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Highly differentiated human airway epithelial cells: a model to study host cell-parasite interactions in pertussis.
Guevara C, Zhang C, Gaddy JA, Iqbal J, Guerra J, Greenberg DP, Decker MD, Carbonetti N, Starner TD, McCray PB, Mooi FR, Gómez-Duarte OG
(2016) Infect Dis (Lond) 48: 177-88
MeSH Terms: Animals, Antigens, Bacterial, Bacterial Adhesion, Bordetella pertussis, Bronchi, Epithelial Cells, Fimbriae Proteins, Host-Pathogen Interactions, Humans, Mice, Models, Biological, Primary Cell Culture, Respiratory Mucosa, Virulence Factors, Bordetella, Whooping Cough
Show Abstract · Added April 26, 2017
BACKGROUND - Bordetella pertussis colonizes the human respiratory mucosa. Most studies on B. pertussis adherence have relied on cultured mammalian cells that lack key features present in differentiated human airway cells or on animal models that are not natural hosts of B. pertussis. The objectives of this work were to evaluate B. pertussis infection in highly differentiated human airway cells in vitro and to show the role of B. pertussis fimbriae in cell adherence.
METHODS - Primary human airway epithelial (PHAE) cells from human bronchi and a human bronchial epithelial (HBE) cell line were grown in vitro under air-liquid interface conditions.
RESULTS - PHAE and HBE cells infected with B. pertussis wild-type strain revealed bacterial adherence to the apical surface of cells, bacteria-induced cytoskeleton changes, and cell detachment. Mutations in the major fimbrial subunits Fim2/3 or in the minor fimbrial adhesin subunit FimD affected B. pertussis adherence to predominantly HBE cells. This cell model recapitulates the morphologic features of the human airway infected by B. pertussis and confirms the role of fimbriae in B. pertussis adherence. Furthermore, HBE cells show that fimbrial subunits, and specifically FimD adhesin, are critical in B. pertussis adherence to airway cells.
CONCLUSIONS - The relevance of this model to study host-parasite interaction in pertussis lies in the striking physiologic and morphologic similarity between the PHAE and HBE cells and the human airway ciliated and goblet cells in vivo. These cells can proliferate in vitro, differentiate, and express the same genetic profile as human respiratory cells in vivo.
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15 MeSH Terms
Antibody-induced activation of beta1 integrin receptors stimulates cAMP-dependent migration of breast cells on laminin-5.
Plopper GE, Huff JL, Rust WL, Schwartz MA, Quaranta V
(2000) Mol Cell Biol Res Commun 4: 129-35
MeSH Terms: Adenosine Diphosphate Ribose, Antibodies, Monoclonal, Breast Neoplasms, Cell Adhesion, Cell Adhesion Molecules, Cell Movement, Cells, Cultured, Cyclic AMP, DNA Primers, Female, Heterotrimeric GTP-Binding Proteins, Humans, Integrin alpha3beta1, Integrins, Pertussis Toxin, Precipitin Tests, Receptors, Laminin, Signal Transduction, Tumor Cells, Cultured, Virulence Factors, Bordetella
Show Abstract · Added March 27, 2014
The beta1 integrin-stimulating antibody TS2/16 induces cAMP-dependent migration of MCF-10A breast cells on the extracellular matrix protein laminin-5. TS2/16 stimulates a rise in intracellular cAMP within 20 min after plating. Pertussis toxin, which inhibits both antibody-induced migration and cAMP accumulation, targets the Galphai3 subunit of heterotrimeric G proteins in these cells, suggesting that Galphai3 may link integrin activation and migration via a cAMP signaling pathway.
Copyright 2000 Academic Press.
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20 MeSH Terms
The CXC chemokine receptor 2, CXCR2, is the putative receptor for ELR+ CXC chemokine-induced angiogenic activity.
Addison CL, Daniel TO, Burdick MD, Liu H, Ehlert JE, Xue YY, Buechi L, Walz A, Richmond A, Strieter RM
(2000) J Immunol 165: 5269-77
MeSH Terms: Administration, Topical, Amino Acid Motifs, Amino Acid Sequence, Angiogenesis Inhibitors, Animals, Antibodies, Blocking, Cell Migration Inhibition, Cells, Cultured, Chemokines, CXC, Cornea, Endothelium, Vascular, Humans, Immune Sera, Mice, Mice, Inbred C57BL, Mice, Knockout, Microcirculation, Molecular Sequence Data, Neovascularization, Physiologic, Pertussis Toxin, Rats, Receptors, Interleukin-8B, Virulence Factors, Bordetella
Show Abstract · Added May 31, 2013
We have previously shown that members of the ELR(+) CXC chemokine family, including IL-8; growth-related oncogenes alpha, beta, and gamma; granulocyte chemotactic protein 2; and epithelial neutrophil-activating protein-78, can mediate angiogenesis in the absence of preceding inflammation. To date, the receptor on endothelial cells responsible for chemotaxis and neovascularization mediated by these ELR(+) CXC chemokines has not been determined. Because all ELR(+) CXC chemokines bind to CXC chemokine receptor 2 (CXCR2), we hypothesized that CXCR2 is the putative receptor for ELR(+) CXC chemokine-mediated angiogenesis. To test this postulate, we first determined whether cultured human microvascular endothelial cells expressed CXCR2. CXCR2 was detected in human microvascular endothelial cells at the protein level by both Western blot analysis and immunohistochemistry using polyclonal Abs specific for human CXCR2. To determine whether CXCR2 played a functional role in angiogenesis, we determined whether this receptor was involved in endothelial cell chemotaxis. We found that microvascular endothelial cell chemotaxis in response to ELR(+) CXC chemokines was inhibited by anti-CXCR2 Abs. In addition, endothelial cell chemotaxis in response to ELR(+) CXC chemokines was sensitive to pertussis toxin, suggesting a role for G protein-linked receptor mechanisms in this biological response. The importance of CXCR2 in mediating ELR(+) CXC chemokine-induced angiogenesis in vivo was also demonstrated by the lack of angiogenic activity induced by ELR(+) CXC chemokines in the presence of neutralizing Abs to CXCR2 in the rat corneal micropocket assay, or in the corneas of CXCR2(-/-) mice. We thus conclude that CXCR2 is the receptor responsible for ELR(+) CXC chemokine-mediated angiogenesis.
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23 MeSH Terms
Voltage-dependent, pertussis toxin insensitive inhibition of calcium currents by histamine in bovine adrenal chromaffin cells.
Currie KP, Fox AP
(2000) J Neurophysiol 83: 1435-42
MeSH Terms: Adenosine Triphosphate, Animals, Autocrine Communication, Calcium Channel Blockers, Calcium Channels, N-Type, Calcium Channels, Q-Type, Catecholamines, Cattle, Chelating Agents, Chromaffin Cells, Dinoprostone, Egtazic Acid, Electrophysiology, GTP-Binding Proteins, Histamine, Histamine Agonists, Histamine H1 Antagonists, Membrane Potentials, Paracrine Communication, Patch-Clamp Techniques, Pertussis Toxin, Virulence Factors, Bordetella
Show Abstract · Added March 30, 2013
Histamine is a known secretagogue in adrenal chromaffin cells. Activation of G-protein linked H(1) receptors stimulates phospholipase C, which generates inositol trisphosphate leading to release of intracellular calcium stores and stimulation of calcium influx through store operated and other channels. This calcium leads to the release of catecholamines. In chromaffin cells, the main physiological trigger for catecholamine release is calcium influx through voltage-gated calcium channels (I(Ca)). Therefore, these channels are important targets for the regulation of secretion. In particular N- and P/Q-type I(Ca) are subject to inhibition by transmitter/hormone receptor activation of heterotrimeric G-proteins. However, the direct effect of histamine on I(Ca) in chromaffin cells is unknown. This paper reports that histamine inhibited I(Ca) in cultured bovine adrenal chromaffin cells and this response was blocked by the H(1) antagonist mepyramine. With high levels of calcium buffering in the patch pipette solution (10 mM EGTA), histamine slowed the activation kinetics and inhibited the amplitude of I(Ca). A conditioning prepulse to +100 mV reversed the kinetic slowing and partially relieved the inhibition. These features are characteristic of a membrane delimited, voltage-dependent pathway which is thought to involve direct binding of G-protein betagamma subunits to the Ca channels. However, unlike virtually every other example of this type of inhibition, the response to histamine was not blocked by pretreating the cells with pertussis toxin (PTX). The voltage-dependent, PTX insensitive inhibition produced by histamine was modest compared with the PTX sensitive inhibition produced by ATP (28% vs. 53%). When histamine and ATP were applied concomitantly there was no additivity of the inhibition beyond that produced by ATP alone (even though the agonists appear to activate distinct G-proteins) suggesting that the inhibition produced by ATP is maximal. When experiments were carried out under conditions of low levels of calcium buffering in the patch pipette solution (0.1 mM EGTA), histamine inhibited I(Ca) in some cells using an entirely voltage insensitive pathway. We demonstrate that activation of PTX insensitive G-proteins (most likely Gq) by H(1) receptors inhibits I(Ca). This may represent a mechanism by which histamine exerts inhibitory (in addition to previously identified stimulatory) effects on catecholamine release.
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Evidence for paracrine signaling between macrophages and bovine adrenal chromaffin cell Ca(2+) channels.
Currie KP, Zhou Z, Fox AP
(2000) J Neurophysiol 83: 280-7
MeSH Terms: Adrenal Medulla, Animals, Calcium Channels, Cattle, Cell Line, Cells, Cultured, Chromaffin Cells, Coculture Techniques, Dinoprostone, GTP-Binding Proteins, Ibuprofen, Interleukin-1, Interleukin-6, Lipopolysaccharides, Macrophages, Masoprocol, Mice, Patch-Clamp Techniques, Pertussis Toxin, Signal Transduction, Virulence Factors, Bordetella
Show Abstract · Added March 30, 2013
The adrenal gland contains resident macrophages, some of which lie adjacent to the catecholamine producing chromaffin cells. Because macrophages release a variety of secretory products, it is possible that paracrine signaling between these two cell types exists. Of particular interest is the potential paracrine modulation of voltage-gated calcium channels (I(Ca)), which are the main calcium influx pathway triggering catecholamine release from chromaffin cells. We report that prostaglandin E(2) (PGE(2)), one of the main signals produced by macrophages, inhibited I(Ca) in cultured bovine adrenal chromaffin cells. The inhibition is rapid, robust, and voltage dependent; the activation kinetics are slowed and inhibition is largely reversed by a large depolarizing prepulse, suggesting that the inhibition is mediated by a direct G-protein betagamma subunit interaction with the calcium channels. About half of the response to PGE(2) was sensitive to pertussis toxin (PTX) incubation, suggesting both PTX-sensitive and -insensitive G proteins were involved. We show that activation of macrophages by endotoxin rapidly (within minutes) releases a signal that inhibits I(Ca) in chromaffin cells. The inhibition is voltage dependent and partially PTX sensitive. PGE(2) is not responsible for this inhibition as blocking cyclooxygenase with ibuprofen did not prevent the production of the inhibitory signal by the macrophages. Nor did blocking the lipoxygenase pathway with nordihydroguaiaretic acid alter production of the inhibitory signal. Our results suggest that macrophages may modulate I(Ca) and catecholamine secretion by releasing PGE(2) and other chemical signal(s).
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Opposing effects of beta(1)- and beta(2)-adrenergic receptors on cardiac myocyte apoptosis : role of a pertussis toxin-sensitive G protein.
Communal C, Singh K, Sawyer DB, Colucci WS
(1999) Circulation 100: 2210-2
MeSH Terms: Adenylate Cyclase Toxin, Adrenergic beta-Agonists, Adrenergic beta-Antagonists, Animals, Apoptosis, Carbachol, Cardiotonic Agents, Cyclic AMP, GTP-Binding Protein alpha Subunits, Gi-Go, Heart, Imidazoles, Isoproterenol, Male, Muscarinic Agonists, Myocardium, Pertussis Toxin, Prazosin, Propanolamines, Rats, Rats, Sprague-Dawley, Receptors, Adrenergic, beta-1, Receptors, Adrenergic, beta-2, Second Messenger Systems, Virulence Factors, Bordetella
Show Abstract · Added March 5, 2014
BACKGROUND - beta-Adrenergic receptor (beta-AR) stimulation increases apoptosis in adult rat cardiac (ventricular) myocytes (ARVMs) via activation of adenylyl cyclase. beta(2)-ARs may couple to a G(i)-mediated signaling pathway that can oppose the actions of adenylyl cyclase.
METHODS AND RESULTS - In ARVMs, beta-AR stimulation for 24 hours increased the number of apoptotic cells as measured by flow cytometry. beta-AR-stimulated apoptosis was abolished by the beta(1)-AR-selective antagonist CGP 20712A (P<0.05 versus beta-AR stimulation alone) but was potentiated by the beta(2)-AR-selective antagonist ICI 118,551 (P<0.05 versus beta-AR stimulation alone). The muscarinic agonist carbachol also prevented beta-AR-stimulated apoptosis (P<0.05 versus beta-AR stimulation alone), whereas pertussis toxin potentiated the apoptotic action of beta-AR stimulation (P<0.05 versus beta-AR stimulation alone) and prevented the antiapoptotic action of carbachol.
CONCLUSIONS - In ARVMs, stimulation of beta(1)-ARs increases apoptosis via a cAMP-dependent mechanism, whereas stimulation of beta(2)-ARs inhibits apoptosis via a G(i)-coupled pathway. These findings have implications for the pathophysiology and treatment of myocardial failure.
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24 MeSH Terms
Molecular events associated with the regulation of signaling by M2 muscarinic receptors.
Hosey MM, Pals-Rylaarsdam R, Lee KB, Roseberry AG, Benovic JL, Gurevich VV, Bünemann M
(1999) Life Sci 64: 363-8
MeSH Terms: Adenylate Cyclase Toxin, Amino Acid Substitution, Arrestins, Barium, Carbachol, Cell Line, Cyclic AMP-Dependent Protein Kinases, Down-Regulation, G Protein-Coupled Inwardly-Rectifying Potassium Channels, GTP-Binding Proteins, GTPase-Activating Proteins, Genes, Dominant, Humans, Phosphorylation, Potassium Channel Blockers, Potassium Channels, Potassium Channels, Inwardly Rectifying, Proteins, RGS Proteins, Receptor, Muscarinic M2, Receptors, Muscarinic, Signal Transduction, Transfection, Virulence Factors, Bordetella, beta-Adrenergic Receptor Kinases
Show Abstract · Added December 10, 2013
Multiple events are associated with the regulation of signaling by the M2 muscarinic cholinergic receptors (mAChRs). Desensitization of the attenuation of adenylyl cyclase by the M2 mAChRs appears to involve agonist-dependent phosphorylation of M2 mAChRs by G-protein coupled receptor kinases (GRKs) that phosphorylate the receptors in a serine/threonine rich motif in the 3rd intracellular domain of the receptors. Mutation of residues 307-311 from TVSTS to AVAAA in this domain of the human M2 mAChR results in a loss of receptor/G-protein uncoupling and a loss of arrestin binding. Agonist-induced sequestration of receptors away from their normal membrane environment is also regulated by agonist-induced phosphorylation of the M2 mAChRs on the 3rd intracellular domain, but in HEK cells, the predominant pathway of internalization is not regulated by GRKs or arrestins. This pathway of internalization is not inhibited by a dominant negative dynamin, and does not appear to involve either clathrin coated pits or caveolae. The signaling of the M2 mAChR to G-protein regulated inwardly rectifying K channels (GIRKs) can be modified by RGS proteins. In HEK cells, expression of RGS proteins leads to a constitutive activation of the channels through a mechanism that depends on Gbetagamma. RGS proteins appear to increase the concentration of free Gbetagamma in addition to acting as GAPs. Thus multiple mechanisms acting at either the level of the M2 mAChRs or the G-proteins can contribute to the regulation of signaling via the M2 mAChRs.
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25 MeSH Terms
Expression and immunogenicity of pertussis toxin S1 subunit-tetanus toxin fragment C fusions in Salmonella typhi vaccine strain CVD 908.
Barry EM, Gomez-Duarte O, Chatfield S, Rappuoli R, Pizza M, Losonsky G, Galen J, Levine MM
(1996) Infect Immun 64: 4172-81
MeSH Terms: Animals, Antibodies, Bacterial, CHO Cells, Cricetinae, Female, Immunization, Mice, Mice, Inbred BALB C, Peptide Fragments, Pertussis Toxin, Recombinant Fusion Proteins, Salmonella typhi, Tetanus Toxin, Vaccines, Synthetic, Virulence Factors, Bordetella
Show Abstract · Added May 27, 2014
Salmonella typhi vaccine strain CVD 908 can deliver heterologous antigens to the host immune system following mucosal immunization. Stable expression of foreign proteins in Salmonella cells often requires antigen-specific engineering strategies. Fusion of antigens to stabilizing proteins has proven to be a successful strategy for rescuing otherwise unstable proteins. We designed plasmids to allow the fusion of antigens to the amino terminus or carboxyl terminus of fragment C of tetanus toxin, separated by a 4-amino-acid hinge region. Towards the ultimate goal of developing a live oral diphtheria-pertussis-tetanus vaccine, we used these plasmids to stably express the S1 subunit of pertussis toxin in CVD 908. Driven by the anaerobically inducible nirB promoter, the S1 subunit alone was expressed poorly in Salmonella cytoplasm. In contrast, hybrid proteins with S1 fused to either the amino or carboxyl terminus of fragment C were expressed at a high level in CVD 908 and were recognized in Western blot (immunoblot) analysis by monoclonal antibodies directed to S1 and to fragment C. Mice were immunized by the oral or intranasal routes with CVD 908 derivatives harboring these recombinant plasmids. All fusion proteins elicited serum antibody responses to fragment C following intranasal immunization, whereas oral inoculation did not. The configuration of antigens constituting the fusion was critical; S1 fused to the amino terminus of fragment C was less effective than S1 fused to the carboxyl terminus in generating anti-fragment C antibodies. CVD 908 expressing truncated S1 fused to the carboxyl terminus of fragment C elicited neutralizing serum pertussis antitoxin following intranasal immunization of mice.
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Activated alpha 2-macroglobulin promotes mitogenesis in rat vascular smooth muscle cells by a mechanism that is independent of growth-factor-carrier activity.
Webb DJ, Hussaini IM, Weaver AM, Atkins TL, Chu CT, Pizzo SV, Owens GK, Gonias SL
(1995) Eur J Biochem 234: 714-22
MeSH Terms: Animals, Carrier Proteins, Cell Division, Cells, Cultured, Glycoproteins, Inositol 1,4,5-Trisphosphate, LDL-Receptor Related Protein-Associated Protein, Low Density Lipoprotein Receptor-Related Protein-1, Methylamines, Mitogens, Muscle, Smooth, Vascular, Pertussis Toxin, Protein Binding, Rats, Rats, Sprague-Dawley, Receptors, Immunologic, Recombinant Proteins, Signal Transduction, Transforming Growth Factor beta, Trypsin, Virulence Factors, Bordetella, alpha-Macroglobulins
Show Abstract · Added March 5, 2014
Vascular smooth muscle cell (vSMC) proliferation is important in atherosclerosis. We previously demonstrated that methylamine-activated alpha 2-macroglobulin (alpha 2M) and transforming growth factor beta 1 (TGF-beta 1) cause a synergistic proliferative response in quiescent rat aortic vSMCs [Stouffer, G. A., La-Marre, J., Gonias, S. L. & Owens, G. K. (1993) J. Biol. Chem. 268, 18,340-18,344]. The first goal of this study was to determine whether the synergy is due to the ability of alpha 2M-methylamine (alpha 2M-MeNH2) to bind TGF-beta 1 and target the growth factor to vSMCs that express the alpha 2M receptor. Receptor-recognized alpha 2M derivatives without TGF-beta 1-binding activity, including ternary alpha 2M-trypsin, an 18-kDa proteolytic fragment of the alpha 2M subunit, and the corresponding recombinant receptor-binding fragment (rRBF) increased vSMC [3H]thymidine incorporation and cell number in a manner similar to alpha 2M-MeNH2. In combination with TGF-beta 1, each alpha 2M derivative caused a synergistic vSMC proliferative response. vSMCs responded comparably when treated with alpha 2M-MeNH2 and TGF-beta 1 simultaneously or in sequence. Furthermore, alpha 2M-MeNH2-TGF-beta 1 complexes increased [3H]thymidine incorporation no more than alpha 2M-MeNH2 alone. These results indicate that TGF-beta 1 binding to alpha 2M is not responsible for the synergistic mitogenic activity. Additional studies were undertaken to determine whether activated alpha 2M independently induces a signal-transduction response in vSMCs. alpha 2M-MeNH2 and rRBF caused a rapid, transient increase in vSMC inositol 1,4,5-trisphosphate. This response was pertussis-toxin insensitive. Receptor-associated protein (RAP; 170 nmol/L) inhibited 91-95% of the specific binding of 125I-alpha 2M-MeNH2 and 125I-rRBF to vSMC; however, RAP did not affect the inositol 1,4,5-trisphosphate response or the mitogenic response. These studies suggest that vSMCs express a receptor, other than low-density-lipoprotein-receptor-related protein, that transduces a signal in response to activated alpha 2M. This receptor may mediate the mitogenic activity of alpha 2M in vSMC culture.
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G protein beta gamma subunits. Simplified purification and properties of novel isoforms.
Ueda N, Iñiguez-Lluhi JA, Lee E, Smrcka AV, Robishaw JD, Gilman AG
(1994) J Biol Chem 269: 4388-95
MeSH Terms: Adenylate Cyclase Toxin, Adenylyl Cyclases, Animals, Base Sequence, Calcium, Calmodulin, Cattle, Cloning, Molecular, DNA Primers, Enzyme Activation, GTP-Binding Proteins, In Vitro Techniques, Molecular Sequence Data, Moths, Mutagenesis, Site-Directed, Pertussis Toxin, Protein Processing, Post-Translational, Rats, Recombinant Proteins, Structure-Activity Relationship, Type C Phospholipases, Virulence Factors, Bordetella
Show Abstract · Added March 5, 2014
The beta and gamma subunits of heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) form tightly associated complexes. To examine functional differences among the large number of possible combinations of unique beta and gamma subunits, we have synthesized and characterized beta gamma complexes containing gamma 5 and gamma 7, two widely distributed gamma subunits. When either gamma 5 or gamma 7 is expressed concurrently with beta 1 or beta 2 subunits in a baculovirus/Sf9 cell system, all four subunit complexes support pertussis toxin-catalyzed ADP-ribosylation of rGi alpha 1 (where "r" indicates recombinant), indicating formation of functional complexes. Each of the complexes was purified by subunit exchange chromatography, using the G203A mutant of rGi alpha 1 as the immobilized ligand. The purified preparations were compared with other recombinant beta gamma subunits, including beta 1 gamma 1 and beta 1 gamma 2, for their ability to modulate type I and II adenylyl cyclase activities; stimulate phosphoinositide-specific phospholipase C beta; support pertussis toxin-catalyzed ADP-ribosylation of rGi alpha 1 and Go alpha; and inhibit steady-state GTP hydrolysis catalyzed by Gs alpha, Go alpha, and myristoylated rGi alpha 2. The results emphasize the unique properties of beta 1 gamma 1. The properties of the complexes containing gamma 5 or gamma 7 were similar to each other and to those of beta 1 gamma 2.
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22 MeSH Terms