibitor,L-1-tosylamide-2-phenylethylchloromethyl ketone (TPCK), stimulated the O 2 − production, H2O2 generation, oxygen consumption, and the hexose monophosphate shunt of guinea pig peritoneal polymorphs. Other protease inhibitors were not able to stimulate the metabolic burst of these cells. Maximum stimulation was obtained at 100 µM concentration of the compound. No stimulation was seen in human blood polymorphs even at concentrations higher than those effective on guinea pig polymorphs. TPCK also stimulated the oxidative metabolism of guinea pig blood polymorphs and of guinea pig resident peritoneal macrophages. At concentrations which did not stimulate the oxidative metabolism of guinea pig polymorphs, TPCK inhibited the O 2 − production induced in these cells by treatment with phorbol myristate acetate (PMA) or with other soluble stimuli. Other protease inhibitors also inhibited the respiratory burst induced by PMA. It is concluded that TPCK exerts two effects on the metabolism of guinea pig phagocytes, which are probably mediated by different mechanisms. The inhibitory effect on the PMA-stimulated respiratory burst might be related to the antiprotease activity of TPCK, while the stimulation of the respiratory burst seems to be independent of protease inhibition.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract This study investigated the interaction between neutrophil myeloperoxidase (MPO) and the C1q component of the complement system. Using a dot-spot assay, MPO was found to bind to C1q in a dose-dependent manner. The specificity of this reaction was proved by the inhibitory effect of F(ab')2 antibodies to C1q and by the inability of MPO to bind to Clr, Cls and IgG. The interaction between MPO and C1q did not influence the enzymatic activity of the peroxidase but resulted in a more stable C1q as assessed by hemolytic assay for C1q. The protective effect of MPO on C1q did not require the presence of H2O2 in the reaction mixture nor was it inhibited by sodium azide, whereas it was abolished by heating the peroxidase. Lactoferrin and lysozyme, unlike MPO, were ineffective in protecting C1q from functional decay. Addition of H2O2 and chloride to MPO and C1q led to a complete inactivation of C1q, which could not be induced by H2O2 alone. The hypochlorite, which is known to be generated during the reaction of MPO with H2O2 and chloride, exhibited a similar inactivating effect on C1q, which was prevented by an external source of methionine.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 74 (1969), S. 17-29 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The respective importance of mitochondria and of sarcoplasmic reticulum in the uptake and maintenance of Ca++ by the isolated rat diaphragm has been compared. Diaphragms were incubated at 30° in conditions optimal for Ca++ uptake either by isolated mitochondria or by sarcoplasmic reticulum: more Ca++ was taken up from the “mitochondrial” medium. For maximal uptake, Pi and Mg++ were necessary; substitution of NaCl and KC1 with sucrose had no effect on the uptake. The uptake was markedly inhibited by uncouplers of oxidative phosphorylation, by respiratory inhibitors, and by lowering the temperature of the incubation medium to 0°; it was not affected by oligomycin, aurovertin, DCCD, nor by inhibitors of Ca++ transport in the isolated sarcoplasmic reticulum (ergotamine, ergobasinine, caffeine). The lack of effect of caffeine was not due to lack of penetration into the muscle. Permeability barriers for ergotamine and ergobasinine could not be excluded. The maintenance of Ca++ by the diaphragm was optimal in a medium contaming Pi and Mg++. Uncoupling agents and respiratory inhibitors accelerated the rate and extent of release of Ca++ by the diaphragm. Lowering the temperature of the incubation medium to 0°, or addition of oligomycin, aurovertin, DCCD, had no effect on the release. The release of Ca++ was also unaffected by ergotamine, ergobasinine, caffeine. The results suggest a role for mitochondria in the uptake and maintenance of Ca++ by the isolated diaphragm.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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