Relevant bibliographies by topics / Periplasmic phosphate binding protein

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Academic literature on the topic 'Periplasmic phosphate binding protein'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Periplasmic phosphate binding protein"

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Schweizer, Herbert P. "Coordinate derepression of alkaline phosphatase, and binding protein dependent transport systems for phosphate and sn-glycerol-3-phosphate by phosphate starvation in Erwinia carotovora subsp. carotovora." Canadian Journal of Microbiology 40, no. 4 (April 1, 1994): 310–13. http://dx.doi.org/10.1139/m94-050.

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In Erwinia carotovora subsp. carotovora EC14 grown under conditions of phosphate starvation, alkaline phosphatase, and binding protein dependent transport systems for inorganic phosphate andsn-glycerol-3-phosphate were simultaneously derepressed. Analysis of periplasmic protein profiles from phosphate-starved cells revealed four starvation-inducible proteins. Three of these proteins corresponded to alkaline phosphatase, a binding protein for phosphate, and a binding protein for.sn-glycerol-3-phosphate, respectively. The coordinate derepression of these proteins demonstrates the existence of a phosphate regulon similar to that found in other members of the family Enterobacteriaceae.Key words: Erwinia, phosphate, regulon, alkaline phosphatase, binding protein.
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Dennis, Matthew L., Lygie Esquirol, Tom Nebl, Janet Newman, Colin Scott, and Thomas S. Peat. "The evolving story of AtzT, a periplasmic binding protein." Acta Crystallographica Section D Structural Biology 75, no. 11 (October 31, 2019): 995–1002. http://dx.doi.org/10.1107/s2059798319013883.

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Atrazine is an s-triazine-based herbicide that is used in many countries around the world in many millions of tons per year. A small number of organisms, such as Pseudomonas sp. strain ADP, have evolved to use this modified s-triazine as a food source, and the various genes required to metabolize atrazine can be found on a single plasmid. The atomic structures of seven of the eight proteins involved in the breakdown of atrazine by Pseudomonas sp. strain ADP have been determined by X-ray crystallography, but the structures of the proteins required by the cell to import atrazine for use as an energy source are still lacking. The structure of AtzT, a periplasmic binding protein that may be involved in the transport of a derivative of atrazine, 2-hydroxyatrazine, into the cell for mineralization, has now been determined. The structure was determined by SAD phasing using an ethylmercury phosphate derivative that diffracted X-rays to beyond 1.9 Å resolution. `Native' (guanine-bound) and 2-hydroxyatrazine-bound structures were also determined to high resolution (1.67 and 1.65 Å, respectively), showing that 2-hydroxyatrazine binds in a similar way to the purportedly native ligand. Structural similarities led to the belief that it may be possible to evolve AtzT from a purine-binding protein to a protein that can bind and detect atrazine in the environment.
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Pegos, Vanessa R., Louis Hey, Jacob LaMirande, Rachel Pfeffer, Rosalie Lipsh, Moshe Amitay, Daniel Gonzalez, and Mikael Elias. "Phosphate-binding protein fromPolaromonasJS666: purification, characterization, crystallization and sulfur SAD phasing." Acta Crystallographica Section F Structural Biology Communications 73, no. 6 (May 25, 2017): 342–46. http://dx.doi.org/10.1107/s2053230x17007373.

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Phosphate-binding proteins (PBPs) are key proteins that belong to the bacterial ABC-type phosphate transporters. PBPs are periplasmic (or membrane-anchored) proteins that capture phosphate anions from the environment and release them to the transmembrane transporter. Recent work has suggested that PBPs have evolved for high affinity as well as high selectivity. In particular, a short, unique hydrogen bond between the phosphate anion and an aspartate residue has been shown to be critical for selectivity, yet is not strictly conserved in PBPs. Here, the PBP fromPolaromonasJS666 is focused on. Interestingly, this PBP is predicted to harbor different phosphate-binding residues to currently known PBPs. Here, it is shown that the PBP fromPolaromonasJS666 is capable of binding phosphate, with a maximal binding activity at pH 8. Its structure is expected to reveal its binding-cleft configuration as well as its phosphate-binding mode. Here, the expression, purification, characterization, crystallization and X-ray diffraction data collection to 1.35 Å resolution of the PBP fromPolaromonasJS666 are reported.
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Pegos, Vanessa R., Francisco Javier Medrano, and Andrea Balan. "Crystallization and preliminary X-ray diffraction analysis of the phosphate-binding protein PhoX fromXanthomonas citri." Acta Crystallographica Section F Structural Biology Communications 70, no. 12 (November 14, 2014): 1604–7. http://dx.doi.org/10.1107/s2053230x14021840.

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Xanthomonas axonopodispv.citri(X. citri) is an important bacterium that causes citrus canker disease in plants in Brazil and around the world, leading to significant economic losses. Determination of the physiology and mechanisms of pathogenesis of this bacterium is an important step in the development of strategies for its containment. Phosphate is an essential ion in all microrganisms owing its importance during the synthesis of macromolecules and in gene and protein regulation. Interestingly,X. citrihas been identified to present two periplasmic binding proteins that have not been further characterized: PstS, from an ATP-binding cassette for high-affinity uptake and transport of phosphate, and PhoX, which is encoded by an operon that also contains a putative porin for the transport of phosphate. Here, the expression, purification and crystallization of the phosphate-binding protein PhoX and X-ray data collection at 3.0 Å resolution are described. Biochemical, biophysical and structural data for this protein will be helpful in the elucidation of its function in phosphate uptake and the physiology of the bacterium.
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Khan, Ali G., Stephen R. Shouldice, Leslie W. Tari, and Anthony B. Schryvers. "The role of the synergistic phosphate anion in iron transport by the periplasmic iron-binding protein from Haemophilus influenzae." Biochemical Journal 403, no. 1 (March 13, 2007): 43–48. http://dx.doi.org/10.1042/bj20061589.

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The acquisition of iron from transferrin by Gram-negative bacterial pathogens is dependent on a periplasmic ferric-ion-binding protein, FbpA. FbpA shuttles iron from the outer membrane to an inner membrane transport complex. A bound phosphate anion completes the iron co-ordination shell of FbpA and kinetic studies demonstrate that the anion plays a critical role in iron binding and release in vitro. The present study was initiated to directly address the hypothesis that the synergistic anion is required for transport of iron in intact cells. A series of site-directed mutants in the anion-binding amino acids of the Haemophilus influenzae FbpA (Gln-58, Asn-175 and Asn-193) were prepared to provide proteins defective in binding of the phosphate anion. Crystal structures of various mutants have revealed that alteration of the C-terminal domain ligands (Asn-175 or Asn-193) but not the N-terminal domain ligand (Gln-58) abrogated binding of the phosphate anion. The mutant proteins were introduced into H. influenzae to evaluate their ability to mediate iron transport. All of the single site-directed mutants (Q58L, N175L and N193L) were capable of mediating iron acquisition from transferrin and from limiting concentrations of ferric citrate. The results suggest that the transport of iron by FbpA is not dependent on binding of phosphate in the synergistic anion-binding site.
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Khambati, Husain K., Trevor F. Moraes, Jagroop Singh, Stephen R. Shouldice, Rong-hua Yu, and Anthony B. Schryvers. "The role of vicinal tyrosine residues in the function of Haemophilus influenzae ferric-binding protein A." Biochemical Journal 432, no. 1 (October 25, 2010): 57–67. http://dx.doi.org/10.1042/bj20101043.

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The periplasmic FbpA (ferric-binding protein A) from Haemophilus influenzae plays a critical role in acquiring iron from host transferrin, shuttling iron from the outer-membrane receptor complex to the inner-membrane transport complex responsible for transporting iron into the cytoplasm. In the present study, we report on the properties of a series of site-directed mutants of two adjacent tyrosine residues involved in iron co-ordination, and demonstrate that, in contrast with mutation of equivalent residues in the N-lobe of human transferrin, the mutant FbpAs retain significant iron-binding affinity regardless of the nature of the replacement amino acid. The Y195A and Y196A FbpAs are not only capable of binding iron, but are proficient in mediating periplasm-to-cytoplasm iron transport in a reconstituted FbpABC pathway in a specialized Escherichia coli reporter strain. This indicates that their inability to mediate iron acquisition from transferrin is due to their inability to compete for iron with receptor-bound transferrin. Wild-type iron-loaded FbpA could be crystalized in a closed or open state depending upon the crystallization conditions. The synergistic phosphate anion was not present in the iron-loaded open form, suggesting that initial anchoring of iron was mediated by the adjacent tyrosine residues and that alternate pathways for iron and anion binding and release may be considered. Collectively, these results demonstrate that the presence of a twin-tyrosine motif common to many periplasmic iron-binding proteins is critical for initially capturing the ferric ion released by the outer-membrane receptor complex.
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Choi, Suk Soon, Hyun Min Lee, Jeong Hyub Ha, Dong Gyun Kang, Chang Sup Kim, Jeong Hyun Seo, and Hyung Joon Cha. "Biological Removal of Phosphate at Low Concentrations Using Recombinant Escherichia coli Expressing Phosphate-Binding Protein in Periplasmic Space." Applied Biochemistry and Biotechnology 171, no. 5 (March 16, 2013): 1170–77. http://dx.doi.org/10.1007/s12010-013-0187-1.

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Eppler, Tanja, Pieter Postma, Alexandra Schütz, Uwe Völker, and Winfried Boos. "Glycerol-3-Phosphate-Induced Catabolite Repression in Escherichia coli." Journal of Bacteriology 184, no. 11 (June 1, 2002): 3044–52. http://dx.doi.org/10.1128/jb.184.11.3044-3052.2002.

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ABSTRACT The formation of glycerol-3-phosphate (G3P) in cells growing on TB causes catabolite repression, as shown by the reduction in malT expression. For this repression to occur, the general proteins of the phosphoenolpyruvate-dependent phosphotransferase system (PTS), in particular EIIAGlc, as well as the adenylate cyclase and the cyclic AMP-catabolite activator protein system, have to be present. We followed the level of EIIAGlc phosphorylation after the addition of glycerol or G3P. In contrast to glucose, which causes a dramatic shift to the dephosphorylated form, glycerol or G3P only slightly increased the amount of dephosphorylated EIIAGlc. Isopropyl-β-d-thiogalactopyranoside-induced overexpression of EIIAGlc did not prevent repression by G3P, excluding the possibility that G3P-mediated catabolite repression is due to the formation of unphosphorylated EIIAGlc. A mutant carrying a C-terminally truncated adenylate cyclase was no longer subject to G3P-mediated repression. We conclude that the stimulation of adenylate cyclase by phosphorylated EIIAGlc is controlled by G3P and other phosphorylated sugars such as d-glucose-6-phosphate and is the basis for catabolite repression by non-PTS compounds. Further metabolism of these compounds is not necessary for repression. Two-dimensional polyacrylamide gel electrophoresis was used to obtain an overview of proteins that are subject to catabolite repression by glycerol. Some of the prominently repressed proteins were identified by peptide mass fingerprinting. Among these were periplasmic binding proteins (glutamine and oligopeptide binding protein, for example), enzymes of the tricarboxylic acid cycle, aldehyde dehydrogenase, Dps (a stress-induced DNA binding protein), and d-tagatose-1,6-bisphosphate aldolase.
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Keegan, Ronan, David G. Waterman, David J. Hopper, Leighton Coates, Graham Taylor, Jingxu Guo, Alun R. Coker, Peter T. Erskine, Steve P. Wood, and Jonathan B. Cooper. "The 1.1 Å resolution structure of a periplasmic phosphate-binding protein fromStenotrophomonas maltophilia: a crystallization contaminant identified by molecular replacement using the entire Protein Data Bank." Acta Crystallographica Section D Structural Biology 72, no. 8 (July 27, 2016): 933–43. http://dx.doi.org/10.1107/s2059798316010433.

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During efforts to crystallize the enzyme 2,4-dihydroxyacetophenone dioxygenase (DAD) fromAlcaligenessp. 4HAP, a small number of strongly diffracting protein crystals were obtained after two years of crystal growth in one condition. The crystals diffracted synchrotron radiation to almost 1.0 Å resolution and were, until recently, assumed to be formed by the DAD protein. However, when another crystal form of this enzyme was eventually solved at lower resolution, molecular replacement using this new structure as the search model did not give a convincing solution with the original atomic resolution data set. Hence, it was considered that these crystals might have arisen from a protein impurity, although molecular replacement using the structures of common crystallization contaminants as search models again failed. A script to perform molecular replacement usingMOLREPin which the first chain of every structure in the PDB was used as a search model was run on a multi-core cluster. This identified a number of prokaryotic phosphate-binding proteins as scoring highly in theMOLREPpeak lists. Calculation of an electron-density map at 1.1 Å resolution based on the solution obtained with PDB entry 2q9t allowed most of the amino acids to be identified visually and built into the model. ABLASTsearch then indicated that the molecule was most probably a phosphate-binding protein fromStenotrophomonas maltophilia(UniProt ID B4SL31; gene ID Smal_2208), and fitting of the corresponding sequence to the atomic resolution map fully corroborated this. Proteins in this family have been linked to the virulence of antibiotic-resistant strains of pathogenic bacteria and with biofilm formation. The structure of theS. maltophiliaprotein has been refined to anRfactor of 10.15% and anRfreeof 12.46% at 1.1 Å resolution. The molecule adopts the type II periplasmic binding protein (PBP) fold with a number of extensively elaborated loop regions. A fully dehydrated phosphate anion is bound tightly between the two domains of the protein and interacts with conserved residues and a number of helix dipoles.
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Taschner, Natalia Pasternak, Ezra Yagil, and Beny Spira. "A differential effect of σ S on the expression of the PHO regulon genes of Escherichia coli." Microbiology 150, no. 9 (September 1, 2004): 2985–92. http://dx.doi.org/10.1099/mic.0.27124-0.

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The RNA polymerase core associated with σ S transcribes many genes related to stress or to the stationary phase. When cells enter a phase of phosphate starvation, the transcription of several genes and operons, collectively known as the PHO regulon, is strongly induced. The promoters of the PHO genes hitherto analysed are recognized by σ D-associated RNA polymerase. A mutation in the gene that encodes σ S, rpoS, significantly increases the level of alkaline phosphatase activity and the overproduction of σ S inhibits it. Other PHO genes such as phoE and ugpB are likewise affected by σ S. In contrast, pstS, which encodes a periplasmic phosphate-binding protein and is a negative regulator of PHO, is stimulated by σ S. The effect of σ S on the PHO genes is at the transcriptional level. It is shown that a cytosine residue at position −13 is important for the positive effect of σ S on pst. The interpretation of these observations is based on the competition between σ S and σ D for the binding to the core RNA polymerase.
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Dissertations / Theses on the topic "Periplasmic phosphate binding protein"

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Anba, Jamila. "Biosynthese et exportation d'une proteine periplasmique, phos, chez escherichia coli k-12." Aix-Marseille 2, 1987. http://www.theses.fr/1987AIX22062.

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La surproduction par escherichia coli de la proteine periplasmique affine pour le phosphate (phos) provoque l'accumulation du precurseur de phos a la fois dans la membrane interne et le cytoplasme. Seul le precurseur membranaire peut etre mature et exporte, alors que le precurseur cytoplasmique subit une coupure lente de sa sequence signal et donne naissance a une forme "pseudo-mature" cytoplasmique. Existence d'un captage entre la synthese et l'exportation. Une application du systeme phos a ete realisee pour la production du facteur de liberation de l'hormone de croissance humaine (hgrf) chez e. Coli. En carence de phosphate, la proteine hybride phos-hgrf est synthetisee et exportee vers le periplasme
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Forward, Jason Andrew. "Mechanism of a novel class periplasmic binding protein dependent solute transport system." Thesis, University of Sheffield, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.389733.

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Robinson, Renee. "A heme periplasmic-binding protein hHBP mediates heme transport in Haemophilus ducreyi." Thesis, University of Ottawa (Canada), 2010. http://hdl.handle.net/10393/28801.

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Haemophilus ducreyi, a Gram-negative and heme-dependent bacterium, is the causative agent of chancroid, a genital ulcer sexually transmitted infection. Although the precise molecular mechanism of heme acquisition in H. ducreyi is unclear, heme uptake likely proceeds via a receptor mediated process. The initial event involves binding to either of two outer membrane receptors, TdhA and HgbA. Once heme is deposited into the periplasmic space, a heme permease is postulated to transport heme across the periplasmic space to the inner membrane. In prior experiments, using protein expression profiling of the H. ducreyi periplasmic proteome, we identified a periplasmic-binding protein hHBP that we propose is a component of a heme trafficking operon. Biochemical and genetic approaches were used to functionally characterize hHBP. First, purified hHBP was incubated with increasing concentrations of heme and the mixtures were resolved by non-denaturing polyacylamide gel electrophoresis. Separated proteins were transferred onto PVDF membranes and heme-protein complexes were detected by enhanced chemiluminescence (ECL). Second, the hhbp gene was cloned in the E. coli recombinant mutant E. coli FB827 dppA::Km mppA::Cm (pAM238-HasR) which expresses the Serratia marcescens HasR heme receptor allowing heme translocaton into the periplasm, but denies heme entry into the cytoplasm because of the presence of the double mutation (dppA::Km mppA::Cm) resulting in a mutant lacking the two periplasmic proteins DppA and MppA. We found that heme binding to hHBP was saturable as determined by ECL. Genetic complementation in trans with hhbp repaired the growth defect of the mutant E. coli for heme utilization as an iron source. The growth restoration was comparable to that seen with the E. coli mutant complemented with the intact Dpp permease. Additionally, growth of the mutant was not rescued with the empty plasmid vector. We concluded that H. ducreyi hHBP functionally binds heme. Complementation of the E. coli mutant for heme competency supports the proposal that hHBP participates in the transit of heme in H. ducreyi.
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St, Denis Melissa. "Identification and characterization of a heme-dedicated periplasmic binding protein in Haemophilus ducreyi." Thesis, University of Ottawa (Canada), 2007. http://hdl.handle.net/10393/27487.

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In Haemophilus ducreyi, heme uptake likely proceeds via a receptor-mediated process. The initial event involves binding to either of two outer membrane receptors, TdhA and HgbA. Once heme is deposited into the periplasmic space, we hypothesize that a heme-dedicated periplasmic binding protein (hHBP) is responsible for transporting heme across the periplasmic space to the inner membrane. To identify the hHBP, periplasmic extracts were generated from H. ducreyi 35000 grown under high and low heme conditions and subjected to proteome mapping. Peptide sequences of upregulated proteins grown under heme-restrictive conditions were determined by mass spectroscopy. A candidate hHBP was identified as a periplasmic binding protein homologous to YfeA of Yersinia pestis. The gene encoding this protein appears to be in a typical ABC transporter operon. Under iron-limiting conditions, no upregulation of the hHBP expression was observed; however, the purified hHBP was shown to specifically bind heme in a concentration-dependent manner.
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Magnusson, Ulrika. "Structural Studies of Binding Proteins: Investigations of Flexibility, Specificity and Stability." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3640.

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Gonzalez, Daniel. "Les "phosphate binding protein" : entre import du phosphate et inhibition de la transcription virale." Thesis, Aix-Marseille, 2014. http://www.theses.fr/2014AIXM4019.

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Les « phosphate binding protein » (PBP) constituent une famille de protéines présentes de manière ubiquitaire chez les bactéries et plus marginalement chez les Eucaryotes. Impliquées dans l'import du phosphate extracellulaire chez les bactéries, les PBPs présentent un site de fixation du phosphate très bien caractérisé avec, notamment, une liaison hydrogène particulière nommée «low barrier hydrogen bond» (LBHB). Cette LBHB est impliquée dans la discrimination entre le phosphate et des anions proches chez les PBPs. Bien que cette discrimination semble nécessiter une haute conservation du site de fixation du phosphate, dans la nature différentes configurations sont observées. Au cours de ce travail, nous nous sommes intéressés à la PBP d'un organisme pathogène, C.perfringens qui présente un site de fixation alternatif. Avec, entre autre, une perte de la LBHB, cette PBP présente la plus faible capacité de discrimination testée à ce jour. Cette faible capacité de discrimination pourrait être liée au biotope de la bactérie ou bien à un phénomène d'adaptation fonctionnelle. D'autre part, certaines PBPs présentent des propriétés d'inhibition du VIH via l'étape de la transcription virale. Cependant, ces protéines sont particulièrement difficiles à produire en système hétérologue limitant l'étude fonctionnelle. Afin de lever ce verrou technique, nous avons développé une nouvelle méthodologie basée sur la phylogénie en vue de solubiliser notre modèle d'étude (HPBP). Nous avons obtenu un variant soluble de HPBP qui conserve ses activités antivirales permettant de débloquer les études fonctionnelles
The "phosphate binding protein" constitutes a family of proteins ubiquitously found in Prokaryotes but also more sparsely distributed in Eukaryotes. Involved in phosphate import, PBPs exhibits a well-characterized phosphate binding site with a peculiar hydrogen bond called "low barrier hydrogen bond" (LBHB). This LBHB is involved in the unique discrimination properties of PBPs, capable of discriminating phosphate from other similar anions such as arsenate of sulfate. Albeit this high discriminating property needs a high conservation of the phosphate binding pocket, different configurations are observed in nature. Herein, we have been interested in a PBP from a human pathogen, Clostridium perfringens, which presents an alternative phosphate binding site. Exhibiting a loss of the LBHB, C.perfringens PBP is the least discriminating PBP isolated so far. This weak discrimination property might be related to the environment of C.perfringens or to a functional adaptation of the PBP. On the other hand, PBPs issued from eukaryotic tissues exhibit HIV inhibition properties via a step not yet targeted in current therapies, i.e. the transcription. However, these proteins are difficult to obtain from human tissues and their expression in heterologous system remains impossible. We have developed a new methodology based on phylogeny in order to solubilise our study model, HPBP. Thus, we have obtained a soluble variant of HPBP which conserves the HIV-inhibiting properties. This unique tool both allow to unlock functional studies and lead to a better understanding on how PBPs are capable of inhibiting HIV
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Oaew, Sukunya. "Engineering the phosphate binding protein for an oxyanion sensor array." Thesis, Imperial College London, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.413382.

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Björkman, A. Joakim. "Structure-function studies of the periplasmic ribose-binding protein, a receptor in bacterial chemotaxis and transport /." Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 1998. http://epsilon.slu.se/avh/1998/91-576-5545-6.gif.

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Loftin, Isabell. "Structural and Biochemical Studies of the Metal Binding Protein CusF and its Role in Escherichia coli Copper Homeostasis." Diss., The University of Arizona, 2008. http://hdl.handle.net/10150/193875.

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Biometals such as copper, cobalt and zinc are essential to life. These transition metals are used as cofactors in many enzymes. Nonetheless, these metals cause deleterious effects if their intracellular concentration exceeds the cells' requirement. Prokaryotic organisms usually employ efflux systems to maintain metals in appropriate intracellular concentrations.The Cus system of Escherichia coli plays a crucial part in the copper homeostasis of the organism. This system is a tetrapartite efflux system, which includes an additional component compared to similar efflux systems. This fourth component is a small periplasmic protein, CusF. CusF is essential for full copper resistance, yet its role within the Cus system has not been characterized. It could potentially serve in the role of a metallochaperone or as a regulator to the Cus system.To gain insight into the molecular mechanism of resistance of this system, I have structurally and biochemically characterized CusF. Using X-ray crystallography I determined the CusF structure. CusF displays a novel fold for a copper binding protein. Through multiple sequence alignment and NMR chemical shift experiments, I proposed a metal binding site in CusF, which I confirmed through determination of the structure of CusF-Ag(I). CusF displays a novel coordination of Ag(I) and Cu(I) through a Met2His motif and a cation-pi interaction between the metal ion and a tryptophan sidechain. Furthermore, I have shown that CusF binds Cu(I) and Ag(I) specifically and tightly.I investigated the role of the tryptophan at the binding site to establish its effect on metal binding and function of CusF. I have shown through competitive binding assays, NMR studies and through collaborative EXAFS studies that the tryptophan plays an essential role in CusF metal handling. The affinity of CusF for Cu(I) is influenced by this residue. Moreover, the tryptophan also caps the binding site such that oxidation of the bound metal as well access to adventitious ligands is prevented. In summary, these findings show that the structure and metal site of CusF are unique and are specifically designed to perform the function of CusF as a metallochaperone to the Cus system.
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Churamani, Dev. "Properties of the nicotinic acid adenine dinucleotide phosphate-binding protein in sea urchin eggs." Thesis, University College London (University of London), 2006. http://discovery.ucl.ac.uk/1444577/.

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Nicotinic acid adenine dinucleotide phosphate (NAADP) has recently emerged as a novel intracellular calcium mobilising messenger in a variety of cells. Whilst increasing evidence suggests that NAADP acts on a distinct binding protein, little is known regarding the biochemical properties of the putative NAADP "receptor". My thesis investigates properties of the NAADP-binding protein in sea urchin eggs. Firstly, I show that NAADP binding to its target protein is inhibited by altering the protein:lipid ratio of soluble sea urchin egg homogenates - an effect prevented and reversed specifically by addition of exogenous phospholipids. These data highlight the importance of the lipid environment in maintenance of NAADP binding to its target protein. In addition, I show that upon binding its ligand, the NAADP-binding protein undergoes an unusual stabilization process that is dependent upon the time the receptor is exposed to its ligand. This property endows the NAADP-binding protein with the extraordinary ability to detect the duration of its activation. Finally I describe the development of a highly sensitive radioreceptor assay (based upon the sea urchin egg NAADP-binding protein) that is capable of detecting low levels of NAADP from cellular extracts. I apply this technique to determine NAADP levels in a variety of extracts prepared from cells under resting and stimulated conditions.
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Books on the topic "Periplasmic phosphate binding protein"

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Ünligil, Uluğ Mete. Protein structure and evolution: A study of the X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I and haemophilus influenzae periplasmic zinc-binding protein 1. 2002.

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Bronner, Felix, and Meinrad Peterlik. Extra- and Intracellular Calcium and Phosphate Regulation: From Basic Research to Clinical Medicine. CRC, 1992.

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Felix, Bronner, and Peterlik Meinrad, eds. Extra- and intracellular calcium and phosphate regulation: From basic research to clinical medicine. Boca Raton: CRC Press, 1992.

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Book chapters on the topic "Periplasmic phosphate binding protein"

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Quiocho, F. A., N. K. Vyas, J. S. Sack, and M. A. Storey. "Periplasmic Binding Proteins: Structures and New Understanding of Protein-Ligand Interactions." In Crystallography in Molecular Biology, 385–94. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5272-3_35.

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Kessler, Ralph J., Duke A. Vaughn, Christian Schäli, and Darrell D. Fanestil. "Phosphorin, A Phosphate-Binding Hydrophobic Protein Isolated from Renal Brush Border Membranes." In Phosphate and Mineral Homeostasis, 83–92. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5206-8_8.

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Króliczewski, Jarosław, and Andrzej Szczepaniak. "Localisation of Apocytochrome b 6 Fused to Expressed Periplasmic Maltose-binding Protein in Escherichia coli." In Photosynthesis: Mechanisms and Effects, 1557–60. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_366.

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Garvis, S. G., G. J. Puzon, and M. E. Konkel. "Cloning, Sequencing, and Expression of a Campylobacter Jejuni Periplasmic Binding Protein (P29) Involved in Histidine Transport." In Advances in Experimental Medicine and Biology, 263–64. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-1828-4_42.

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Sagot, B., G. Alloing, D. Hérouart, D. Le Rudulier, and L. Dupont. "Identification of BetX, a Periplasmic Protein Involved in Binding and Uptake of Proline Betaine and Glycine Betaine in Sinorhizobium meliloti." In Biological Nitrogen Fixation: Towards Poverty Alleviation through Sustainable Agriculture, 265. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-8252-8_101.

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Hunt, Arthur G., and Jen-Shiang Hong. "[24] Reconstitution of periplasmic binding protein-dependent glutamine transport in vesicles." In Methods in Enzymology, 302–9. Elsevier, 1986. http://dx.doi.org/10.1016/s0076-6879(86)25026-0.

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IRIARTE, A., F. ALTIERI, J. DEL SOLAR, J. R. MATTINGLY, and M. MARTINEZ-CARRION. "Lipid Dependency of the Binding of a Mitochondrial Precursor Protein to Model Membranes." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors, 527–29. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50109-6.

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Boos, Winfried. "[4] Binding protein-dependent ABC transport system for glycerol 3-phosphate of Escherichia coli." In Methods in Enzymology, 40–51. Elsevier, 1998. http://dx.doi.org/10.1016/s0076-6879(98)92006-7.

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Brass, Johann M. "[23] Calcium-induced permeabilization of the outer membrane: A method for reconstitution of periplasmic binding protein-dependent transport systems in Escherichia coli and Salmonella typhimurium." In Methods in Enzymology, 289–302. Elsevier, 1986. http://dx.doi.org/10.1016/s0076-6879(86)25025-9.

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Johnson, Jason L., and Gregory D. Reinhart. "Effects of High Pressure on the Allosteric Properties of Phosphofructokinase from Escherlchia coli." In High Pressure Effects in Molecular Biophysics and Enzymology. Oxford University Press, 1996. http://dx.doi.org/10.1093/oso/9780195097221.003.0019.

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Phosphofructokinase (PFK) from Escherichia coli is subject to allosteric regulation by phosphoenolpyruvate (PEP) and MgADP. These ligands inhibit and activate, respectively, by binding to a single allosteric binding domain and thereby altering the affinity the enzyme displays for its substrate, fructose-6-phosphate (Fru-6-P). The effect of hydrostatic pressure of up to 1.4 kbar on the binding of each of these ligands to PFK has been evaluated. This pressure range is insufficient to cause significant dissociation of the PFK tetramers. However, the logarithm of the equilibrium constant for each ligand binding to free enzyme decreases in a linear manner, and to virtually the same extent, when pressure is increased from 1 to 700 bar. Consequently, the ΔV associated with the binding of the inhibitor ligand PEP is virtually identical to the ΔV for the binding of the activator ligand MgADP or the substrate Fru-6-P, which falls within the range of 40–45 ml mol−1. The apparent ΔV for Fru-6-P binding decreases with increasing concentration of PEP until it is equal to +18 ml mol when PEP is fully saturating. Similarly, ΔV for Fru-6-P binding decreases to +26 ml mol−1 when MgADP is fully saturating. These data are interpreted as implying that both PEP and MgADP improve the “fit” of Fru-6-P to its binding domain despite the fact that the ligands have opposing effects on Fru-6-P binding affinity. Phosphofructokinase (PFK) from E. coli is a prototypical allosteric enzyme which was one of the first to be studied in depth (Blangy & Buc, 1967; Blangy et al., 1968) after Monod et al. (1965) published their famous proposal that allosteric behavior results from the concerted transition between discrete functional states of a protein (the MWC two-state model). PFK from E. coli is a tetrameric enzyme with a single allosteric binding domain that can bind either the activator MgADP or the inhibitor PEP. Under many circumstances the substrate, fructose 6-phosphate (Fru-6-P), binds to the enzyme with positive cooperativity, and the affinity and cooperativity that Fru-6-P exhibits is modulated by the allosteric ligands in classic K-type fashion.
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Conference papers on the topic "Periplasmic phosphate binding protein"

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Peterson, C. B., C. M. Noyes, J. M. Pecon, F. C. Church, and M. N. Blackburn. "LYSINE-125 IS ESSENTIAL FOR HEPARIN BINDING TO ANTITHROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643769.

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Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent, pyridoxal-5'-phosphate. Modification of antithrombin (AT) with limiting amounts of reagent yields an average incorporation of the phos-phopyridoxyl label into one lysine per protein molecule. Fractionation of the labeled AT by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated AT species devoid of heparin binding (Pool I) from modified protein which retained affinity for heparin (Pool II). Pool I contained an average of 1.6 mol phosphopyridoxyl label per mol AT, whereas Pool II was labeled to a lesser extent, with a ratio of 1.0 mol phosphopyridoxyl per mol protein. To generate peptide maps of the two AT species, the proteins were reductively denatured, S-carboxymethylated, and digested with trypsin. Fractionation of the tryptic digests by reverse-phase HPLC indicated one peak in the chromatogram of the non-heparin-binding species to be clearly different when compared to the chromatogram of the heparin-binding species. Upon sequencing of the unique peptide by automated Edman degradation, the modified residue was identified as Lys-125 in the primary sequence of AT. Additionally, AT was reacted with pyridoxal-5 ′-phosphate in the presence of added heparin for comparison with protein modified in the absence of heparin. Overall incorporation of the phosphopyridoxyl label was 3-4 mol reagent per mol protein, without inclusion of heparin during the modification reaction, and only 2-3 mol pyridoxyl per mol protein with heparin added. Tryptic peptide maps of these two modified ATs indicated that eight lysine residues are "protected" from modification by addition of heparin. The "protected" lysines identified, in addition to the essential Lys-125, are residues 11, 39, 133, 136, 257, 275, and 287. Identification of Lys-125 as the critical lysine for heparin binding strongly supports previous data which indicates that the heparin-binding domain of AT is located at the N-termi-nus within one of the disulfide cross-linked loops of the protein.
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PEERSCHKE, E. IB, and B. Ghebrehiwet. "CHARACTERIZATION OF HUMAN PLATELET ClQ BINDING SITES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643503.

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We have recently shown that platelets possess specific binding sites for Clq, a subcomponent of the first component of complement, Cl, and that occupancy of these receptor sites correlates with the previously described inhibitory effect of Clq on collagen-induced platelet aggregation. To further characterize platelet Clq receptors, washed platelets were solubilized in 5 mM sodium phosphate buffer, pH 7.5 containing 10 mM EDTA, 150 mM NaCl, 10 mM EACA, 0.5 mM PMSF, and 1% Triton X-100. After dialysis against 5 mM phosphate buffer pH 7.5 containing 10 mM EDTA, 20 mM NaCl, 10 mM EACA,0.5 mM PMSF and 0.1% Triton X-100, the lysate was passed over Clq-Sepharose-4B affinity columns. A single protein peak eluted with buffer containing 300 mM NaCl. This peak was composed of two predominant molecular weight species (85-95K, 60-66K) as assessed by SDS-polyacrylamide gel electrophoresis under non-reducing conditions. When 125-iodine surface labeled platelets were solubilized and applied to Clq-Sepharose affinity resins, the same two molecular weight species eluted and could be visualized by autoradiography following SDS-polyacrylamide gel electrophoresis. Immunoabsorption studies performed under nondenaturing conditions using protein A and the IIl/Dl monoclonal antibody, which binds specifically to platelets and inhibits platelet-Clq interactions, revealed that the 85-95K molecular weight component was preferentially absorbed, but incomplete immunoabsorption of the 60-66K molecular weight constituent was also noted. Affinity purified Clq binding sites sedimented as a single peak during 5-40% sucrose density ultracentrifugation with an S value of approximately 2.4. In addition, both the 85-95K and the 60-66K molecular weight species coeluted in the void volume of Sephadex G-100 columns. The data suggest that the 85-95K and 60-66K molecular weight species represent platelet membrane Clq binding sites, and that these sites may form weak, noncovalently associated complexes.
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Jakobs, K. H., P. Gierschik, and R. Grandt. "THE ROLE OF GTP-BINDING PROTEINS EXHIBITING GTPase ACTIVITY IN PLATELET ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644773.

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Activation of platelets by agonists acting via cell surface-located receptors apparently involves as an early event in transmembrane signalling an interaction of the agonist-occupied receptor with a guanine nucleotide-binding regulatory protein (G-protein). The activated G-protein, then, transduces the information to the effector molecule, being responsible for the changes in intracellular second messengers. At least two changes in intracellular signal molecules are often found to be associated with platelet activation by agonists, i.e., increases in inositol trisphosphate and diacylglycerol levels caused by activation of a polyphosphoinositide-specific phospholipase C and decrease in cyclic AMP concentration caused by inhibition of adenylate cyclase.Both actions of platelet-activating agents apparently involve G-proteins as transducing elements. Generally, the function of a G-protein in signal transduction can be measured either by its ability to regulate the activity of the effector molecule (phospholipase C or adenylate cyclase) or the binding affinity of an agonist to its specific receptor or by the abitlity of the G-protein to bind and hydrolyze GTP or one of its analogs in response to agonist-activated receptors. Some platelet-activating agonists (e.g. thrombin) can cause both adenylate cyclase inhibition and phospholipase C activation, whereas others induce either inhibition of adenylate cyclase (e.g. α2-adrenoceptor agonists) or activation of phospholipase C (e.g. stable endoperoxide analogs) . It is not yet known whether the simultaneous activation of two signal transduction systems is due to activation of two separate G-proteins by one receptor, to two distinct receptors activating each a distinct G-protein or to activation of two effector molecules by one G-protein.For some of the G-proteins, rather specific compounds are available causing inactivation of their function. In comparison to Gs, the stimulatory G-protein of the adenylate cyclase system, the adenylate cyclase inhibitory Gi-protein is rather specifically inactivated by ADP-ribosylation of its a-subunit by pertussis toxin, “unfortunately” not acting in intact platelets, and by SH-group reactive agents such as N-ethylmaleimide and diamide, apparently also affecting the Giα-subunit. Both of these treatments completely block α2-adrenoceptor-induced GTPase stimulation and adenylate cyclase inhibition and also thrombin-induced inhibition of adenylate cyclase. In order to know whether the G-protein coupling receptors to phospholipase C is similar to or different from the Gi-protein, high affinity GTPase stimulation by agents known to activate phospholipase C was evaluated in platelet membranes. The data obtained indicated that GTPase stimulation by agents causing both adenylate cyclase inhibition and phospholipase C activation is reduced, but only partially, by the above mentioned Gi-inactivating agents, while stimulation of GTPase by agents stimulating only phospholipase C is not affected by these treatments. These data suggested that the G-protein regulating phospholipase C activity in platelet membranes is different from the Gi-protein and may also not be a substrate for pertussis toxin. Measuring thrombin stimulation of inositol phosphate and diacylglycerol formation in saponin-permeabilized platelets, apparently contradictory data were reported after pertussis toxin treatment, being without effect or causing even an increase in thrombin stimulation of inositol phosphate formation (Lapetina: BBA 884, 219, 1986) or being inhibitory to thrombin stimulation of diacylglycerol formation (Brass et al.: JBC 261, 16838, 1986). These data indicate that the nature of the phospholipase C-related G-protein(s) is not yet defined and that their elucidation requires more specific tools as well as purification and reconstitution experiments. Preliminary data suggest that some antibiotics may serve as useful tools to characterize the phospho-lipase-related G-proteins. The possible role of G-protein phosphorylation by intracellular signal molecule-activated protein kinases in attenuation of signal transduction in platelets will be discussed.
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Church, F. C., R. E. Treanor, and H. C. Whinna. "ACTIVATION OF HEPARIN COFACTOR II BY PHOSVITIN, A PHOSPHOGLYCO-PROTEIN, AND OTHER PHOSPHATE-CONTAINING POLYANIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643867.

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We are characterizing the specificity of the polyanion-binding domain of the heparin/dermatan sulfate-dependent plasma protease inhibitor, heparin cofactor II (HCII). Various phosphate-containing polyanions accelerate the HCII-catalyzed inhibition of thrombin (T). Phosvitin, a phosphoprotein, enhances the HCII/T reaction at 25°C and pH 8.0 with the apparent second-order rate constant value (K2) increasing from 5 × 104 M−1 min−1 (in the absence of phosvitin) to 8 x 10' M”1 min as phosvitin increased from 0.05 to 30 ug/ml and then decreases as phosvitin is increased above 30 ug/ml. Apparent dissociation constant values for phosvitin-HCII and phosvitin-T are 450 nM and 10 nM, respectively. Polynucleotides accelerate the HCII/T reaction and have the following specificity (concentrations examined from 1-200 ug/ml): poly(guanylic acid) >> poly(adeny-lic acid, guanylic acid) > poly(inosinic acid) > poly(guanylic acid, uridylic acid) > poly(uridylic acid) = poly(adenylic acid) > poly(cytidylic acid). Polyphosphate anions (phosphate chain length, n, ranging from 5-100) enhance the HCII/T reaction. When compared at an equimolar phosphate concentration (1 mM), the rate was saturated at n = 50 with a maximum V.2 of about 5 × 107 M−1 min−1. Ca2+ (or Mg2+)-phosvitin/polyphosphate anion complexes and salmon protamine-polynucleotide complexes have lost the ability to enhance the HCII/T reaction. Phospho-pyridoxylated-HCII (lysine modified), with greatly reduced heparin cofactor activity, has lost its accelerating effect with phosvitin, polynucleotides and the polyphosphate anions. None of the above mentioned polyphosphate-containing compounds are effective at accelerating either the HCII-catalyzed inhibition of chymotrypsin or the antithrombin Ill-catalyzed T reaction. Our results suggest that (i) HCII is activated by the multiple negative charges of phosphate polyanions but they alone are not sufficient; (ii) the effective phosphate polyanions must also possess a specific conformation for maximum activity; and (iii) the phosphoserine-containing protein, phosvitin, can serve as a "template" for HCII/T.
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Bago, Ruzica, Eeva Sommer, Nazma Malik, Michael J. Munson, Alan R. Prescott, Paul Davies, Shpiro Natalia, Ian G. Ganley, and Dario R. Alessi. "Abstract A04: Characterization of VPS34-IN1, a specific inhibitor of Vps34 reveals that the phosphatidylinositol 3-phosphate binding SGK3 protein kinase is regulated by class III PI-3 kinase." In Abstracts: AACR Special Conference: Targeting the PI3K-mTOR Network in Cancer; September 14-17, 2014; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-8514.pi3k14-a04.

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Asaji, T., E. Murakami, N. Takekoshi, S. Matsui, and T. Imaoka. "EFFECT OF ATRIAL NATRIURETIC POLYPEPTIDES ON PLATELET FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644872.

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Atrial natriuretic polypeptides (ANP) have been shown to possess a potent diuretic and natriuretic activity, and medicated to patients with heart insufficiency as a drug to be mediated by cGMPaccumulation in glomeruli. A existence of receptors for ANP have recently beenreported in human platelet. But, whether ANP has a direct effect on platelet function remains to be known.Single stimulation of ANP in any concentration did not induce aggregation in neither platelet rich plasma, nor washed platelets. Also no effect of pretreatment with ANP was observed against aggregation triggered by known mediators of platelet activation (Thrombin, ADP, Epinephrine, Collagen) using platelet rich plasma and washed platelets.Therefore, biochemical parameters such as cyclic nucleotides (cAMP, cGMP), phosphatidylinositol hydrolysis and protein phosphorylation, leading to the early stage of platelet activation were examined to investigate the effect of ANP in receptor linked transducing mechanism. Neither cyclic nucleotides accumulation nor [32 P] phosphatidic acid production were detected in platelets treated with ANP. ANP caused a small increase of 32P incorporation into M 30K protein, but no change on the level of phosphorylation of 47K, 20K protein (Imaoka, T. and Haslam, R.J., J.Biol.Chem.258,11404, 1983) was observed.These results clearly suggested thatANP binding with membrane receptor was not linked with adenylate cyclase, ganulate cyclase and phosphatidylinositol phosphate turnover in human platelet, maybe because of too few numbers of ANP receptor. Mechanism of 30K protein phosphorylation and Ca++ mobilization are important subjects for future study, (supported by MESC of Japan)
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Moake, J. L., M. A. Harris, C. E. Whitley, and C. P. Alfrey. "RAPID, SENSITIVE N0N-RADI0ACTIVE QUANTIFICATION AND ANALYSIS OF PLASMA VON WILLEBRAND FACTOR (vWF) MULTIMERS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644085.

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Assessment of plasma vWF abnormalities by clinical coagulation laboratories is difficult because the available test systems for vWF antigen quantification and multimer analysis are expensive, laborious, and require days, radioactive anti-vWF antibodies and autoradiographic methods. We have devised simple, rapid, sensitive alternative techniques for vWF quantification and multimer analysis that can be readily installed in clinical laboratories. Plasma vWF antigen quantification is by a 2 hour enzyme immunoassay that accurately detects levels as low as 0.23% of normal. Plasma vWF to be quantified is bound to polyclonal monospecific antihuman vWF attached to small glass beads, and anti-human vWF conjugated with alkaline phosphatase is added to make an insoluble "sandwich." A substrate solution consisting of phenylphosphate and 4-amino-antipurine is added, followed by potassium ferricyanide. Optical density (at 490-510 nm) of the red color that develops is directly proportional to the plasma concentration of vWF antigen. Plasma vWF multimeric analysis is by a one-day electrophoretic immunobiot procedure. Plasma vWF multimer forms are solubilized in SDS-urea-Tris-EDTA, separated by horizontal 1% agarose gel electrophoresis, and transferred to a cationic membrane. Other protein binding sites on the membrane are blocked with milk proteins, and the membrane is overlaid with anti-vWF IgG linked to alkaline phosphatase. vWF multimers are then displayed as blue bands by soaking the membrane in an alkaline solution of the histochemical stain, fast blue RR (commonly used for leukocyte alkaline phosphatase scoring) dissolved in naphtol AS-MX phosphate. These simple, non-radioactive procedures performed together permit the rapid distinction of classical (Type I) von Willebrand's disease (vWD), characterized by low vWF antigen and normal multimers, from the Type II vWD syndromes, characterized by a relative deficiency of the largest plasma vWF forms. Unusually large vWF multimers, present in remission plasma of patients with chronic relapsing thrombotic thrombocytopenic purpura (TTP), are also easily detected using this rapid system of multimer analysis.
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Wang, Chong, Silvia D. Gonzales, Weiyong Gu, and C. Y. Charles Huang. "Accumulation of Extracellular ATP in Porcine Nucleus Pulposus." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80671.

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There are many reasons for people to miss work; one of the leading contributors is low back pain (LBP), which is believed to affect 80% of the population at some point during their lifetime. Suffering from back pain is the chief complaint of 5% of people who visit the doctor in the US [1]. The total medical cost related to low back pain in the US exceeds 100 billion dollars every year [2]. The cause of LBP is still unclear. However, recent studies revealed that intervertebral disc (IVD) degeneration is closely related to LBP [3]. IVD transfers loads and allows the spine to move through torsion, bending or compression [4–6]. There are two main anatomic regions in IVD: nucleus pulposus (NP) and annulus fibrosis (AF). The loss of notochordal cells in the NP region has been associated with the initiation of disc degeneration [7]. Our recent studies demonstrated that the adenosine triphosphate (ATP) production of notochordal NP cells was much higher than that of the AF cells while mechanical loading promoted ATP release from IVD cells [8]. Extracellular ATP (eATP) is a powerful signaling molecule that can mediate a wide variety of biological responses, such as cell metabolism, survival, and growth by binding to the purinergic receptors: G protein coupled receptor (P2Y) or ligand-gated ionotropic receptor (P2X) [9]. In addition, eATP is often rapidly hydrolyzed by several families of ectonucleotidases [10–12]. The by-products of eATP hydrolysis include inorganic pyrophosphate (PPi) and phosphate (Pi) which are closely related to mineral crystal formation and tissue calcification [12–15]. PPi and Pi released from eATP hydrolysis may contribute to endplate calcification which has been associated with disc degeneration. However, eATP accumulation in the IVD has not been studied yet. Therefore, the objective of this study was to investigate the accumulative level of eATP in the NP region of porcine IVD using a novel optical ATP sensor.
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