Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0043167 (pertussis)
 19,595 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The respiratory electron transport chain of Bordetella pertussis was examined in whole cell suspensions using difference spectra obtained at room temperature. Phase I (virulent) strains were found to possess cytochromes a-603, b-560, c-550, d-629 and cytochrome o. Cytochrome c-553, previously reported (Sutherland, 1963) was not detected and was assumed to be masked by the alpha-peaks for c-550 and b-560. Phase IV (avirulent) strains and C-mode cells (phase I strains grown in the presence of 20 mM MgSO4) were deficient in cytochrome d-629 and appeared to have higher levels of cytochromes a-603, b-560, c-550 and cytochrome o. Preliminary data indicate that B. parapertussis and B. bronchiseptica have electron transport chains similar to that of B. pertussis.
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PMID:Phase-shift markers in the genus Bordetella: loss of cytochrome d-629 in phase IV variants. 628 28

The effect of prostaglandin F2 alpha (PGF2 alpha) on superoxide radical production by macrophages was studied in pseudopregnant rats. Peritoneal macrophages prepared on day 7 or 13 of pseudopregnancy (psp) were incubated with various doses of PGF2 alpha for 90 min, and the production of superoxide radical was measured by the cytochrome C reduction method. PGF2 alpha significantly stimulated superoxide radical production by macrophages on day 13 of psp, but not on day 7 of psp. The pretreatment of macrophages with an inhibitor of protein kinase C (H7), Ca2+ channel blocker (Verapamil), Ca2+ chelators (EGTA, BAPTA), and an inhibitor of GTP-binding protein (pertussis toxin) prevented the stimulatory effects of PGF2 alpha on superoxide radical production. In conclusion, PGF2 alpha stimulated superoxide radical production by macrophages through the intracellular signal transduction pathway including activation of protein kinase C through the GTP-binding protein and Ca2+ influx, which would play important roles in the luteolytic process in psp rats.
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PMID:[Involvement of stimulatory effect of prostaglandin F2 alpha on superoxide radical production by macrophages in corpus luteum regression]. 875 99

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 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 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

Unlike other cytochromes, c-type cytochromes have two covalent bonds formed between the two vinyl groups of haem and two cysteines of the protein. This haem ligation requires specific assembly proteins in prokaryotes or eukaryotic mitochondria and chloroplasts. Here, it is shown that Bordetella pertussis is an excellent bacterial model for the widespread system II cytochrome c synthesis pathway. Mutations in four different genes (ccsA, ccsB, ccsX and dipZ) result in B. pertussis strains unable to synthesize any of at least seven c-type cytochromes. Using a cytochrome c4:alkaline phosphatase fusion protein as a bifunctional reporter, it was demonstrated that the B. pertussis wild-type and mutant strains secrete an active alkaline phosphatase fusion protein. However, unlike the wild type, all four mutants are unable to attach haem covalently, resulting in a degraded N-terminal apocytochrome c4 component. Thus, apocytochrome c secretion is normal in each of the four mutants, but all are defective in a periplasmic assembly step (or export of haem). CcsX is related to thioredoxins, which possess a conserved CysXxxXxxCys motif. Using phoA gene fusions as reporters, CcsX was proven to be a periplasmic thioredoxin-like protein. Both the B. pertussis dipZ (i. e. dsbD) and ccsX mutants are corrected for their assembly defects by the thiol-reducing compounds, dithiothreitol and 2-mercaptoethanesulphonic acid. These results indicate that DipZ and CcsX are required for the periplasmic reduction of the cysteines of apocytochromes c before ligation. In contrast, the ccsA and ccsB mutants are not corrected by exogenous reducing agents, suggesting that CcsA and CcsB are required for the haem ligation step itself in the periplasm (or export of haem to the periplasm). Related to this suggestion, the topology of CcsB was determined experimentally, demonstrating that CcsB has four transmembrane domains and a large 435-amino-acid periplasmic region.
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PMID:Four genes are required for the system II cytochrome c biogenesis pathway in Bordetella pertussis, a unique bacterial model. 1106 71

Genetic analysis has indicated that the system II pathway for c-type cytochrome biogenesis in Bordetella pertussis requires at least four biogenesis proteins (CcsB, CcsA, DsbD and CcsX). In this study, the eight genes (ccmA-H) associated with the system I pathway in Escherichia coli were deleted. Using B. pertussis cytochrome c4 as a reporter for cytochromes c assembly, it is demonstrated that a single fused ccsBA polypeptide can replace the function of the eight system I genes in E. coli. Thus, the CcsB and CcsA membrane complex of system II is likely to possess the haem delivery and periplasmic cytochrome c-haem ligation functions. Using recombinant system II and system I, both under control of IPTG, we have begun to study the capabilities and characteristics of each system in the same organism (E. coli). The ferrochelatase inhibitor N-methylprotoporphyrin was used to modulate haem levels in vivo and it is shown that system I can use endogenous haem at much lower levels than system II. Additionally, while system I encodes a covalently bound haem chaperone (holo-CcmE), no covalent intermediate has been found in system II. It is shown that this allows system I to use holo-CcmE as a haem reservoir, a capability system II does not possess.
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PMID:Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli. 1662 58