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Query: UMLS:C0043167 (pertussis)
 19,595 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Bordetella pertussis gene sodB, encoding superoxide dismutase (SOD), was cloned by complementation of an Escherichia coli sodAsodB double mutant. The nucleotide sequence of sodB predicted a 21-kDa protein with homology to manganese- and iron-containing SODs from other organisms. Examination of SOD activity on gels suggests that B. pertussis extracts have a single SOD containing Fe3+ as a prosthetic group. A SOD-deficient mutant was obtained by insertional inactivation of sodB in B. pertussis, confirming that there is only one SOD in this organism.
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PMID:Characterization of the gene encoding superoxide dismutase of Bordetella pertussis and construction of a SOD-deficient mutant. 818 62

Exposure of rats to hyperoxia or to treatment with endotoxin, increases lung manganese superoxide dismutase (MnSOD) gene expression. However, the paths by which these environmental signals are transduced into enhanced MnSOD gene expression are unknown. We now provide evidence that heterotrimeric G proteins are involved in the hyperoxia-induced increase in lung MnSOD gene expression but that pertussis toxin-sensitive G proteins are not involved in the endotoxin-induced elevation of lung MnSOD gene expression. We also show that treating rats with pertussis toxin decreased lung MnSOD activity approximately 50%. This decline in MnSOD activity occurred without a change in the lung activity of copper-zinc SOD, catalase, or glutathione peroxidase. In air-breathing rats, the pertussis toxin-induced decrease in MnSOD activity was associated with the development of lung edema, pleural effusion with a high concentration of protein, and biochemical evidence of lung oxygen toxicity. Compared to air-breathing rats, maintenance of pertussis toxin-treated rats under hypoxic or hyperoxic conditions respectively decreased or increased intrathoracic fluid. Endotoxin treatment elevated lung MnSOD activity and protected pertussis toxin-treated rats from an increase in intrathoracic fluid.
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PMID:Pertussis toxin treatment alters manganese superoxide dismutase activity in lung. Evidence for lung oxygen toxicity in air-breathing rats. 820 Sep 62

Bordetella pertussis produces a catalase and a Fe-superoxide dismutase. The importance of these enzymes in virulence was investigated, in vitro as well as in vivo, by using mutants deficient in their production. The catalase-deficient mutant survived within polymorphonuclear leukocytes, killed J774A.1 macrophages through apoptosis, and behaved as the parental strain in a murine respiratory infection model. These results suggest no direct role for catalase in B. pertussis virulence. The absence of expression of Fe-superoxide dismutase had profound effects on the bacterium including a reduced ability to express adenylate cyclase-hemolysin and pertactin, two factors important for B. pertussis pathogenesis. The Fe-superoxide dismutase-deficient mutant also had decreased abilities to colonize and persist in the murine respiratory infection model.
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PMID:In vivo and in vitro analysis of Bordetella pertussis catalase and Fe-superoxide dismutase mutants. 881 May 7

The novel human CC-chemokine Eotaxin is a potent and selective chemotaxin for eosinophils. Here, the biological activities and the activation profile of Eotaxin were further characterized and compared with those of other eosinophil chemotaxins such as complement fragment C5a (C5a), platelet-activating factor (PAF), and RANTES in human eosinophils. Eotaxin stimulated the production of reactive oxygen metabolites as shown by lucigenin-dependent chemiluminescence and superoxide dismutase-inhibitable cytochrome C reduction. Furthermore, Eotaxin induced upregulation of the integrin CD11b. In addition, fluorescence measurements with Fura-2-labeled eosinophils in the presence of EGTA indicated Ca(2+)-mobilization from intracellular stores by Eotaxin. Flow cytometric studies showed rapid and translent actin polymerization on stimulation with Eotaxin. At optimal concentrations, the changes induced by Eotaxin were comparable with those obtained by C5a, PAF, and RANTES. Call responses elicited by Eotaxin were inhibited by pertussis toxin, indicating coupling of its putative receptor to heterotrimeric guanine nucleotide-binding proteins. These results indicate that Eotaxin is a strong activator of eosinophils with biological activity comparable with those of the eosinophil chemotaxins C5a, PAF, and RANTES. These findings point to a role of Eotaxin in the pathogenesis of eosinophilic inflammation as a chemotaxin as well as an activator of proinflammatory effector functions.
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PMID:Recombinant human eotaxin induces oxygen radical production, Ca(2+)-mobilization, actin reorganization, and CD11b upregulation in human eosinophils via a pertussis toxin-sensitive heterotrimeric guanine nucleotide-binding protein. 887 20

The effects of the N-formyl methionyl peptide, formyl-methionyl-leucyl phenylalanine (fMLF) on the lateral mobility of the complement receptor type 1 (CR1/CD35) in glass-adherent human neutrophils were investigated, using fluorescence recovery after photobleaching (FRAP) and confocal microscopy (CSLM). It was found that addition of 0.1-1 microM fMLF increased the diffusion constant (D) of CR1/CD35 to 167-228% of controls. No effect was observed on the receptor distribution or the mobile fraction of receptors. The effect of fMLF on the lateral diffusion of CR1/CD35 could be totally inhibited by addition of pertussis toxon (PD, 250 ng/ml) or of the free radical scavenger enzymes superoxide dismutase (SOD, 2000 U/ml) and catalase (CAT, 200 U/ml), added together the results show that oxidative metabolites produced by neutrophils in response to fMLF can modulate CR1/CD35 diffusion, and indicate a regulatory role for oxygen radicals in phagocytosis.
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PMID:The N-formyl methionyl peptide, formyl-methionyl-leucyl phenylalanine (fMLF) increases the lateral diffusion of complement receptor 1 (CR1/CD35) in human neutrophils; a causative role for oxidative metabolites? 891 29

The arachidonic acid metabolites 5-oxo-[6E,8Z,11Z,14Z]-eicosatetraen oic acid (5oETE) and 5-oxo-15-hydroxy-[6E,8Z,11Z,13E]-eicosatetrae noi c acid (5oHETE) are potent eosinophil chemotaxins. Here, the activation profile of 5-oxo-eicosanoids in eosinophils was further characterized and compared to other eosinophil activators such as complement fragment C5a (C5a), platelet-activating factor (PAF), interleukin-5 (IL-5), and phorbol ester (PMA). Flow cytometric studies revealed a rapid and transient actin polymerization upon stimulation by both 5-oxo-eicosanoids. Desensitization studies using actin polymerization as the parameter indicated cross-desensitization between the two 5-oxo-eicosanoids but revealed no interference with the response to other chemotaxins. Fluorescence measurements with Fura-2-labeled eosinophils in the presence of EGTA indicated Ca2+-mobilization from intracellular stores by 5oETE and 5oHETE. Both 5-oxo-eicosanoids stimulated the production of reactive oxygen metabolites as demonstrated by lucigenin-dependent chemiluminescence, superoxide dismutase-inhibitable cytochrome C reduction, and flow cytometric dihydrorhodamine-123 analysis. At optimal concentrations the changes induced by 5-oxo-eicosanoids were comparable to those obtained by C5a and PAF, whereas IL-5 and PMA induced only a restricted pattern of cell responses. Cell responses elicited by 5-oxo-eicosanoids were inhibited by pertussis toxin, indicating coupling of the putative 5-oxo-eicosanoid-receptor to G-proteins. These results indicate that 5-oxo-eicosanoids are stong activators of eosinophils with comparable biologic activity to the eosinophil chemotaxins C5a and PAF. These findings point to a role of 5-oxo-eicosanoids in the pathogenesis of eosinophilic inflammation as chemotaxins as well as activators of pro-inflammatory activities.
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PMID:Chemotactic 5-oxo-eicosatetraenoic acids induce oxygen radical production, Ca2+-mobilization, and actin reorganization in human eosinophils via a pertussis toxin-sensitive G-protein. 898 Feb 98

The Fur titration assay (FURTA) recently developed by I. Stojiljkovic and coworkers (J. Mol. Biol. 236:531-545, 1994) was applied to clone iron-regulated genes of Bordetella pertussis. After sequence analysis, one of the clones obtained by this selection procedure was shown to contain an open reading frame with significant sequence similarities to Mn-containing superoxide dismutases (SodA). The open reading frame was preceded by a Fur consensus binding site, which according to primer extension analysis overlaps the -10 region of the sodA promoter. Southern blot analysis also revealed the presence of sodA homologous sequences in Bordetella bronchiseptica. On the transcriptional level, sodA expression is strictly iron regulated in both organisms and also in the heterologous host Escherichia coli harboring a plasmid with the sodA gene. Accordingly, SodA-mediated superoxide dismutase activity in Bordetella lysates was detected only after cultivation of the bacteria in iron-restricted media. A B. bronchiseptica fur mutant constitutively expressed SodA, thereby confirming the functional similarity of the iron regulatory systems in the two genera. Apart from iron regulation, sodA expression was affected by changes in DNA topology induced by coumermycin A but not by the global virulence regulatory Bvg system. B. pertussis and B. bronchiseptica sodA deletion mutants did not show significant changes in their growth properties. In contrast, mutation of the previously described Fe-containing SodB enzyme resulted in clones strongly impaired in viability. No direct involvement of SodA in bacterial virulence could be revealed because deletion of the sodA gene affected survival of Bordetella species neither in cultured macrophages nor in a mouse respiratory infection model.
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PMID:Cloning and characterization of an Mn-containing superoxide dismutase (SodA) of Bordetella pertussis. 907 4

In order to examine the mechanisms of ischemia-reperfusion induced changes in beta-adrenoceptor-linked signal transduction pathway, isolated rat hearts perfused in the absence or presence of superoxide dismutase (SOD) plus catalase (CAT) were made ischemic for 30 min and then reperfused for 60 min. The left ventricular developed pressure as well as the rare of contraction and rate of relaxation were markedly decreased, whereas the left ventricular end-diastolic pressure increased in the ischemic hearts. A significant increase in the density and affinity of beta 1-adrenoceptors without any changes in the characteristics of beta 2-adrenoceptors was evident in cardiac membranes obtained from the ischemic hearts. The recovery of contractile abnormalities in the ischemic heart was depressed upon reperfusion; the ischemic-reperfused hearts also showed attenuated inotropic responses to isoproterenol. The affinities and densities of beta- and beta-adrenoceptors were decreased in the ischemic-reperfused hearts; the magnitude of changes in beta 1-adrenoceptors was greater than that in beta 2-adrenoceptors. The isoproterenol-stimulated adenylyl cyclase activity was depressed in both ischemic hearts and ischemic-reperfused hearts. The basal and forskolin-stimulated adenylyl cyclase activities were unaltered due to ischemia but were increased upon reperfusion. The NaF- and 5'-Guanylyl-imidodiphosphate[Gpp(NH)p]-stimulated adenylyl cyclase activities were depressed in the ischemic hearts and increased in the ischemic reperfused hearts. Cholera toxin (CT)-stimulated adenylyl cyclase as well as the CT-catalysed ADP-ribosylation activity and stimulatory G protein (Gs protein) immunoreactivity were decreased in the ischemic hearts and increased in the reperfused hearts. Pertussis toxin (PT)-stimulated adenylyl cyclase activity was unaltered in both ischemic and ischemic-reperfused hearts, whereas the PT-catalysed ribosylation and inhibitory G protein (Gi protein) immunoactivity were slightly increased in the reperfused myocardium. Thus the inability of isoproterenol to stimulate adenylyl cyclase in the ischemic-reperfused hearts may be due to alterations mainly in the characteristics of beta 1-adrenoceptors including density, affinity and coupling with the adenylyl cyclase. Scavenging of oxyradicals by the addition of SOD plus CAT in the perfusion medium prevented the reperfusion-induced changes in contractile function, inotropic responses of the heart to isoproterenol, activation of adenylyl cyclase by isoproterenol, as well as densities and affinities of beta-adrenoceptors in cardiac membranes. These results suggest that the depressed contractile activity and the attenuated inotropic responses of ischemic-reperfused hearts to isoproterenol as well as the defects in beta-adrenoceptor-linked signal transduction may be due to the formation of oxyradicals in the myocardium.
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PMID:Beta-adrenoceptor-linked signal transduction in ischemic-reperfused heart and scavenging of oxyradicals. 914 Aug 14

To assess the effects of oxyradicals on cardiac beta-adrenoceptors, G-proteins and adenylyl cyclase, rat heart membranes were incubated with xanthine (X) plus xanthine oxidase (XO) for different intervals. The basal as well as forskolin-, NaF-, 5'-guanylylimidodiphosphate and isoproterenol-stimulated adenylyl cyclase activities showed an increase at 10 min and a decrease at 30 min of incubation with X plus XO. Treatment of membranes with H2O2 also produced biphasic changes in adenylyl cyclase activities. The density of beta1-adrenoceptors was decreased when cardiac membranes were treated with X plus XO for 10 and 30 min whereas the affinity of beta1-adrenoceptors was increased after 10 min and reduced after 30 min of incubation. The beta2-adrenoceptors were not modified at 10 min whereas incubation of cardiac membranes with X plus XO for 30 min increased the affinity and decreased the density. Cholera toxin-stimulated adenylyl cyclase activity, cholera toxin-catalyzed ADP-ribosylation and stimulatory guanine nucleotide binding protein immunoreactivity in cardiac membranes were increased at 10 min and decreased at 30 min of incubation with X plus XO. However, the pertussis toxin-stimulated adenylyl cyclase activity, pertussis toxin-catalyzed ADP ribosylation and inhibitory guanine nucleotide binding protein immunoreactivity were not affected on treatment of membranes with X plus XO. Addition of superoxide dismutase plus catalase in the incubation medium prevented the X plus XO-induced alterations in adenylyl cyclase activities, stimulatory guanine nucleotide binding protein-related ADP-ribosylation and changes in the characteristics of beta-adrenoceptors except the increased affinity of beta1-adrenoceptors at 10 min of incubation. These data suggest that alterations in the beta1-adrenoceptor-linked stimulatory guanine nucleotide binding protein-adenylyl cyclase pathway due to X plus XO are biphasic in nature and these changes may likely be due to the formation of H2O2.
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PMID:Biphasic alterations in cardiac beta-adrenoceptor signal transduction mechanism due to oxyradicals. 931 80

The novel human CC-chemokine monocyte chemotactic protein-4 (MCP-4) is a chemotaxin for eosinophils. Here, the biological activities and the activation profile of MCP-4 was further characterized in eosinophils and compared to other activators such as platelet activating factor (PAF), Eotaxin and RANTES. As demonstrated by lucigenin-dependent chemiluminescence and superoxide dismutase-inhibitable cytochrome C reduction MCP-4 stimulated the production of reactive oxygen metabolites. Furthermore, MCP-4 induced up-regulation of the integrin CD11b. Flow cytometric studies revealed rapid and transient actin polymerization upon stimulation with MCP-4. At optimal concentrations the changes induced by MCP-4 were weaker than the effects after stimulation with PAF and comparable to those obtained by RANTES and Eotaxin. Cell responses elicited by MCP-4 were inhibited by pertussis toxin indicating involvement of Gi-proteins in this signal pathway. These findings point to a role of MCP-4 in the pathogenesis of eosinophilic inflammation as chemotaxin as well as activator of pro-inflammatory effector functions.
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PMID:The monocyte chemotactic protein-4 induces oxygen radical production, actin reorganization, and CD11b up-regulation via a pertussis toxin-sensitive G-protein in human eosinophils. 936 76


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