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[PMID]:28886080
[Au] Autor:Curtis PD
[Ad] Endereço:Department of Biology, University of Mississippi, University, MS, United States of America.
[Ti] Título:Stalk formation of Brevundimonas and how it compares to Caulobacter crescentus.
[So] Source:PLoS One;12(9):e0184063, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Caulobacter crescentus cell extension known as a stalk represents an unusual bacterial morphology. C. crescentus produces stalks under multiple nutrient conditions, but the length of the stalk is increased in response to phosphate starvation. However, the exact function of the stalk is not known, nor is it known how much stalk biogenesis or function is conserved with other stalked bacteria. Work presented here shows that many organisms in the Caulobacter genus and the next closest genus (Brevundimonas) generally do not synthesize stalks in the relatively-rich PYE growth medium, suggesting that the synthesis of a stalk under nutrient-rich conditions by C. crescentus may be the exception instead of the norm among its phylogenetic group. Brevundimonas subvibrioides can be induced to synthesize stalks by genetically mimicking phosphate starvation conditions, indicating stalk synthesis in this organism may be performed on an as-need basis. This mutation, however, does not appear to increase the incidence of holdfast synthesis. While B. subvibrioides stalks appear to be synthesized with the same polarity with respect to holdfast as C. crescentus stalks, evidence is presented that suggests B. subvibrioides may disassemble stalks when they are no longer needed. Many homologs of C. crescentus genes encoding stalk-associated proteins are absent in the B. subvibrioides genome, and B. subvibrioides PstA-GFP as well as C. crescentus StpX-GFP are able to enter the B. subvibrioides stalk compartment, calling into question the level of compartmentalization of the B. subvibrioides stalk. In summary, this work begins to address how much the C. crescentus model for this unusual morphological adaptation can be extended to related organisms.
[Mh] Termos MeSH primário: Alphaproteobacteria/ultraestrutura
Caulobacter crescentus/ultraestrutura
[Mh] Termos MeSH secundário: Alphaproteobacteria/fisiologia
Caulobacter crescentus/fisiologia
Evolução Molecular
Deleção de Genes
Mutação
Fenômenos Fisiológicos da Nutrição
Proteínas de Ligação a Fosfato/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphate-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184063


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[PMID]:28542513
[Au] Autor:Pegos VR; Santos RML; Medrano FJ; Balan A
[Ad] Endereço:Universidade Estadual de Campinas - UNICAMP, Instituto de Biologia (IB), Campinas, São Paulo, Brazil.
[Ti] Título:Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri.
[So] Source:PLoS One;12(5):e0178162, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Escherichia coli, the ATP-Binding Cassette transporter for phosphate is encoded by the pstSCAB operon. PstS is the periplasmic component responsible for affinity and specificity of the system and has also been related to a regulatory role and chemotaxis during depletion of phosphate. Xanthomonas citri has two phosphate-binding proteins: PstS and PhoX, which are differentially expressed under phosphate limitation. In this work, we focused on PhoX characterization and comparison with PstS. The PhoX three-dimensional structure was solved in a closed conformation with a phosphate engulfed in the binding site pocket between two domains. Comparison between PhoX and PstS revealed that they originated from gene duplication, but despite their similarities they show significant differences in the region that interacts with the permeases.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Regulação Bacteriana da Expressão Gênica
Proteínas de Ligação a Fosfato/química
Regulon/genética
Xanthomonas/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Cristalografia por Raios X
Proteínas de Ligação a Fosfato/genética
Proteínas de Ligação a Fosfato/metabolismo
Fosfatos/metabolismo
Conformação Proteica
Alinhamento de Sequência
Xanthomonas/crescimento & desenvolvimento
Xanthomonas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Phosphate-Binding Proteins); 0 (Phosphates)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178162


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[PMID]:27710929
[Au] Autor:Hatti K; Gulati A; Srinivasan N; Murthy MR
[Ad] Endereço:Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, Karnataka 560 012, India.
[Ti] Título:Determination of crystal structures of proteins of unknown identity using a marathon molecular replacement procedure: structure of Stenotrophomonas maltophilia phosphate-binding protein.
[So] Source:Acta Crystallogr D Struct Biol;72(Pt 10):1081-1089, 2016 10 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During the past decade, the authors have collected a few X-ray diffraction data sets from protein crystals that appeared to be easy cases of molecular replacement but failed to yield structures even after extensive trials. Here, the use of a large-scale molecular replacement method that explores all structurally characterized domains as phasing models to determine the structure corresponding to two data sets collected at 1.9 and 2.3 Šresolution is reported. These two structures were of the same protein independently crystallized in 2007 and 2011. The structures derived are virtually identical and were found to consist of two compact globular domains connected by a hinge. The high resolution of one of these data sets enabled inference of the amino-acid sequence from the electron-density map. The deduced sequence is nearly identical to that of a protein from the multidrug-resistant bacterium Stenotrophomonas maltophilia. Although the structure of this protein has not been determined previously, it is homologous to the well studied DING proteins which mediate the cellular uptake of phosphate ions. The final electron-density maps from both of the data sets revealed a large density at the interface of the two globular domains that is likely to represent a phosphate ion. Thus, the structure is likely to be that of a phosphate-binding protein encoded by the S. maltophilia genome (SmPBP; PDB entry 5j1d). The nature of the phosphate-binding site of SmPBP closely resembles that of Pseudomonas fluorescens DING (PfluDING), which displays remarkable discrimination between the closely similar phosphate and arsenate ions. The results presented here illustrate that routine crystallization trials may occasionally lead to the serendipitous crystallization of a protein of unknown identity and brute-force molecular replacement through `fold space' might allow the identification of the unknown protein.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Cristalografia por Raios X/métodos
Proteínas de Ligação a Fosfato/química
Stenotrophomonas maltophilia/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Infecções por Bactérias Gram-Negativas/microbiologia
Modelos Moleculares
Conformação Proteica
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Phosphate-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161007
[St] Status:MEDLINE


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[PMID]:27487824
[Au] Autor:Keegan R; Waterman DG; Hopper DJ; Coates L; Taylor G; Guo J; Coker AR; Erskine PT; Wood SP; Cooper JB
[Ad] Endereço:STFC, Rutherford Appleton Laboratory, Harwell Oxford, Didcot OX11 0FA, England.
[Ti] Título:The 1.1 Šresolution structure of a periplasmic phosphate-binding protein from Stenotrophomonas maltophilia: a crystallization contaminant identified by molecular replacement using the entire Protein Data Bank.
[So] Source:Acta Crystallogr D Struct Biol;72(Pt 8):933-43, 2016 08.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During efforts to crystallize the enzyme 2,4-dihydroxyacetophenone dioxygenase (DAD) from Alcaligenes sp. 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 Šresolution 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 using MOLREP in 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 the MOLREP peak lists. Calculation of an electron-density map at 1.1 Šresolution based on the solution obtained with PDB entry 2q9t allowed most of the amino acids to be identified visually and built into the model. A BLAST search then indicated that the molecule was most probably a phosphate-binding protein from Stenotrophomonas 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 the S. maltophilia protein has been refined to an R factor of 10.15% and an Rfree of 12.46% at 1.1 Šresolution. 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.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Ligação a Fosfato/química
Stenotrophomonas maltophilia/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Cristalização
Cristalografia por Raios X
Bases de Dados de Proteínas
Infecções por Bactérias Gram-Negativas/microbiologia
Seres Humanos
Modelos Moleculares
Conformação Proteica
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Phosphate-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160805
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798316010433


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[PMID]:27479950
[Au] Autor:Yuen NK; Ananthakrishnan S; Campbell MJ
[Ad] Endereço:Surgical Resident at the University of California, Davis in Sacramento. nkyuen@ucdavis.edu.
[Ti] Título:Hyperparathyroidism of Renal Disease.
[So] Source:Perm J;20(3):78-83, 2016.
[Is] ISSN:1552-5775
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Renal hyperparathyroidism (rHPT) is a common complication of chronic kidney disease characterized by elevated parathyroid hormone levels secondary to derangements in the homeostasis of calcium, phosphate, and vitamin D. Patients with rHPT experience increased rates of cardiovascular problems and bone disease. The Kidney Disease: Improving Global Outcomes guidelines recommend that screening and management of rHPT be initiated for all patients with chronic kidney disease stage 3 (estimated glomerular filtration rate, < 60 mL/min/1.73 m(2)). Since the 1990s, improving medical management with vitamin D analogs, phosphate binders, and calcimimetic drugs has expanded the treatment options for patients with rHPT, but some patients still require a parathyroidectomy to mitigate the sequelae of this challenging disease.
[Mh] Termos MeSH primário: Hiperparatireoidismo
Falência Renal Crônica
[Mh] Termos MeSH secundário: California
Tomada de Decisões
Seres Humanos
Hiperparatireoidismo/diagnóstico
Hiperparatireoidismo/dietoterapia
Hiperparatireoidismo/tratamento farmacológico
Hiperparatireoidismo/fisiopatologia
Proteínas de Ligação a Fosfato/uso terapêutico
Vitamina D/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Phosphate-Binding Proteins); 1406-16-2 (Vitamin D)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE
[do] DOI:10.7812/TPP/15-127


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[PMID]:27426274
[Au] Autor:Ito T; Yamauchi A; Hemmi H; Yoshimura T
[Ad] Endereço:Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furou-chou, Chikusa, Nagoya, Aichi 464-8601, Japan. Electronic address: ito-t@agr.nagoya-u.ac.jp.
[Ti] Título:Ophthalmic acid accumulation in an Escherichia coli mutant lacking the conserved pyridoxal 5'-phosphate-binding protein YggS.
[So] Source:J Biosci Bioeng;122(6):689-693, 2016 Dec.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Escherichia coli YggS is a highly conserved pyridoxal 5'-phosphate (PLP)-binding protein whose biochemical function is currently unknown. A previous study with a yggS-deficient E. coli strain (ΔyggS) demonstrated that YggS controls l-Ile- and l-Val-metabolism by modulating 2-ketobutyrate (2-KB), l-2-aminobutyrate (l-2-AB), and/or coenzyme A (CoA) availability in a PLP-dependent fashion. In this study, we found that ΔyggS accumulates an unknown metabolite as judged by amino acid analyses. LC/MS and MS/MS analyses of the compound with propyl chloroformate derivatization, and co-chromatography analysis identified this compound as γ-l-glutamyl-l-2-aminobutyryl-glycine (ophthalmic acid), a glutathione (GSH) analogue in which the l-Cys moiety is replaced by l-2-AB. We also determine the metabolic consequence of the yggS mutation. Absence of YggS initially increases l-2-AB availability, and then causes ophthalmic acid accumulation and CoA limitation in the cell. The expression of a γ-glutamylcysteine synthetase and a glutathione synthetase in a ΔyggS background causes high-level accumulation of ophthalmic acid in the cells (∼1.2 nmol/mg cells) in a minimal synthetic medium. This opens the possibility of a first fermentative production of ophthalmic acid.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
Proteínas de Escherichia coli/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Deleção de Genes
Oligopeptídeos/biossíntese
[Mh] Termos MeSH secundário: Proteínas de Transporte/metabolismo
Coenzima A/metabolismo
Sequência Conservada
Dipeptídeos/genética
Dipeptídeos/metabolismo
Proteínas de Escherichia coli/metabolismo
Glutamato-Cisteína Ligase/genética
Glutamato-Cisteína Ligase/metabolismo
Glutationa Sintase/genética
Glutationa Sintase/metabolismo
Organismos Geneticamente Modificados
Proteínas de Ligação a Fosfato/genética
Proteínas de Ligação a Fosfato/metabolismo
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Dipeptides); 0 (Escherichia coli Proteins); 0 (Oligopeptides); 0 (Phosphate-Binding Proteins); 0 (YggS protein, E coli); 3A60475Q1Q (ophthalmic acid); EC 6.3.2.2 (Glutamate-Cysteine Ligase); EC 6.3.2.3 (Glutathione Synthase); M984VJS48P (gamma-glutamylcysteine); SAA04E81UX (Coenzyme A)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160719
[St] Status:MEDLINE


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[PMID]:26729302
[Au] Autor:Sekercioglu N; Busse JW; Mustafa RA; Guyatt GH; Thabane L
[Ad] Endereço:Department of Clinical Epidemiology and Biostatistics, McMaster University, 1280 Main Street West, Hamilton, Ontario, L8S 4K1, Canada. sekercn@mcmaster.ca.
[Ti] Título:Cinacalcet versus standard treatment for chronic kidney disease: a protocol for a systematic review and meta-analysis.
[So] Source:Syst Rev;5:2, 2016 Jan 04.
[Is] ISSN:2046-4053
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Chronic kidney disease-mineral and bone disorders (CKD-MBD) have been associated with poor health outcomes, including diminished quality and length of life. Standard management for CKD-MBD includes phosphate-restricted diet, active vitamin D, vitamin D analogs, and phosphate binders. Persistently elevated parathyroid hormone (PTH) levels may require the addition of Cinacalcet hydrochloride (cinacalcet) which sensitizes calcium receptors on the parathyroid glands. The objective of this systematic review is to compare the effect of cinacalcet versus standard treatment in patients with CKD-MBD. METHODS/DESIGN: Data sources will include MEDLINE, EMBASE, the Cochrane Register of Controlled Trials, and Web of Science from 1996 to June 2015. Teams of two reviewers will, independently and in duplicate, screen titles and abstracts and potentially eligible full text reports to determine eligibility, and subsequently abstract data and assess risk of bias in eligible trials. We will calculate the effect estimates (risk ratios or mean differences) and 95 % confidence intervals, as well as statistical measures of variability in results across studies using random effect models for patient-important and intermediate outcomes. We will use the GRADE (Grading of Recommendations, Assessment, Development and Evaluation) approach to rate the quality of evidence about estimates of effect on an outcome-by-outcome basis. We will present our results with a GRADE summary table. DISCUSSION: Our review will explore the effect of cinacalcet versus standard treatment in patients with CKD-MBD. The results of this systematic review will help guide management of this patient population, and identify targets for future research. SYSTEMATIC REVIEW REGISTRATION: PROSPERO CRD42015020318 http://www.crd.york.ac.uk/PROSPERO/display_record.asp?ID=CRD42015020318.
[Mh] Termos MeSH primário: Cloridrato de Cinacalcete/uso terapêutico
Insuficiência Renal Crônica/terapia
[Mh] Termos MeSH secundário: Calcimiméticos/uso terapêutico
Dieta/métodos
Seres Humanos
Hormônio Paratireóideo/uso terapêutico
Proteínas de Ligação a Fosfato/uso terapêutico
Insuficiência Renal Crônica/tratamento farmacológico
Resultado do Tratamento
Vitamina D/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS; REVIEW
[Nm] Nome de substância:
0 (Calcimimetic Agents); 0 (Parathyroid Hormone); 0 (Phosphate-Binding Proteins); 1406-16-2 (Vitamin D); 1K860WSG25 (Cinacalcet Hydrochloride)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160106
[St] Status:MEDLINE
[do] DOI:10.1186/s13643-015-0177-1


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[PMID]:26522011
[Au] Autor:Lin X; Ding H; Zeng Q
[Ad] Endereço:Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
[Ti] Título:Transcriptomic response during phage infection of a marine cyanobacterium under phosphorus-limited conditions.
[So] Source:Environ Microbiol;18(2):450-60, 2016 Feb.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The transcriptomic responses of bacteria to environmental stresses have been studied extensively, yet we know little about how the stressed cells respond to bacteriophage infection. Here, we conducted the first whole transcriptome sequencing (RNA-seq) study of stressed bacteria to phage infection by infecting the marine picocyanobacterium Prochlorococcus NATL2A with cyanomyovirus P-SSM2 under P limitation, a strong selective force in the oceans. Transcripts of the P-acquisition genes in the uninfected cells were enriched after P limitation, including the high-affinity phosphate-binding protein gene pstS. They were still enriched in the infected cells under P-limited conditions. In contrast, transcripts of adenosine triphosphate (ATP) synthase and ribosomal protein genes were depleted in the uninfected cells after P limitation but were enriched during phage infection of P-starved cells. Cyanophage P-SSM2 contains pstS, and pstS and its adjacent gene g247 of unknown function were the only phage genes that were enriched under P-limited conditions. We further found that the host pstS transcript number per cell decreased after infection, however, it was still much higher in the P-limited infected cells than that in the nutrient-replete cells. Moreover, phage pstS transcript number per cell was ∼ 20 times higher than the host copy, which may help maintain the host phosphate uptake rate during infection.
[Mh] Termos MeSH primário: Bacteriófagos/genética
Fósforo/deficiência
Prochlorococcus/genética
Prochlorococcus/virologia
Estresse Fisiológico/genética
Transcriptoma
Microbiologia da Água
[Mh] Termos MeSH secundário: Sequência de Bases
DNA Bacteriano/genética
Perfilação da Expressão Gênica
ATPases Mitocondriais Próton-Translocadoras/genética
Dados de Sequência Molecular
Oceanos e Mares
Proteínas de Ligação a Fosfato/genética
Fosfatos/deficiência
Prochlorococcus/metabolismo
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Phosphate-Binding Proteins); 0 (Phosphates); 27YLU75U4W (Phosphorus); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151103
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.13104


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[PMID]:26508681
[Au] Autor:Sherman RA
[Ad] Endereço:Division of Nephrology, Department of Medicine, Rutgers Robert Wood Johnson Medical School, New Brunswick, NJ. Electronic address: sherman@rwjms.rutgers.edu.
[Ti] Título:Hyperphosphatemia in Dialysis Patients: Beyond Nonadherence to Diet and Binders.
[So] Source:Am J Kidney Dis;67(2):182-6, 2016 Feb.
[Is] ISSN:1523-6838
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hyperphosphatemia in dialysis patients is routinely attributed to nonadherence to diet, prescribed phosphate binders, or both. The role of individual patient variability in other determinants of phosphate control is not widely recognized. In a manner that cannot be explained by dialysis parameters or serum phosphate levels, dialytic removal of phosphate may vary by >400mg per treatment. Similarly, enteral phosphate absorption, unexplained by diet or vitamin D intake, may differ by ≥250mg/d among patients. Binder efficacy also varies among patients, with 2-fold differences reported. One or more elements of this triple threat-varying dialytic removal, phosphate absorption, and phosphate binding-may account for hyperphosphatemia in dialysis patients rather than nonadherence to therapy. Just as the cause(s) of hyperphosphatemia may vary, so too may an individual patient's response to different therapeutic interventions.
[Mh] Termos MeSH primário: Dieta
Hiperfosfatemia/sangue
Hiperfosfatemia/dietoterapia
Cooperação do Paciente
Fosfatos/sangue
Diálise Renal/efeitos adversos
[Mh] Termos MeSH secundário: Dieta/efeitos adversos
Seres Humanos
Hiperfosfatemia/diagnóstico
Falência Renal Crônica/sangue
Falência Renal Crônica/diagnóstico
Falência Renal Crônica/terapia
Proteínas de Ligação a Fosfato/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Phosphate-Binding Proteins); 0 (Phosphates)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:160124
[Lr] Data última revisão:
160124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151029
[St] Status:MEDLINE


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[PMID]:26462737
[Au] Autor:Ferreira EL; Batista MT; Cavalcante RC; Pegos VR; Passos HM; Silva DA; Balan A; Ferreira LC; Ferreira RC
[Ad] Endereço:Department of Microbiology, Biomedical Science Institute, University of São Paulo, São Paulo, Brazil.
[Ti] Título:Sublingual immunization with the phosphate-binding-protein (PstS) reduces oral colonization by Streptococcus mutans.
[So] Source:Mol Oral Microbiol;31(5):410-22, 2016 Oct.
[Is] ISSN:2041-1014
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:Bacterial ATP-binding cassette (ABC) transporters play a crucial role in the physiology and pathogenicity of different bacterial species. Components of ABC transporters have also been tested as target antigens for the development of vaccines against different bacterial species, such as those belonging to the Streptococcus genus. Streptococcus mutans is the etiological agent of dental caries, and previous studies have demonstrated that deletion of the gene encoding PstS, the substrate-binding component of the phosphate uptake system (Pst), reduced the adherence of the bacteria to abiotic surfaces. In the current study, we generated a recombinant form of the S. mutans PstS protein (rPstS) with preserved structural features, and we evaluated the induction of antibody responses in mice after sublingual mucosal immunization with a formulation containing the recombinant protein and an adjuvant derived from the heat-labile toxin from enterotoxigenic Escherichia coli strains. Mice immunized with rPstS exhibited systemic and secreted antibody responses, measured by the number of immunoglobulin A-secreting cells in draining lymph nodes. Serum antibodies raised in mice immunized with rPstS interfered with the adhesion of bacteria to the oral cavity of naive mice challenged with S. mutans. Similarly, mice actively immunized with rPstS were partially protected from oral colonization after challenge with the S. mutans NG8 strain. Therefore, our results indicate that S. mutans PstS is a potential target antigen capable of inducing specific and protective antibody responses after sublingual administration. Overall, these observations raise interesting perspectives for the development of vaccines to prevent dental caries.
[Mh] Termos MeSH primário: Anticorpos Antibacterianos/sangue
Cárie Dentária/prevenção & controle
Imunização/métodos
Boca/microbiologia
Proteínas de Ligação a Fosfato/imunologia
Streptococcus mutans/crescimento & desenvolvimento
Streptococcus mutans/imunologia
[Mh] Termos MeSH secundário: Adjuvantes Imunológicos
Administração Sublingual
Animais
Antígenos de Bactérias/imunologia
Aderência Bacteriana
Vacinas Bacterianas/imunologia
Cárie Dentária/microbiologia
Escherichia coli Enterotoxigênica/química
Feminino
Imunidade nas Mucosas
Imunoglobulina A/análise
Camundongos
Proteínas de Ligação a Fosfato/administração & dosagem
Proteínas Recombinantes/administração & dosagem
Proteínas Recombinantes/imunologia
Saliva/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Antibodies, Bacterial); 0 (Antigens, Bacterial); 0 (Bacterial Vaccines); 0 (Immunoglobulin A); 0 (Phosphate-Binding Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170526
[Lr] Data última revisão:
170526
[Sb] Subgrupo de revista:D
[Da] Data de entrada para processamento:151015
[St] Status:MEDLINE
[do] DOI:10.1111/omi.12142



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