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Results: 171 to 177 of 177

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Surfaces of interaction between Gt and rhodopsin in the GDP-bound and empty-pocket configurations.
Hamm HE
(1990) Adv Second Messenger Phosphoprotein Res 24: 76-82
MeSH Terms: Adenosine Diphosphate Ribose, Animals, Cattle, Guanine Nucleotides, Guanosine Diphosphate, Protein Binding, Protein Conformation, Rhodopsin, Rod Cell Outer Segment, Transducin, Virulence Factors, Bordetella
Added December 10, 2013
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11 MeSH Terms
The development of physiologic responsiveness to muscarinic stimulation in embryonic chick heart. Relationship to increased levels of pertussis toxin substrates.
Barnett JV, Shamah SM, Galper JB
(1990) Ann N Y Acad Sci 588: 145-54
MeSH Terms: Adenylate Cyclase Toxin, Adenylyl Cyclases, Animals, Chick Embryo, GTP-Binding Proteins, Heart, Immunoblotting, Isoproterenol, Myocardium, Organ Culture Techniques, Pertussis Toxin, Poly(ADP-ribose) Polymerases, Receptors, Muscarinic, Substrate Specificity, Virulence Factors, Bordetella
Show Abstract · Added February 21, 2016
Studies of the development of parasympathetic responsiveness in embryonic chick hearts have demonstrated that between days 2.5 and 10 in ovo the ability of muscarinic agonists to inhibit adenylate cyclase activity increases 10-fold in parallel with a 2.7-fold increase in the level of alpha i and alpha o. Thus, muscarinic inhibition of adenylate cyclase increases in parallel with an increase in alpha o and alpha i. These data suggest that changes in levels of guanine nucleotide regulatory proteins control, at least in part, the appearance of a parasympathetic response in the heart during embryonic development of the chick.
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15 MeSH Terms
Evidence that UTP and ATP regulate phospholipase C through a common extracellular 5'-nucleotide receptor in human airway epithelial cells.
Brown HA, Lazarowski ER, Boucher RC, Harden TK
(1991) Mol Pharmacol 40: 648-55
MeSH Terms: Adenosine Triphosphate, Chlorides, Enzyme Activation, Epithelium, GTP-Binding Proteins, Guanosine 5'-O-(3-Thiotriphosphate), Humans, Nucleotides, Pertussis Toxin, Receptors, Purinergic, Trachea, Type C Phospholipases, Uridine Triphosphate, Virulence Factors, Bordetella
Show Abstract · Added March 21, 2013
Extracellular ATP and UTP produced a rapid accumulation of inositol phosphates in human airway epithelial cells (CF/T43). The order of agonist potencies for a series of nucleotide analogues differed markedly from that of the classically described P2x- or P2y-purinergic receptors. UTP was the most potent agonist and was fully efficacious; ATP and adenosine-5'-O-(3-thiotriphosphate) were also full agonists. In contrast, 2-methylthio-ATP, adenosine-5'-O-(2-thiodiphosphate) and alpha,beta-methylene-ATP were without effect. ADP and UDP had little or no effect at concentrations as high as 100 microM, and deoxyribose and dideoxyribose compounds were inactive. The effects of ATP and UTP were not additive, whereas bradykinin- or histamine-stimulated inositol phosphate production was additive with the effects of ATP or UTP. Preincubation of cells with either UTP or ATP resulted in a parallel loss of responsiveness to both agonists. Desensitization was specific for the response to nucleotides, because no ATP- or UTP-induced effect on the response to histamine or bradykinin was observed. Pertussis toxin treatment of CF/T43 cells produced a 30-40% decrease in the response to ATP or UTP, which correlated with the ADP-ribosylation of 41- and 43-kDa proteins. Bradykinin and histamine responses were not modified by pertussis toxin. Guanine nucleotides had little effect on the inositol phosphate response in intact CF/T43 cells at concentrations below 100 microM. However, in streptolysin-O-permeabilized cells GTP-gamma S produced a concentration-dependence activation of inositol phosphate formation. UTP or ATP had little effect in permeabilized cells in the absence of guanine nucleotides but markedly increased inositol phosphate formation in the presence of guanine nucleotides. Taken together, these results suggest that UTP and ATP activate a 5'-nucleotide receptor on CF/T43 cells that is distinct from the classically defined P2x- and P2y-purinergic receptors. Activation of phospholipase C by this receptor involves, at least in part, a guanine nucleotide-binding regulatory protein.
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14 MeSH Terms
Structural analysis of rod GTP-binding protein, Gt. Limited proteolytic digestion pattern of Gt with four proteases defines monoclonal antibody epitope.
Mazzoni MR, Malinski JA, Hamm HE
(1991) J Biol Chem 266: 14072-81
MeSH Terms: Amino Acid Sequence, Animals, Antibodies, Monoclonal, Blotting, Western, Cattle, Endopeptidases, Epitopes, GTP-Binding Proteins, Guanosine 5'-O-(3-Thiotriphosphate), Metalloendopeptidases, Molecular Sequence Data, Molecular Weight, Peptide Fragments, Rod Cell Outer Segment, Serine Endopeptidases, Time Factors, Trypsin, Virulence Factors, Bordetella
Show Abstract · Added December 10, 2013
The epitope of monoclonal antibody (mAb 4A), which recognizes the alpha subunit of the rod G protein, Gt, has been suggested to be both at the carboxyl terminus (Deretic, D., and Hamm, H.E. (1987) J. Biol. Chem. 262, 10839-10847) and the amino terminus (Navon, S.E., and Fung, B.K.-K. (1988) J. Biol. Chem. 263, 489-496) of the molecule. To characterize further the mAb 4A binding site on alpha t and to resolve the discrepancy between these results limited proteolytic digestion of Gt or alpha t using four proteases with different substrate specificities has been performed. Endoproteinase Arg-C, which cleaves the peptide bond at the carboxylic side of arginine residues, cleaved the majority of alpha t into two fragments of 34 and 5 kDa. The alpha t 34-kDa fragment in the holoprotein, but not alpha t-guanosine 5'-O-(3-thiotriphosphate), was converted further to a 23-kDa fragment. A small fraction of alpha t-GDP was cleaved into 23- and 15-kDa fragments. Endoproteinase Lys-C, which selectively cleaves at lysine residues, progressively removed 17 and then 8 residues from the amino terminus, forming 38- and 36-kDa fragments. Staphylococcus aureus V8 protease is known to remove 21 amino acid residues from the amino-terminal region of alpha t, with the formation of a 38-kDa fragment. L-1-Tosylamido-2-phenylethyl chloromethyl ketone-treated trypsin cleaved alpha t progressively into fragments of known amino acid sequences (38, then 32 and 5, then 21 and 12 kDa) and a transient 34 kDa fragment. The binding of mAb 4A to proteolytic fragments was analyzed by Western blot and immunoprecipitation. The major fragments recognized by mAb 4A on Western blots were the 34- and 23-kDa fragments obtained by endoproteinase Arg-C and tryptic digestion. Under conditions that allowed sequencing of the 15- and 5-kDa fragments neither the 34- nor the 23-kDa fragments could be sequenced by Edman degradation, indicating that they contained a blocked amino terminus. The smallest fragment that retained mAb 4A binding was the 23-kDa fragment containing Met1 to Arg204. Thus the main portion of the mAb 4A antigenic site was located within this fragment, indicating that the carboxyl-terminal residues from Lys205 to Phe350 were not required for recognition by the antibody. Additionally, the antibody did not bind the 38- and 36-kDa or other fragments containing the carboxyl terminus, showing that the amino-terminal residues from Met1 to Lys17 were essential for antibody binding to alpha t.
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18 MeSH Terms
Helicobacter pylori and gastroduodenal disease.
Cover TL, Blaser MJ
(1992) Annu Rev Med 43: 135-45
MeSH Terms: Bacteriological Techniques, Duodenitis, Gastritis, Helicobacter Infections, Helicobacter pylori, Humans, Peptic Ulcer, Virulence
Show Abstract · Added March 5, 2014
Helicobacter pylori infection is now recognized as the primary cause of active chronic gastritis in humans. Most infected persons remain asymptomatic, but are at increased risk for the development of peptic ulcer disease and possibly gastric cancer. The pathogenesis of this infection is not well understood, but motility and urease activity are virulence factors in an animal model. The eradication of H. pylori infection is associated with resolution of gastritis and a decreased rate of duodenal ulcer recurrence.
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8 MeSH Terms
Potentiation of Helicobacter pylori vacuolating toxin activity by nicotine and other weak bases.
Cover TL, Vaughn SG, Cao P, Blaser MJ
(1992) J Infect Dis 166: 1073-8
MeSH Terms: Ammonium Chloride, Bacterial Proteins, Bacterial Toxins, Drug Synergism, HeLa Cells, Helicobacter pylori, Humans, Kinetics, Methylamines, Monensin, Nicotine, Vacuoles, Virulence
Show Abstract · Added March 5, 2014
About 50% of Helicobacter pylori isolates produce a vacuolating toxin in vitro, which may be an important determinant of virulence. Because ammonium salts potentiate H. pylori toxin activity, the effect of other weak bases upon toxin activity was determined. Vacuolation of HeLa cells was quantitated using a neutral red uptake assay. As expected, ammonium chloride, trimethylamine, triethanolamine, and nicotine each induced vacuolation of HeLa cells when tested independently. In addition, each of these weak bases potentiated H. pylori vacuolating toxin activity, whereas sodium chloride or sodium hydroxide did not. Sequential incubation of cells with toxin followed by nicotine resulted in potentiation of vacuolation, whereas sequential incubation in the reverse order did not lead to potentiation. Monensin inhibited the formation of vacuoles by either H. pylori vacuolating toxin or nicotine. The potentiation of H. pylori toxin activity by ammonia and nicotine may contribute to gastroduodenal mucosal injury associated with this infection.
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13 MeSH Terms
Receptor-mediated autocrine growth-stimulatory effect of 5-hydroxytryptamine on cultured human pancreatic carcinoid cells.
Ishizuka J, Beauchamp RD, Townsend CM, Greeley GH, Thompson JC
(1992) J Cell Physiol 150: 1-7
MeSH Terms: 8-Bromo Cyclic Adenosine Monophosphate, Cell Division, Cyclic AMP, Cyclic GMP, Ergolines, Humans, Pancreatic Neoplasms, Pertussis Toxin, Phosphatidylinositols, Pindolol, Receptors, Serotonin, Second Messenger Systems, Serotonin, Serotonin Antagonists, Tumor Cells, Cultured, Virulence Factors, Bordetella
Show Abstract · Added May 3, 2013
5-hydroxytryptamine (5-HT) is a mitogen for fibroblasts, vascular smooth muscle cells, renal mesangial cells, and jejunal crypt cells. The human carcinoid cell line (termed BON) that we established in our laboratory from a pancreatic carcinoid tumor produces and secretes 5-HT. In this study, therefore, we examined the effect of 5-HT on growth of BON cells. Furthermore, by use of selective 5-HT receptor antagonists, we examined receptor and post-receptor mechanisms by which 5-HT-induced responses were produced. 5-HT stimulated growth of BON cells. 5-HT stimulated phosphatidylinositol (PI) hydrolysis in a dose-dependent fashion and inhibited cyclic AMP production in a dose-dependent fashion. The 5-HT1A/1B receptor antagonist, SDZ 21-009, prevented the reduction of cyclic AMP production evoked by 5-HT and inhibited the mitogenic action of 5-HT. The 5-HT1C/2 receptor antagonist, mesulergine, competitively inhibited PI hydrolysis, but did not affect the mitogenic action of 5-HT. The mitogenic action of 5-HT and the reduction of cyclic AMP production evoked by 5-HT were also inhibited by pertussis toxin. These results suggest that 5-HT is an autocrine growth factor for BON cells and that mitogenic mechanism of 5-HT involves receptor-mediated inhibition of the production of cyclic AMP which may be linked to pertussis toxin-sensitive GTP binding protein. 8-bromo-cyclic AMP inhibited growth of BON cells whereas 8-bromo-cyclic GMP had no effect on cell growth. Involvement of protein kinase A in BON cell growth regulation was confirmed by the observation that a cAMP-dependent protein kinase antagonist (Rp-cAMPS) could stimulate BON cell growth.
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16 MeSH Terms