Base de dados : MEDLINE
Pesquisa : D12.644.050.450 [Categoria DeCS]
Referências encontradas : 258 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 26 ir para página                         

  1 / 258 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28763199
[Au] Autor:Conklin SE; Bridgman EC; Su Q; Riggs-Gelasco P; Haas KL; Franz KJ
[Ad] Endereço:Department of Chemistry, Duke University , Durham, North Carolina 27708, United States.
[Ti] Título:Specific Histidine Residues Confer Histatin Peptides with Copper-Dependent Activity against Candida albicans.
[So] Source:Biochemistry;56(32):4244-4255, 2017 Aug 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The histidine-rich salivary peptides of the histatin family are known to bind copper (Cu) and other metal ions in vitro; however, the details of these interactions are poorly understood, and their implications for in vivo antifungal activity have not been established. Here, we show that the availability of Cu during exposure of Candida albicans to histatin-5 (Hist-5) modulates its antifungal activity. Antifungal susceptibility testing revealed that co-treatment of Hist-5 with Cu improved the EC from ∼5 to ∼1 µM, whereas co-treatment with a high-affinity Cu-specific chelator abrogated antifungal activity. Spectrophotometric titrations revealed two previously unrecognized Cu(I)-binding sites with apparent K values at pH 7.4, ∼20 nM, and confirmed a high-affinity Cu(II)-binding site at the Hist-5 N-terminus with an apparent K of ∼8 pM. Evaluation of a series of His-to-Ala full-length and truncated Hist-5 peptides identified adjacent His residues (bis-His) as critical anchors for Cu(I) binding, with the presence of a third ligand revealed by X-ray absorption spectroscopy. On their own, the truncated peptides were ineffective at inhibiting the growth of C. albicans, but treatment with supplemental Cu resulted in EC values down to ∼5 µM, approaching that of full-length Hist-5. The efficacy of the peptides depended on an intact bis-His site and correlated with Cu(I) affinity. Together, these results establish new structure-function relationships linking specific histidine residues with Cu binding affinity and antifungal activity and provide further evidence of the involvement of metals in modulating the biological activity of these antifungal peptides.
[Mh] Termos MeSH primário: Antifúngicos
Candida albicans/crescimento & desenvolvimento
Cobre
Histatinas
[Mh] Termos MeSH secundário: Antifúngicos/química
Antifúngicos/farmacologia
Cobre/química
Cobre/farmacologia
Histatinas/química
Histatinas/farmacologia
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (HTN3 protein, human); 0 (Histatins); 789U1901C5 (Copper)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00348


  2 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28586222
[Au] Autor:Jephthah S; Henriques J; Cragnell C; Puri S; Edgerton M; Skepö M
[Ad] Endereço:Division of Theoretical Chemistry, Lund University , Post Office Box 124, S-221 00 Lund, Sweden.
[Ti] Título:Structural Characterization of Histatin 5-Spermidine Conjugates: A Combined Experimental and Theoretical Study.
[So] Source:J Chem Inf Model;57(6):1330-1341, 2017 Jun 26.
[Is] ISSN:1549-960X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histatin 5 (Hst5) is a naturally occurring antimicrobial peptide that acts as the first line of defense against oral candidiasis. It has been shown that conjugation of the active Hst5 fragment, Hst5 , and the polyamine spermidine (Spd) improves the candidacidal effect. Knowledge about the structure of these conjugates is, however, very limited. Thus, the aim of this study was to characterize the structural properties of the Hst5 -Spd conjugates by performing atomistic molecular dynamics simulations in combination with small-angle X-ray scattering. It was shown that the Hst5 -Spd conjugates adopt extended and slightly rigid random coil conformations without any secondary structure in aqueous solution. It is hypothesized that the increased fungal killing potential of Hst5 -Spd, in comparison with the Spd-Hst5 conjugate, is due to the more extended conformations of the former, which cause the bonded Spd molecule to be more accessible for recognition by polyamine transporters in the cell.
[Mh] Termos MeSH primário: Histatinas/química
Simulação de Dinâmica Molecular
Espermidina/química
[Mh] Termos MeSH secundário: Conformação Molecular
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histatins); U87FK77H25 (Spermidine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170607
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jcim.7b00150


  3 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28542418
[Au] Autor:Shah D; Ali M; Shukla D; Jain S; Aakalu VK
[Ad] Endereço:Lacrimal Cell Biology Laboratory, University of Illinois at Chicago, Department of Ophthalmology and Visual Sciences, Chicago, United States of America.
[Ti] Título:Effects of histatin-1 peptide on human corneal epithelial cells.
[So] Source:PLoS One;12(5):e0178030, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Ocular surface and corneal epithelial wounds are common and potentially debilitating problems. Ideal treatments for these injuries would promote epithelial healing without inflammation, infection and scarring. In addition the best treatments would be cost-efficient, effective, non-toxic and easily applied. Histatin-1 peptides have been shown to be safe and effective enhancers of epithelial wound healing in other model systems. We sought to determine whether histatin-1 peptides could enhance human corneal epithelial wound healing in vitro. METHODS: Histatin-1 peptides were applied to human corneal epithelial cells and compared over useful dose ranges in scratch assays using time-lapse microscopy. In addition, path finding analysis, cell spreading assays, toxicity and proliferation assays were performed to further characterize the effects of histatin-1 peptide on human corneal limbal epithelial (HCLE). RESULTS: Histatin-1 enhanced human corneal epithelial wound healing in typical wound healing models. There was minimal toxicity and no significant enhancement of proliferation of corneal epithelium in response to histatin-1 application. Corneal epithelial spreading and pathfinding appeared to be enhanced by the application of histatin-1 peptides. CONCLUSIONS: Histatin -1 peptide may enhance migration of HCLE cells and wound healing in vitro. These peptides may have benefit in corneal epithelial wounds and need to be investigated further.
[Mh] Termos MeSH primário: Lesões da Córnea/tratamento farmacológico
Epitélio Anterior/efeitos dos fármacos
Histatinas/farmacologia
Substâncias Protetoras/farmacologia
Reepitelização/efeitos dos fármacos
[Mh] Termos MeSH secundário: Análise de Variância
Bromodesoxiuridina
Movimento Celular/efeitos dos fármacos
Movimento Celular/fisiologia
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/fisiologia
Células Cultivadas
Lesões da Córnea/metabolismo
Lesões da Córnea/patologia
Relação Dose-Resposta a Droga
Avaliação Pré-Clínica de Medicamentos
Epitélio Anterior/metabolismo
Epitélio Anterior/patologia
Imunofluorescência
Histatinas/síntese química
Histatinas/toxicidade
Seres Humanos
Substâncias Protetoras/síntese química
Substâncias Protetoras/toxicidade
Reepitelização/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histatins); 0 (Protective Agents); G34N38R2N1 (Bromodeoxyuridine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178030


  4 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28522595
[Au] Autor:van Dijk IA; Ferrando ML; van der Wijk AE; Hoebe RA; Nazmi K; de Jonge WJ; Krawczyk PM; Bolscher JGM; Veerman ECI; Stap J
[Ad] Endereço:Department of Medical Biology and Core Facility Cellular Imaging, Van Leeuwenhoek Centre for Advanced Microscopy-Academic Medical Center (LCAM-AMC), University of Amsterdam, Amsterdam, The Netherlands; i.a.vandijk@amc.uva.nl.
[Ti] Título:Human salivary peptide histatin-1 stimulates epithelial and endothelial cell adhesion and barrier function.
[So] Source:FASEB J;31(9):3922-3933, 2017 Sep.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histatins are multifunctional histidine-rich peptides secreted by the salivary glands and exclusively present in the saliva of higher primates, where they play a fundamental role in the protection of the oral cavity. Our previously published results demonstrated that histatin-1 (Hst1) promotes cell-substrate adhesion in various cell types and hinted that it could also be involved in cell-cell adhesion, a process of fundamental importance to epithelial and endothelial barriers. Here we explore the effects of Hst1 on cellular barrier function. We show that Hst1 improved endothelial barrier integrity, decreased its permeability for large molecules, and prevented translocation of bacteria across epithelial cell layers. These effects are mediated by the adherens junction protein E-cadherin (E-cad) and by the tight junction protein zonula occludens 1, as Hst1 increases the levels of zonula occludens 1 and of active E-cad. Hst1 may also promote epithelial differentiation as Hst1 induced transcription of the epithelial cell differentiation marker apolipoprotein A-IV (a downstream E-cad target). In addition, Hst1 counteracted the effects of epithelial-mesenchymal transition inducers on the outgrowth of oral cancer cell spheroids, suggesting that Hst1 affects processes that are implicated in cancer progression.-Van Dijk, I. A., Ferrando, M. L., van der Wijk, A.-E., Hoebe, R. A., Nazmi, K., de Jonge, W. J., Krawczyk, P. M., Bolscher, J. G. M., Veerman, E. C. I., Stap, J. Human salivary peptide histatin-1 stimulates epithelial and endothelial cell adhesion and barrier function.
[Mh] Termos MeSH primário: Células Endoteliais/fisiologia
Células Epiteliais/fisiologia
Regulação da Expressão Gênica/fisiologia
Histatinas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Histatinas/genética
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histatins); 101056-53-5 (HTN1 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201700180R


  5 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28511604
[Au] Autor:Basiri T; Johnson ND; Moffa EB; Mulyar Y; Serra Nunes PL; Machado MAAM; Siqueira WL
[Ad] Endereço:1 School of Dentistry and Department of Biochemistry, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, ON, Canada.
[Ti] Título:Duplicated or Hybridized Peptide Functional Domains Promote Oral Homeostasis.
[So] Source:J Dent Res;96(10):1162-1167, 2017 Sep.
[Is] ISSN:1544-0591
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteins that have existed for millions of years frequently contain repeats of functional domains within their primary structure, thereby improving their functional capacity. In the evolutionary young statherin protein contained within the in vivo-acquired enamel pellicle (AEP), we identified a single functional domain (DR9) located within the protein N-terminal portion that exhibits a higher affinity for hydroxyapatite and more efficient protection against enamel demineralization compared to other native statherin peptides. Thus, we tested the hypothesis that multiplication of functional domains of naturally occurring pellicle peptides amplifies protection against enamel demineralization. In addition, a specific amino acid sequence from histatin 3 (RR-14) was introduced to the hybrid peptides for further testing. Enamel specimens were sectioned to 150-µm thickness and randomly grouped as follows: DR9, DR9-DR9, DR9-RR14, statherin, histatin 1, or distilled water (control). After submersion for 2 h at 37°C, the specimens were placed in 2 mL demineralization solution for 12 d at 37°C. Upon sample removal, the remaining solution was subjected to colorimetric assays to determine the amount of calcium and phosphate released from each specimen. DR9-DR9 amplified protection against enamel demineralization when compared to single DR9 or statherin. Notably, the hybrid peptide DR9-RR14 demonstrated relatively strong protection when the antimicrobial property of these peptides was tested against Candida albicans and Streptococcus mutans. DR9-RR14 was able to maintain 50% of the antifungal activity compared with RR14 for C. albicans and similar values of S. mutans killing activity. This study has pioneered the functional exploration of the natural peptide constituents of the AEP and their evolution-inspired engineered peptides. The knowledge obtained here may provide a basis for the development of stable (proteinase-resistant) synthetic peptides for therapeutic use against dental caries, dental erosion, and/or oral candidiasis.
[Mh] Termos MeSH primário: Proteínas do Esmalte Dentário/análise
Película Dentária/química
Durapatita/química
Homeostase/fisiologia
Proteínas e Peptídeos Salivares/análise
[Mh] Termos MeSH secundário: Proteínas do Esmalte Dentário/química
Histatinas/química
Seres Humanos
Dente Molar
Proteínas e Peptídeos Salivares/química
Desmineralização do Dente/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dental Enamel Proteins); 0 (Histatins); 0 (STATH protein, human); 0 (Salivary Proteins and Peptides); 91D9GV0Z28 (Durapatite)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1177/0022034517708552


  6 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28264651
[Au] Autor:Blotnick E; Sol A; Bachrach G; Muhlrad A
[Ad] Endereço:Department of Medical Neurobiology, Institute for Medical Research-Israel-Canada, Hebrew University of Jerusalem, Jerusalem, Israel.
[Ti] Título:Interactions of histatin-3 and histatin-5 with actin.
[So] Source:BMC Biochem;18(1):3, 2017 Mar 06.
[Is] ISSN:1471-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Histatins are histidine rich polypeptides produced in the parotid and submandibular gland and secreted into the saliva. Histatin-3 and -5 are the most important polycationic histatins. They possess antimicrobial activity against fungi such as Candida albicans. Histatin-5 has a higher antifungal activity than histatin-3 while histatin-3 is mostly involved in wound healing in the oral cavity. We found that these histatins, like other polycationic peptides and proteins, such as LL-37, lysozyme and histones, interact with extracellular actin. RESULTS: Histatin-3 and -5 polymerize globular actin (G-actin) to filamentous actin (F-actin) and bundle F-actin filaments. Both actin polymerization and bundling by histatins is pH sensitive due to the high histidine content of histatins. In spite of the equal number of net positive charges and histidine residues in histatin-3 and -5, less histatin-3 is needed than histatin-5 for polymerization and bundling of actin. The efficiency of actin polymerization and bundling by histatins greatly increases with decreasing pH. Histatin-3 and -5 induced actin bundles are dissociated by 100 and 50 mM NaCl, respectively. The relatively low NaCl concentration required to dissociate histatin-induced bundles implies that the actin-histatin filaments bind to each other mainly by electrostatic forces. The binding of histatin-3 to F-actin is stronger than that of histatin-5 showing that hydrophobic forces have also some role in histatin-3- actin interaction. Histatins affect the fluorescence of probes attached to the D-loop of G-actin indicating histatin induced changes in actin structure. Transglutaminase cross-links histatins to actin. Competition and limited proteolysis experiments indicate that the main histatin cross-linking site on actin is glutamine-49 on the D-loop of actin. CONCLUSIONS: Both histatin-3 and -5 interacts with actin, however, histatin 3 binds stronger to actin and affects actin structure at lower concentration than histatin-5 due to the extra 8 amino acid sequence at the C-terminus of histatin-3. Extracellular actin might regulate histatin activity in the oral cavity, which should be the subject of further investigation.
[Mh] Termos MeSH primário: Actinas/metabolismo
Histatinas/metabolismo
[Mh] Termos MeSH secundário: Actinas/química
Difusão Dinâmica da Luz
Corantes Fluorescentes/química
Histatinas/química
Seres Humanos
Concentração de Íons de Hidrogênio
Cinética
Concentração Osmolar
Ligação Proteica
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Fluorescent Dyes); 0 (HTN3 protein, human); 0 (Histatins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170519
[Lr] Data última revisão:
170519
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1186/s12858-017-0078-0


  7 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28261570
[Au] Autor:Du H; Puri S; McCall A; Norris HL; Russo T; Edgerton M
[Ad] Endereço:Department of Oral Biology, School of Dental Medicine, University at Buffalo Buffalo, NY, USA.
[Ti] Título:Human Salivary Protein Histatin 5 Has Potent Bactericidal Activity against ESKAPE Pathogens.
[So] Source:Front Cell Infect Microbiol;7:41, 2017.
[Is] ISSN:2235-2988
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:ESKAPE ( , , , , , and species) pathogens have characteristic multiple-drug resistance and cause an increasing number of nosocomial infections worldwide. Peptide-based therapeutics to treat ESKAPE infections might be an alternative to conventional antibiotics. Histatin 5 (Hst 5) is a salivary cationic histidine-rich peptide produced only in humans and higher primates. It has high antifungal activity against through an energy-dependent, non-lytic process; but its bactericidal effects are less known. We found Hst 5 has bactericidal activity against (60-70% killing) and (85-90% killing) in 10 and 100 mM sodium phosphate buffer (NaPB), while killing of >99% of , 60-80% and 20-60% of was found in 10 mM NaPB. Hst 5 killed 60% of biofilm cells of , but had reduced activity against biofilms of and . Hst 5 killed 20% of biofilm cells but not planktonic cells. Binding and uptake studies using FITC-labeled Hst 5 showed killing required Hst 5 internalization and was energy dependent, while bactericidal activity was rapid against and suggesting membrane disruption. Hst 5-mediated killing of was both non-lytic and energy independent. Additionally, we found that spermidine conjugated Hst 5 (Hst5-Spd) had improved killing activity against , and . Hst 5 or its derivative has antibacterial activity against five out of six ESKAPE pathogens and may be an alternative treatment for these infections.
[Mh] Termos MeSH primário: Antibacterianos/metabolismo
Biofilmes/efeitos dos fármacos
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
Histatinas/metabolismo
Viabilidade Microbiana/efeitos dos fármacos
[Mh] Termos MeSH secundário: Bactérias Gram-Negativas/fisiologia
Bactérias Gram-Positivas/fisiologia
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (HTN3 protein, human); 0 (Histatins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170307
[St] Status:MEDLINE
[do] DOI:10.3389/fcimb.2017.00041


  8 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27941125
[Au] Autor:van Dijk IA; Beker AF; Jellema W; Nazmi K; Wu G; Wismeijer D; Krawczyk PM; Bolscher JG; Veerman EC; Stap J
[Ad] Endereço:1 Department of Cell Biology and Histology, LCAM-AMC, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.
[Ti] Título:Histatin 1 Enhances Cell Adhesion to Titanium in an Implant Integration Model.
[So] Source:J Dent Res;96(4):430-436, 2017 Apr.
[Is] ISSN:1544-0591
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular adhesion is essential for successful integration of dental implants. Rapid soft tissue integration is important to create a seal around the implant and prevent infections, which commonly cause implant failure and can result in bone loss. In addition, soft tissue management is important to obtain good dental aesthetics. We previously demonstrated that the salivary peptide histatin 1 (Hst1) causes a more than 2-fold increase in the ability of human adherent cells to attach and spread on a glass surface. Cells treated with Hst1 attached more rapidly and firmly to the substrate and to each other. In the current study, we examine the potential application of Hst1 for promotion of dental implant integration. Our results show that Hst1 enhances the attachment and spreading of soft tissue cell types (oral epithelial cells and fibroblasts) to titanium (Ti) and hydroxyapatite (HAP), biomaterials that have found wide applications as implant material in dentistry and orthopedics. For improved visualization of cell adhesion to Ti, we developed a novel technique that uses sputtering to deposit a thin, transparent layer of Ti onto glass slides. This approach allows detailed, high-resolution analysis of cell adherence to Ti in real time. Furthermore, our results suggest that Hst1 has no negative effects on cell survival. Given its natural occurrence in the oral cavity, Hst1 could be an attractive agent for clinical application. Importantly, even though Hst1 is specific for saliva of humans and higher primates, it stimulated the attachment and spreading of canine cells, paving the way for preclinical studies in canine models.
[Mh] Termos MeSH primário: Adesão Celular/efeitos dos fármacos
Implantes Dentários
Durapatita/química
Histatinas/farmacologia
Titânio/química
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Cães
Fibroblastos/citologia
Gengiva/citologia
Seres Humanos
Camundongos
Microscopia de Fluorescência
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dental Implants); 0 (Histatins); 101056-53-5 (HTN1 protein, human); 91D9GV0Z28 (Durapatite); D1JT611TNE (Titanium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1177/0022034516681761


  9 / 258 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27780306
[Au] Autor:Santos R; Costa C; Mil-Homens D; Romão D; de Carvalho CC; Pais P; Mira NP; Fialho AM; Teixeira MC
[Ad] Endereço:Department of Bioengineering, Instituto Superior Técnico, Universidade de Lisboa, Lisbon, Portugal.
[Ti] Título:The multidrug resistance transporters CgTpo1_1 and CgTpo1_2 play a role in virulence and biofilm formation in the human pathogen Candida glabrata.
[So] Source:Cell Microbiol;19(5), 2017 May.
[Is] ISSN:1462-5822
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mechanisms of persistence and virulence associated with Candida glabrata infections are poorly understood, limiting the ability to fight this fungal pathogen. In this study, the multidrug resistance transporters CgTpo1_1 and CgTpo1_2 are shown to play a role in C. glabrata virulence. The survival of the infection model Galleria mellonella, infected with C. glabrata, was found to increase upon the deletion of either CgTPO1_1 or CgTPO1_2. The underlying mechanisms were further explored. In the case of CgTpo1_1, this phenotype was found to be consistent with the observation that it confers resistance to antimicrobial peptides (AMP), such as the human AMP histatin-5. The deletion of CgTPO1_2, on the other hand, was found to limit the survival of C. glabrata cells when exposed to phagocytosis and impair biofilm formation. Interestingly, CgTPO1_2 expression was found to be up-regulated during biofilm formation, but and its deletion leads to a decreased expression of adhesin-encoding genes during biofilm formation, which is consistent with a role in biofilm formation. CgTPO1_2 expression was further seen to decrease plasma membrane potential and affect ergosterol and fatty acid content. Altogether, CgTpo1_1 and CgTpo1_2 appear to play an important role in the virulence of C. glabrata infections, being at the cross-road between multidrug resistance and pathogenesis.
[Mh] Termos MeSH primário: Biofilmes
Candida glabrata/fisiologia
Proteínas Fúngicas/fisiologia
Proteínas Associadas à Resistência a Múltiplos Medicamentos/fisiologia
[Mh] Termos MeSH secundário: Animais
Antifúngicos/farmacologia
Candida glabrata/efeitos dos fármacos
Candida glabrata/patogenicidade
Resistência a Múltiplos Medicamentos
Ergosterol/metabolismo
Ácidos Graxos/metabolismo
Expressão Gênica
Genes Fúngicos
Hemócitos/microbiologia
Histatinas/farmacologia
Seres Humanos
Larva/microbiologia
Metabolismo dos Lipídeos
Potenciais da Membrana
Testes de Sensibilidade Microbiana
Viabilidade Microbiana
Mariposas
Fagocitose
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Fatty Acids); 0 (Fungal Proteins); 0 (HTN3 protein, human); 0 (Histatins); 0 (Multidrug Resistance-Associated Proteins); Z30RAY509F (Ergosterol)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE
[do] DOI:10.1111/cmi.12686


  10 / 258 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27612554
[Au] Autor:Ali M; Shah D; Pasha Z; Jassim SH; Jassim Jaboori A; Setabutr P; Aakalu VK
[Ad] Endereço:a Department of Ophthalmology and Visual Sciences , University of Illinois at Chicago , Chicago , IL , USA.
[Ti] Título:Evaluation of Accessory Lacrimal Gland in Muller's Muscle Conjunctival Resection Specimens for Precursor Cell Markers and Biological Markers of Dry Eye Disease.
[So] Source:Curr Eye Res;42(4):491-497, 2017 Apr.
[Is] ISSN:1460-2202
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: The accessory lacrimal glands (ALGs) are an understudied component of the tear functional unit, even though they are important in the development of dry eye syndrome (DES). To advance our understanding of aging changes, regenerative potential, and histologic correlates to human characteristics, we investigated human ALG tissue from surgical samples to determine the presence or absence of progenitor cell markers and lacrimal epithelial markers and to correlate marker expression to relevant patient characteristics. MATERIALS AND METHODS: ALG tissues obtained from Muller's muscle conjunctival resection (MMCR) specimens were created using tissue microarrays (TMAs). Immunofluorescence staining of MMCR sections was performed using primary antibodies specific to cell protein markers. Cell marker localization in TMAs was then assessed by two blinded observers using a standardized scoring system. Patient characteristics including age, race, and status of ocular surface health were then compared against expression of stem cell markers. RESULTS: Human ALG expressed a number of epithelial markers, and in particular, histatin-1 was well correlated with the expression of epithelial markers and was present in most acini. In addition, we noted the presence of precursor cell markers nestin, ABCG2, and CD90 in ALG tissue. There was a decrease in precursor cell marker expression with increasing age. Finally, we noted that a negative association was present between histatin-1 expression and DES. CONCLUSIONS: Thus, we report for the first time that human ALG tissues contain precursor marker-positive cells and that this marker expression may decrease with increasing age. Moreover, histatin-1 expression may be decreased in DES. Future studies will be performed to use these cell markers to isolate and culture lacrimal epithelial cells from heterogeneous tissues, determine the relevance of histatin-1 expression to DES, and isolate candidate precursor cells from ALG tissue.
[Mh] Termos MeSH primário: Biomarcadores/metabolismo
Túnica Conjuntiva/cirurgia
Síndromes do Olho Seco/metabolismo
Proteínas do Olho/metabolismo
Aparelho Lacrimal/metabolismo
Músculos Oculomotores/cirurgia
Células-Tronco/metabolismo
[Mh] Termos MeSH secundário: Blefaroptose/cirurgia
Feminino
Técnica Indireta de Fluorescência para Anticorpo
Histatinas/metabolismo
Seres Humanos
Masculino
Microscopia Confocal
Meia-Idade
Análise Serial de Proteínas
Manejo de Espécimes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Eye Proteins); 0 (Histatins); 101056-53-5 (HTN1 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160911
[St] Status:MEDLINE
[do] DOI:10.1080/02713683.2016.1214966



página 1 de 26 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde