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)

Blood and saliva were collected in the autumn and spring from a group of schoolchildren (39 girls, 35 boys) with a mean age of 11.4 years. Serum immunoglobulin IgG, IgA, IgM and IgE, alpha 1-antitrypsin (A 1-AT), alpha 2 macroglobulin (A 2M), transferrin (TRF), ceruloplasmin (CPL), lysozyme (LYS) and pertussis (PE) antibody levels were determined. Calcium (Ca2+) and total serum protein levels were also determined. Secretory IgA (sIgA) and secretory lysozyme (sLYS) levels were assessed in the saliva. A highly significant drop in Ca2+ levels was found in the spring in boys, while in girls there was only a greater scatter of the values. Mean IgG, IgA and IgM values fell significantly in the spring in both sexes, but IgE levels fell significantly only in boys. PE levels rose significantly in the spring in girls. Among the other proteins, all the values rose in boys, except for TRF, whose levels fell. In girls, LYS and TRF levels rose, but all the other values fell. The coefficients of correlation between Ca2+ and the tested proteins showed a significant relationship only for A 2M and PE in girls and only for the total protein level in boys; in boys, the determination coefficient for sIgA and IgM was over 10%. The results do not testify to the existence of a close relationship between blood Ca2+ levels and Ig and other blood protein levels.
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PMID:Seasonal changes in the relationship of blood calcium levels to immunoglobulins and some of the blood proteins in schoolchildren. 650 75

Experiments on CBA mice were performed to explore the changes in the body immunoreactivity induced by low intensity ultrasound. A study was made of the content of lysozyme, properdine, T and B rosette-forming lymphocytes, and complement in the peripheral blood, the histophysiological properties of the lymphoid organs, and the titer of pertussis antibodies. It has been disclosed that ultrasound has a stimulant effect, primarily on the T system immunity, which was confirmed during immunization with B. pertussis vaccine. The stimulant effect has been also supported by histostructural analysis of the lymphoid organs.
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PMID:[Effect of ultrasound on cellular and humoral immunity factors]. 685 94

In previous studies, we used a photoactivable, radioiodinated lipopolysaccharide (LPS) derivative to define and characterize a specific bacterial endotoxic LPS-binding protein (p73) on mammalian lymphoreticular cells, including B and T lymphocytes and macrophages. More recently, using the same methodology, we characterized a specific interaction of LPS with the S2 subunit of Bordetella pertussis pertussis toxin (PT) in the fluid phase (M.-G. Lei and D. C. Morrison, J. Biol. Chem., 268:1488-1493, 1993). Furthermore, we showed that lysozyme (LZM) but not polymyxin B can compete with PT for binding to LPS in the fluid phase, a result suggesting that these two molecules compete for the same binding site on LPS. In this report, we demonstrate that the binding of PT to murine splenocytes (cell-bound PT) reduces the ability of the LPS photo-cross-linking probe to bind to the p73 receptor. The reduction can also be demonstrated with the PT B oligomer, a result indicating that the observed reduction of LPS binding to the p73 receptor by PT is A-protomer (S1-subunit) independent. More importantly, our studies document that cell-bound PT can be radiolabelled by the LPS probe, coincident with the observed reduction in p73 photoaffinity labelling. The preferential interaction of LPS with the PT S2 subunit in the fluid phase was, however, not observed with cell-bound PT. The reduction in radiolabelling of the p73 receptor by the LPS probe and in radiolabelling of cell-bound PT was shown to be concentration dependent. The data presented here document, however, that LZM does not reduce the ability of the LPS probe to bind to the p73 receptor on mouse splenocytes, nor does the presence of LZM bound to LPS influence the observed reduction in photoaffinity labelling of p73 by the LPS probe or radiolabelling of cell-bound PT by the LPS probe. Collectively, these results support the concept that the ability of LPS to interact with PT in the fluid phase is not responsible for the ability of cell-bound PT to influence the binding of the LPS probe to the p73 receptor. Thus, it is suggested that PT and LPS bind to different sites on the p73 molecule and that this same p73 protein may recognize both LPS and PT.
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PMID:Evidence that lipopolysaccharide and pertussis toxin bind to different domains on the same p73 receptor on murine splenocytes. 768 Oct 44

Previous in vivo and in vitro studies demonstrated that the murine beta-chemokine TCA3 is a chemoattractant for monocytes/macrophages and neutrophils. The ability of TCA3 to activate these cell populations is now evaluated. Treatment with 10 to 20 nM rTCA3 induced a respiratory burst with the production of superoxide and hydrogen peroxide in both casein-elicited and unstimulated neutrophil and macrophage populations. In addition, TCA3 treatment induced the production of reactive nitrogen intermediates, whereas stimulation with higher concentrations (100 nM) of TCA3 induced the exocytosis of lysozyme and elastase in the presence of cytochalasin B (7 micrograms/ml). Subnanomolar concentrations (100 pM) of TCA3 also caused integrin-mediated increases of adhesiveness to fibrinogen by neutrophils and macrophages. Increased adhesiveness is the most sensitive assay for TCA3 bioactivity. TCA3 treatment appears to involve signaling through a G-protein-linked receptor as Pertussis toxin abolished the TCA3-mediated increase of adhesiveness and the production of reactive nitrogen intermediates. The dose dependence of the TCA3-mediated activities indicate a coordinated inflammatory response mediated by varying concentrations of TCA3.
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PMID:Biologic activities of the beta-chemokine TCA3 on neutrophils and macrophages. 773 Jun 38

Calcium, strontium and barium induced an exocytotic response in electropermeabilized rabbit neutrophils while magnesium was without any effect. The extent of enzyme release was found to depend upon the concentration of these cations. For all cations, an optimum concentration was found with the same maximum enzyme release. At concentrations higher than optimum a decrease in lysozyme release was observed. Efficiency to induce enzyme release was in the order: Ca2+ > Sr2+ > Ba2+. Enzyme release was significantly enhanced by guanosine-5'-[gamma-thio]triphosphate (GTP gamma S) resulting in a shift to the left of the dose/response curve. The enhancement by GTP gamma S was strongest with Ca2+, was less with Sr2+, and was very little with Ba2+. The time course of lysozyme release was the same for Ca2+, Sr2+, and Ba2+ in the presence and absence of GTP gamma S when suboptimal cation concentrations were used. A decrease in responsiveness to the effectors after electropermeabilization was observed with Ca2+, Sr2+ and Ba2+ in the presence and absence of GTP gamma S. The lysozyme release induced by the different cations was not inhibited by the protein kinase C inhibitor staurosporine and was slightly affected by pertussis toxin. Ca2+ and Sr2+, but not Ba2+, potentiated formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) induced enzyme release in intact neutrophils. The divalent cation ionophore A23187 induced enzyme release in the presence of Ca2+ and Sr2+ but not in the presence of Ba2+. The results obtained with electropermeabilized neutrophils indicate that Sr2+ and Ba2+ can act as substitutes for Ca2+ in activating exocytosis, and that permeabilized neutrophils provide the best tool to investigate the effects of alkaline earth ions in exocytosis.
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PMID:Strontium and barium induce exocytosis in electropermeabilized neutrophils. 841 94

Using radioiodinated, photoactivable, reducible cross-linker conjugated bacterial endotoxic lipopolysaccharide (125I-ASD-LPS), we have demonstrated that LPS selectively binds to the S2 subunit of pertussis toxin (PT). Since LPS also interacts with the S2 subunit of the B-oligomer of the toxin, the binding of LPS to PT is not A-protomer (S1 subunit) dependent. The binding can be inhibited with native underivatized LPS and with purified lipid A, suggesting that the binding is mediated through the lipid A moiety of the LPS molecule. The binding of PT to LPS can be inhibited by bovine fetuin glycoprotein. Since PT has been demonstrated to interact specifically with N-linked oligosaccharide side chains of fetuin, the interaction of LPS with the S2 subunit of PT may involve carbohydrate-dependent interactions of the disaccharide backbone of lipid A with S2. Additional studies have documented that LPS binding to PT may be competitively inhibited by lysozyme but not by polymyxin B. Sequence analysis has allowed identification of a high degree of amino acid sequence similarity between the S2 subunit of PT and hen egg white lysozyme at the N-terminal 80-residue regions. Shared N-terminal sequence similarity between lysozyme, PT-S2, and a third LPS-binding protein alpha-lactalbumin allows tentative identification of a second family of LPS binding proteins.
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PMID:Lipopolysaccharide interaction with S2 subunit of pertussis toxin. 841 48

The Ca2+-ATPase inhibitor thapsigargin (TG) activates bivalent-cation early in human neutrophils via depletion of intracellular Ca2+ stores bu little is known about the underlying mechanism and the functional role of TG-induced cation entry. We studied the effects of TG on univalent- and bivalent cation entry, lysozyme release and superoxide-anion (O2-) formation in human neutrophils. TG, like the chemotactic peptide, N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLP), stimulated entry of Ca2+, Mn2+, Ba2+, Sr2+ and Na+ in a 1-{beta-[3-(4-methoxyphenyl)propoxy]-4-methoxyphenethyl}-1H-imidazole hydrochloride (SK&F 96365)- and Gd3+-sensitive manner. The inhibitors of protein phosphates 1/2A, calyculin A and okadaic acid, diminished TG-induced cation influxes, whereas the inhibitors of protein phosphatase 2B, cyclosporin A and FK-506, were potentiators. Pertussis toxin (PTX) partially inhibited the effects of TG on Ca2+ and Mn2+ entry. TG and fMLP activated inward currents with a linear current-voltage relationship and a reversal potential at about 0 mV. TG activated lysozyme release and potentiated fMLP-induced O2- formation. TG-induced lysozyme release was inhibited by SK&F 96365, PTX and the removal of extracellular Ca2+ or Na+. Our data show that TG activates a non-selective and SK&F 96365- and Gd3+-sensitive cation entry pathway and is a partial secretagogue. TG-stimulated cation entry involves PTX-sensitive G-proteins and protein phosphatases, with protein phosphatases 1/2A and 2B playing opposite roles.
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PMID:Thapsigargin activates univalent- and bivalent-cation entry in human neutrophils by a SK&F I3 96365- and Gd3+-sensitive pathway and is a partial secretagogue: involvement of pertussis-toxin-sensitive G-proteins and protein phosphatases 1/2A and 2B in the signal-transduction pathway. 867 85

Cell-free lung lavage fluid (LLF) from healthy normal rats killed phase I (wild-type, virulent) Bordetella pertussis at 37 degrees C in vitro. B. parapertussis was also killed by the LLF, but phase IV (avirulent mutant) B. pertussis and some other common bacterial species, including B. bronchiseptica, were not. Transmission electron microscopy of thin sections of the phase I B. pertussis showed extensive structural damage and cell lysis. None of the other mammalian species tested had LLF with bactericidal activity against B. pertussis as high as that of the rat. Rats killed with halothane yielded LLF with higher bactericidal activity than when CO2 was used. Ultracentrifugation of LLF at 55,000 g gave a surfactant (pellet) fraction that had c. 95% of the bactericidal activity and which was biochemically distinct from the 5% of activity in the supernate fraction. Phospholipids and fatty acids appeared to be involved in LLF bactericidal activity, but not complement or lysozyme. Arachidonic acid was the most active of the fatty acids tested. Artificial surfactant, as used in premature infants, had no bactericidal effect on B. pertussis.
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PMID:Bactericidal activity of rat lung lavage fluid against Bordetella pertussis. 1040 14

Pertussis toxin (PT) has been shown to act as an adjuvant that enhances the production of both Th1 and Th2 cytokines to coinjected protein antigens. It has remained unresolved, however, how PT affects the clonal sizes, long-term effector functions, and Th1/Th2/Th0 differentiation of the T cell responses induced. We have studied the effects of PT on the development of the CD4(+) T cell response to a prototypic antigen, hen eggwhite lysozyme (HEL). HEL injection with incomplete Freund's adjuvant (IFA) resulted in an IFN-gamma(-)/IL-5(+) Th2 recall response. In comparison, co-administration of PT with HEL:IFA enhanced the frequencies of IL-5-producing T cells up to eightfold, and induced the differentiation of high frequencies of IFN-gamma-producing CD4(+) T cells. The results showed that the IFN-gamma and IL-5 produced, originated from clonally expanded Th1 and Th2, but not Th0 cells, and that the effector functions of long-term memory cells were unaffected. Adoptive transfer experiments suggested that PT mediated these effects via activation of APC, not by acting on the T cells directly. The effects of PT on the developing T cell response required the presence of the holotoxin (A- and B-subunit); the individual subunits did not show adjuvant effects. The data suggest that PT enhanced cytokine production by promoting differentiation and vigorous clonal expansion of Th1 and Th2 cells via activation of APC.
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PMID:The enhanced antigen-specific production of cytokines induced by pertussis toxin is due to clonal expansion of T cells and not to altered effector functions of long-term memory cells. 1094 Sep 34

The family of peptidoglycan recognition proteins (PGRPs) is conserved from insects to mammals. Recently, Drosophila PGRP-SC1B was demonstrated to be an N-acetylmuramoyl-L-alanine amidase (NAMLAA), an enzyme that cleaves the lactylamide bond between muramic acid and the peptide chain in peptidoglycan (PGN). We now show an M x mPGRP-L mRNA to be expressed in the liver. The recombinant M x mPGRP-L protein has NAMLAA activity and degrades PGN from both Escherichia coli and Staphylococcus aureus; however, the Gram-positive PGN was a better substrate after lysozyme treatment. The activity of M x mPGRP-L was further analysed using Bordetella pertussis tracheal toxin as a substrate. Cleavage products were separated on HPLC and identified using mass spectrometry. From these results we conclude that M x mPGRP-L has activity and other properties identifying it as the NAMLAA protein present in mammalian sera.
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PMID:A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity. 1282 Nov 40


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