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Heteromeric Anopheline odorant receptors exhibit distinct channel properties.
Pask GM, Jones PL, R├╝tzler M, Rinker DC, Zwiebel LJ
(2011) PLoS One 6: e28774
MeSH Terms: Animals, Anopheles, Cations, Divalent, Cations, Monovalent, Cell Line, Ion Channels, Odorants, Permeability, Protein Multimerization, Receptors, Odorant, Ruthenium Red
Show Abstract · Added May 27, 2014
BACKGROUND - Insect odorant receptors (ORs) function as odorant-gated ion channels consisting of a conventional, odorant-binding OR and the Orco coreceptor. While Orco can function as a homomeric ion channel, the role(s) of the conventional OR in heteromeric OR complexes has largely focused only on odorant recognition.
RESULTS - To investigate other roles of odorant-binding ORs, we have employed patch clamp electrophysiology to investigate the properties of the channel pore of several OR complexes formed by a range of different odorant-specific Anopheles gambiae ORs (AgOrs) each paired with AgOrco. These studies reveal significant differences in cation permeability and ruthenium red susceptibility among different AgOr complexes.
CONCLUSIONS - With observable differences in channel function, the data support a model in which the odorant-binding OR also affects the channel pore. The variable effect contributed by the conventional OR on the conductive properties of odorant-gated sensory channels adds additional complexity to insect olfactory signaling, with differences in odor coding beginning with ORs on the periphery of the olfactory system.
0 Communities
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11 MeSH Terms
Acinetobacter baumannii increases tolerance to antibiotics in response to monovalent cations.
Hood MI, Jacobs AC, Sayood K, Dunman PM, Skaar EP
(2010) Antimicrob Agents Chemother 54: 1029-41
MeSH Terms: Acinetobacter baumannii, Anti-Bacterial Agents, Bacterial Proteins, Cations, Monovalent, Culture Media, Drug Resistance, Bacterial, Gene Expression Profiling, Gene Expression Regulation, Bacterial, Humans, Microbial Sensitivity Tests, Oligonucleotide Array Sequence Analysis, Proteomics, Sodium Chloride, Virulence Factors
Show Abstract · Added July 28, 2012
Acinetobacter baumannii is well adapted to the hospital environment, where infections caused by this organism are associated with significant morbidity and mortality. Genetic determinants of antimicrobial resistance have been described extensively, yet the mechanisms by which A. baumannii regulates antibiotic resistance have not been defined. We sought to identify signals encountered within the hospital setting or human host that alter the resistance phenotype of A. baumannii. In this regard, we have identified NaCl as being an important signal that induces significant tolerance to aminoglycosides, carbapenems, quinolones, and colistin upon the culturing of A. baumannii cells in physiological NaCl concentrations. Proteomic analyses of A. baumannii culture supernatants revealed the release of outer membrane proteins in high NaCl, including two porins (CarO and a 33- to 36-kDa protein) whose loss or inactivation is associated with antibiotic resistance. To determine if NaCl affected expression at the transcriptional level, the transcriptional response to NaCl was determined by microarray analyses. These analyses highlighted 18 genes encoding putative efflux transporters that are significantly upregulated in response to NaCl. Consistent with this, the effect of NaCl on the tolerance to levofloxacin and amikacin was significantly reduced upon the treatment of A. baumannii with an efflux pump inhibitor. The effect of physiological concentrations of NaCl on colistin resistance was conserved in a panel of multidrug-resistant isolates of A. baumannii, underscoring the clinical significance of these observations. Taken together, these data demonstrate that A. baumannii sets in motion a global regulatory cascade in response to physiological NaCl concentrations, resulting in broad-spectrum tolerance to antibiotics.
1 Communities
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14 MeSH Terms
Expression of allosteric linkage between the sodium ion binding site and exosite I of thrombin during prothrombin activation.
Kroh HK, Tans G, Nicolaes GA, Rosing J, Bock PE
(2007) J Biol Chem 282: 16095-104
MeSH Terms: Allosteric Regulation, Allosteric Site, Blood Coagulation Factors, Cations, Monovalent, Cell Membrane, Endopeptidases, Enzyme Activation, Enzyme Precursors, Hirudins, Humans, Kinetics, Peptide Fragments, Prothrombin, Sodium, Thrombin
Show Abstract · Added January 20, 2015
The specificity of thrombin for procoagulant and anticoagulant substrates is regulated allosterically by Na+. Ordered cleavage of prothrombin (ProT) at Arg320 by the prothrombinase complex generates proteolytically active, meizothrombin (MzT), followed by cleavage at Arg271 to produce thrombin and fragment 1.2. The alternative pathway of initial cleavage at Arg271 produces the inactive zymogen form, the prethrombin 2 (Pre 2).fragment 1.2 complex, which is cleaved subsequently at Arg320. Cleavage at Arg320 of ProT or prethrombin 1 (Pre 1) activates the catalytic site and the precursor form of exosite I (proexosite I). To determine the pathway of expression of Na+-(pro)exosite I linkage during ProT activation, the effects of Na+ on the affinity of fluorescein-labeled hirudin-(54-65) ([5F]Hir-(54-65)(SO-3)) for the zymogens, ProT, Pre 1, and Pre 2, and for the proteinases, MzT and MzT-desfragment 1 (MzT(-F1)) were quantitated. The zymogens showed no significant linkage between proexosite I and Na+, whereas cleavage at Arg320 caused the affinities of MzT and MzT(-F1) for [5F]Hir-(54-65)(SO-3) to be enhanced by Na+ 8- to 10-fold and 5- to 6-fold, respectively. MzT and MzT(-F1) showed kinetically different mechanisms of Na+ enhancement of chromogenic substrate hydrolysis. The results demonstrate for the first time that MzT is regulated allosterically by Na+. The results suggest that the distinctive procoagulant substrate specificity of MzT, in activating factor V and factor VIII on membranes, and the anticoagulant, membrane-modulated activation of protein C by MzT bound to thrombomodulin are regulated by Na+-induced allosteric transition. Further, the Na+ enhancement in MzT activity and exosite I affinity may function in directing the sequential ProT activation pathway by accelerating thrombin formation from the MzT fast form.
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15 MeSH Terms
Flow-through lipid nanotube arrays for structure-function studies of membrane proteins by solid-state NMR spectroscopy.
Chekmenev EY, Gor'kov PL, Cross TA, Alaouie AM, Smirnov AI
(2006) Biophys J 91: 3076-84
MeSH Terms: Aluminum Oxide, Binding Sites, Cations, Divalent, Cations, Monovalent, Gramicidin, Hydrogen-Ion Concentration, Lipid Bilayers, Magnesium, Membrane Proteins, Nanotubes, Nuclear Magnetic Resonance, Biomolecular, Oxygen Isotopes, Potassium, Protein Array Analysis, Temperature
Show Abstract · Added March 5, 2014
A novel method for studying membrane proteins in a native lipid bilayer environment by solid-state NMR spectroscopy is described and tested. Anodic aluminum oxide (AAO) substrates with flow-through 175 nm wide and 60-mum-long nanopores were employed to form macroscopically aligned peptide-containing lipid bilayers that are fluid and highly hydrated. We demonstrate that the surfaces of both leaflets of such bilayers are fully accessible to aqueous solutes. Thus, high hydration levels as well as pH and desirable ion and/or drug concentrations could be easily maintained and modified as desired in a series of experiments with the same sample. The method allows for membrane protein NMR experiments in a broad pH range that could be extended to as low as 1 and as high as 12 units for a period of up to a few hours and temperatures as high as 70 degrees C without losing the lipid alignment or bilayers from the nanopores. We demonstrate the utility of this method by a solid-state 19.6 T (17)O NMR study of reversible binding effects of mono- and divalent ions on the chemical shift properties of the Leu(10) carbonyl oxygen of transmembrane pore-forming peptide gramicidin A (gA). We further compare the (17)O shifts induced by binding metal ions to the binding of protons in the pH range from 1 to 12 and find a significant difference. This unexpected result points to a difference in mechanisms for ion and proton conduction by the gA pore. We believe that a large number of solid-state NMR-based studies, including structure-function, drug screening, proton exchange, pH, and other titration experiments, will benefit significantly from the method described here.
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15 MeSH Terms
Analysis of unsaturated compounds by Ag+ coordination ionspray mass spectrometry: studies of the formation of the Ag+/lipid complex.
Seal JR, Havrilla CM, Porter NA, Hachey DL
(2003) J Am Soc Mass Spectrom 14: 872-80
MeSH Terms: Cations, Monovalent, Cholesterol Esters, Fats, Unsaturated, Lipid Peroxidation, Silver, Spectrometry, Mass, Electrospray Ionization
Show Abstract · Added March 20, 2014
Coordination ionspray mass spectrometry (CIS-MS) is a useful tool in the detection and identification of cholesterol ester and phospholipid hydroperoxides and diacyl peroxides. Extensive studies of a series of cholesterol esters using CIS-MS revealed the following: (1) Cholesterol esters with equal number of double bonds as the internal standard showed a linear relative response in the mass spectrometer while compounds with non-equal numbers of double bonds gave a nonlinear relative response. (2) Complex adducts containing cholesterol ester, silver ion, AgF, AgBF(4), and 2-propanoxide form when silver is in molar excess of cholesterol esters, reducing the [M + Ag](+) signal. (3) In a mixture of cholesterol esters where silver is limiting, Ch22:6 and Ch20:4 bind to silver at the expense of Ch18:2 and have a higher signal in the mass spectrometer. (4) In a mixture of cholesterol esters where silver concentration is twofold greater than total cholesterol ester concentration, Ch22:6 and Ch20:4 form large complex adducts more frequently than Ch18:2 and have a lower signal in the mass spectrometer.
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6 MeSH Terms
Allosteric effects of a monoclonal antibody against thrombin exosite II.
Colwell NS, Blinder MA, Tsiang M, Gibbs CS, Bock PE, Tollefsen DM
(1998) Biochemistry 37: 15057-65
MeSH Terms: Allosteric Regulation, Animals, Antibodies, Monoclonal, Binding Sites, COS Cells, Cations, Monovalent, Enzyme Activation, Epitopes, Hirudins, Humans, Immunoglobulin Fab Fragments, Immunoglobulin G, Models, Molecular, Multiple Myeloma, Peptide Fragments, Recombinant Proteins, Sodium, Thrombin
Show Abstract · Added January 20, 2015
We previously isolated a monoclonal antithrombin IgG from a patient with multiple myeloma [Colwell et al. (1997) Br. J. Haematol. 97, 219-226]. Using a panel of 55 surface mutants of recombinant thrombin, we now show that the epitope for the IgG most likely includes Arg-101, Arg-233, and Lys-236 in exosite II. The IgG affects the rate at which thrombin cleaves various peptide p-nitroanilide substrates with arginine in the P1 position, increasing the kcat for substrates with a P2 glycine residue but generally decreasing the kcat for substrates with a P2 proline. The allosteric effect of the IgG is altered by deletion of Pro-60b, Pro-60c, and Trp-60d from the 60-loop of thrombin, which lies between exosite II and the catalytic triad. The effect of the IgG, however, does not depend on the presence or absence of sodium ions, a known allosteric regulator of thrombin. The IgG does not affect the conformation of thrombin exosite I as determined by binding of a fluorescent derivative of hirudin54-65. These results provide evidence for a direct allosteric linkage between exosite II and the catalytic site of thrombin.
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18 MeSH Terms