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)

We have developed a model of prolonged immunological inflammation in the rat which has a structural resemblance to the synovial changes in rheumatoid arthritis. Pertussis vaccine was injected into 6-day-old subcutaneous air pouches in animals previously sensitized with pertussis vaccine. The resulting inflammatory response persisted up to 30 days. Examination of exudates showed a wave of polymorphonuclear leucocytes over a 13-day period followed by a mononuclear cell predominance up to 30 days. Histologically, an early polymorphonuclear cell infiltration was followed by the formation of a lining layer of large eosinophilic mononuclear cells, together with deep collections of lymphocytes and plasma cells. Concentrations of the acute-phase reactant alpha 1-glycoprotein, in both serum and exudate, peaked at 3 days. This suggests that the local production of interleukin I in this type of tissue reaction is more closely related to the acute inflammatory phase than to more chronic interactions between monocyte derived cells and lymphocytes.
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PMID:The immune response to pertussis in the 6-day air pouch: a model of chronic synovitis. 402 78

Fertilization is initiated by the species-specific binding of sperm to the extracellular coat of the egg. One sperm receptor for the mouse egg is beta-1,4-galactosyltransferase (GalTase), which binds O-linked oligosaccharides on the egg coat glycoprotein ZP3. ZP3 binding induces acrosomal exocytosis through the activation of a pertussis toxin-sensitive heterotrimeric guanine nucleotide-binding protein (G protein). The cytoplasmic domain of sperm surface GalTase bound to and activated a heterotrimeric G protein complex that contained the Gi alpha subunit. Aggregation of GalTase by multivalent ligands elicited G protein activation. Sperm from transgenic mice that overexpressed GalTase had higher rates of G protein activation than did wild-type sperm, which rendered transgenic sperm hypersensitive to their ZP3 ligand. Thus, the cytoplasmic domain of cell surface GalTase appears to enable it to function as a signal-transducing receptor for extracellular oligosaccharide ligands.
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PMID:Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm. 756 99

Overlapping 10-amino-acid peptides, which consecutively span the amino acid sequence of the S3 subunit of pertussis toxin, were synthesised on polyethylene pins and screened for their ability to bind the glycoprotein fetuin. Fetuin binding was localised to a single peptide comprising amino acids 46-55. A free peptide, (E)S3c, of longer sequence (S3 amino acids 44-58) was also found to bind alpha-1-acid glycoprotein, mixed brain gangliosides and fetuin. (E)S3c also recognised asialofetuin but with a lower apparent affinity relative to fetuin. The single tryptophan residue of the peptide yielded a fluorescence-emission maximum of 355 nm. In the presence of either ganglioside or the phospholipid L-alpha-lysolecithin, but not N-acetylneuramin-lactose or lactosylceramide, the emission intensity of (E)S3c was enhanced and the emission maximum blue-shifted to 340 nm by ganglioside, or to 345 nm by L-alpha-lysolecithin. Monosialogangliosides, disialogangliosides, and trisialogangliosides, when fluorescence-titrated, were each found to bind the peptide with a similar dissociation constant of 4.4 +/- 2.8 microM. These findings demonstrate that region 44-58 of the pertussis-toxin S3 subunit is likely to be involved in the recognition of both glycosylated and phospholipid constituents of target-cell membranes.
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PMID:Localisation of a receptor-recognition domain on the S3 subunit of pertussis toxin by peptide mapping. 767 39

Pertussis toxin is one of several virulence factors produced by Bordetella pertussis, the etiologic agent of whooping cough. Pertussis toxin is an oligomeric A-B class toxin composed of an ADP-ribosyltransferase S1 (A) subunit and a B oligomer containing lectin-like binding domains. The carbohydrate binding specificity of the B oligomer is for sialooligosaccharide sequences expressed on target cell receptors and asparagine-linked glycans found in many serum glycoproteins. Pertussis toxin also has the ability to bind to the inert surfaces of culture tubes. In this report we present data showing that pertussis toxin binding to polypropylene microcentrifuge tubes was enhanced in a time- and concentration-dependent manner by the addition of soluble glycoprotein or oligosaccharide receptor analogs. Evidence obtained using the hydrophilic and hydrophobic surfaces of Gel Bond electrophoresis casting film indicated that receptor-enhanced binding was likely due to hydrophobic interactions. Hydrophobic binding of the isolated B oligomer of pertussis toxin was enhanced only in the presence of high concentrations of glycoproteins. Therefore, the S1 (A) subunit of pertussis holotoxin appears to play a role in receptor-enhanced hydrophobic binding. We propose, therefore, that pertussis toxin binding to its receptors may expose or preferentially orient hydrophobic residues that may contribute to the functional association of the toxin with host cell plasma membranes and delivery of the S1 subunit to its intracellular target.
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PMID:Hydrophobic binding of pertussis toxin is enhanced by oligosaccharide receptors. 768 2

Thrombin binds at least to two sites of the platelet surface; to the recently cloned thrombin receptor [Vu, T. K., Hung, D. T., Wheaton, V. I. & Coughlin, S. R. (1991) Cell 64, 1057-1068] and to glycoprotein Ib. In the present study, the decrease of pertussis-toxin-dependent ADP-ribosylation of membrane and soluble inhibitory guanine-nucleotide-binding alpha (Gi alpha) proteins was measured after platelet stimulation with a thrombin-receptor-activating peptide (TRAP), and compared to stimulation with thrombin. Stimulation of intact platelets with TRAP decreased the pertussis-toxin-dependent ADP-ribosylation of the major membrane 41-kDa Gi alpha protein and the minor soluble 40 kDa Gi alpha protein recently described in platelets [Gennity, J. M. & Siess, W. (1991) Biochem. J. 279, 643-650]. The kinetics and extent of the decrease of pertussis-toxin-dependent ADP-ribosylation after stimulation of TRAP were similar to the effect of thrombin. The decrease of pertussis-toxin-dependent ADP-ribosylation of the soluble Gi alpha protein was more pronounced and observed at lower agonist concentrations than the decrease of the membrane Gi alpha protein. Desensitization of the thrombin receptor by incubating platelets with a low concentration of TRAP reduced the subsequent decrease of pertussis-toxin-dependent ADP-ribosylation of Gi alpha proteins, evoked by TRAP or thrombin. Platelet stimulation with gamma-thrombin that does not bind to glycoprotein Ib also showed a decrease in the pertussis-toxin-dependent ADP-ribosylation of the soluble and membrane Gi alpha proteins. Treatment of platelets with the stable prostacyclin analog, iloprost, reduced the decrease of pertussis-toxin-dependent ADP-ribosylation of Gi alpha proteins induced by TRAP or thrombin. Among other platelet stimuli tested (endoperoxide/thromboxane analog U44619, collagen, ADP, vasopressin), only U44619 decreased the pertussis-toxin-dependent ADP-ribosylation of the soluble and membrane Gi alpha proteins to a degree comparable to TRAP. It is concluded that the thrombin-induced activation of both the membrane and soluble Gi alpha proteins in platelets occurs via stimulation of the recently cloned thrombin receptor and is independent of the binding of thrombin to glycoprotein Ib. Furthermore, the coupling thrombin receptor/Gi protein is reduced by intracellular cAMP.
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PMID:Activation of the cloned platelet thrombin receptor decreases the pertussis-toxin-dependent ADP-ribosylation of the membrane and soluble inhibitory guanine-nucleotide-binding-alpha proteins. Inhibition by the prostacyclin analog, iloprost. 768 67

Glycoproteins that inhibit neurite outgrowth may guide growth cones during development by acting as a barrier and closing off inappropriate routes. Their continued expression in the adult central nervous system may be a key factor in preventing regeneration of central nervous system neurons. A glycoprotein of 55 kDa has been isolated from the detergent-insoluble membrane skeleton from adult chicken brain. Initial experiments showed that dorsal root ganglion neurons would not adhere to or extend neurites on a substratum coated with GP55. Furthermore, GP55 will act as a barrier to the advance of established growth cones in the presence of poly-L-lysine, laminin or G4. Central nervous system neurons from forebrain as well as dorsal root ganglion neurons from the peripheral nervous system are inhibited by GP55. GP55 is also effective in blocking the initial adhesion of neurons to a substratum of poly-L-lysine and, particularly, laminin. In contrast to the inhibition of neurite outgrowth, neuronal adhesion is concentration independent over the range tested. A preliminary investigation of the mechanism by which GP55 inhibits outgrowth suggests that a pertussis toxin-sensitive G protein is required. Preliminary evidence suggests that GP55 is anchored in the membrane by a glycosyl phosphatidylinositol moiety. GP55 is distinct from previously identified inhibitory proteins, based on the source and molecular mass, and is thus a new member of this rapidly expanding family.
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PMID:Identification of a novel protein from adult chicken brain that inhibits neurite outgrowth. 770 93

Platelets present a unique model to study the B-oligomer effects of pertussis toxin because they become activated in response to the B oligomer but are not susceptible to ADP-ribosylation by the holotoxin. In these studies, the B oligomer of pertussis toxin caused concentration-dependent platelet activation, as determined by increases in intracellular calcium concentration, dense granule secretion, and platelet aggregation. Stirring was required for pertussis toxin to increase intracellular calcium. A monoclonal antibody against platelet glycoprotein Ib abolished increases in intracellular calcium concentration and increased the latency and reduced the slope of the aggregation response elicited by the B oligomer. Pertussis toxin also evoked [14C]serotonin release from platelets, and this effect was inhibited, though not eliminated, by an antibody against platelet glycoprotein Ib. Binding of pertussis toxin to glycoprotein Ib was observed after nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These data suggest that the B oligomer of pertussis toxin induces platelet activation mediated, at least in part, by an interaction with platelet glycoprotein Ib.
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PMID:Pertussis toxin activates platelets through an interaction with platelet glycoprotein Ib. 803 78

High affinity binding sites for pancreastatin were identified for the first time, and their molecular characterization was performed with rat liver membranes. Using rat 125I-pancreastatin, we have studied the interaction of pancreastatin with liver membranes. Cross-linking of the tracer to the membranes was performed using the bifunctional reagent dithiobis(succinimidyl propionate). Analysis of binding under equilibrium conditions indicated the existence of one class of binding sites, with a Bmax of 15 fmol/mg of protein and an apparent Kd of 0.2 nM. The cross-linking of 125I-pancreastatin to liver membranes revealed a single band of M(r) 40,000, corresponding to the 125I-pancreastatin-receptor complex. The labeling of this complex was inhibited in the presence of rat pancreastatin (10(-10) to 10(-7) M) and in the presence of guanyl-5'-ylimidodiphosphate (10(-7) to 10(-4) M). Pretreatment of rat liver membranes with pertussis toxin did not affect pancreastatin binding or the inhibition by guanyl-5'-ylimidodiphosphate of pancreastatin binding. The specificity of pancreastatin binding was further assessed by displacement experiments with pancreastatin from other species and vasopressin. The binding of the pancreastatin-receptor complexes to Sepharose coupled to different lectins showed the glycoprotein nature of the pancreastatin receptor. These results strongly suggest that rat liver possesses a specific pancreastatin receptor, a glycoprotein of M(r) 35,000 that is coupled to a pertussis toxin-insensitive G protein in the plasma membrane.
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PMID:Receptors for pancreastatin in rat liver membranes: molecular identification and characterization by covalent cross-linking. 805 54

Active cellular motility is required for tumor cell penetration of the basement membrane and the interstitial stroma during the transition from in situ to invasive carcinoma. Multiple factors, both autocrine and paracrine in origin, appear to influence this motile response. Recently, a potent new cytokine with molecular mass 120 kDa has been purified to homogeneity from a human melanoma cell line (A2058). This new protein, termed autotaxin (ATX), is a basic glycoprotein with pI approximately 7.7. ATX is active in the picomolar range, stimulating pertussis toxin sensitive chemotactic and chemokinetic responses by the same cell line that produces it. Sequence information, obtained on 11 purified tryptic peptides (114 residues), confirmed that the protein is unique with no significant homology to growth factors or previously described motility factors. It is hypothesized that an autocrine motility factor, such as ATX, could play a role in the initiation of the metastatic cascade by stimulating tumor cells to move away from the primary tumor. Other motility stimulating factors, such as components of the extracellular matrix or growth factors, could then influence both the time course and the localization of tumor cell spread.
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PMID:The role of autotaxin and other motility stimulating factors in the regulation of tumor cell motility. 816 65

Down syndrome (DS) was studied in terms of immunological function and serological aspects. It was found that antibody levels against rubella and pertussis in the sera from 36 institutionalized DS patients were comparable with those of healthy controls while low antibody levels were detected against mumps and measles. Six tumor markers were also assayed in the serum from DS patients and the serum concentration of alpha-1-acid glycoprotein (alpha 1-AGP) and immunosuppressive acidic protein, an analogous glycoprotein of alpha 1-AGP, were significantly higher than those of the control group. Multivariate discriminant function was constructed based on the concentration of tumor markers. The function could discriminate between the two groups at a sensitivity of 92.3%. Flow-cytometrical analysis has revealed that helper T level of DS patients' sera was lower than that of the control group.
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PMID:A seroimmunological analysis of Down syndrome. 836 67


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