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[PMID]:29395078
[Au] Autor:Han S; Lee JY; Heo EY; Kwon IK; Yune TY; Youn I
[Ad] Endereço:Biomedical Research Institute, Korea Institute of Science and Technology, 5, Hwarang-ro 14-gil, Seongbuk-gu, Seoul, 02791, Republic of Korea.
[Ti] Título:Implantation of a Matrigel-loaded agarose scaffold promotes functional regeneration of axons after spinal cord injury in rat.
[So] Source:Biochem Biophys Res Commun;496(3):785-791, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An agarose scaffold can be useful for supporting and guiding injured axons after spinal cord injury (SCI), but the electrophysiological signal of regenerated axon in scaffolds has not yet been determined. The current study investigated whether a Matrigel-loaded agarose scaffold would enhance the regeneration of axons after SCI. Moreover, the functional connectivity of regenerated axons within the channels of the scaffold was evaluated by directly recording motor evoked potentials. Our data showed that the agarose scaffold containing Matrigel can support and enhance linearly organized axon regeneration after SCI. Additionally, motor evoked potentials were successfully recorded from regenerated axons. These results demonstrate that an agarose scaffold loaded with Matrigel could promote the regeneration of axons and guide the reconnection of functional axons after SCI.
[Mh] Termos MeSH primário: Axônios/patologia
Colágeno/química
Regeneração Tecidual Guiada/instrumentação
Laminina/química
Regeneração Nervosa/fisiologia
Proteoglicanas/química
Traumatismos da Medula Espinal/patologia
Traumatismos da Medula Espinal/terapia
Tecidos Suporte
[Mh] Termos MeSH secundário: Animais
Materiais Biomiméticos/síntese química
Combinação de Medicamentos
Desenho de Equipamento
Análise de Falha de Equipamento
Masculino
Crescimento Neuronal
Próteses e Implantes
Ratos
Ratos Sprague-Dawley
Recuperação de Função Fisiológica
Sefarose/química
Traumatismos da Medula Espinal/fisiopatologia
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drug Combinations); 0 (Laminin); 0 (Proteoglycans); 119978-18-6 (matrigel); 9007-34-5 (Collagen); 9012-36-6 (Sepharose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180204
[St] Status:MEDLINE


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[PMID]:29388544
[Au] Autor:Christiansen L; Bech PK; Schultz-Johansen M; Martens HJ; Stougaard P
[Ad] Endereço:Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark.
[Ti] Título:Colwellia echini sp. nov., an agar- and carrageenan-solubilizing bacterium isolated from sea urchin.
[So] Source:Int J Syst Evol Microbiol;68(2):687-691, 2018 Feb.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel bacterial strain, A3 , was isolated from the intestines of the sea urchin Strongylocentrotus droebachiensis collected in Øresund, Denmark. The strain was Gram-reaction-negative, rod-shaped and facultatively anaerobic, and displayed growth at 5-25 °C (optimum 20 °C), pH 7-9 (optimum at pH 7) and 1-6 % (w/v) NaCl (optimum 3 %). Furthermore, strain A3 grew on agar, agarose, κ-carrageenan, alginate and laminarin as sole carbon source. Complete liquefaction of agar and κ-carrageenan was observed on solid plate media as a result of enzymatic activities. Major fatty acids were summed feature 3 (C16 : 1ω7c and/or C16 : 1ω6c) and C16 : 0. The respiratory quinones were determined to be ubiquinones Q-8 (92 %) and Q-7 (8 %), and polar lipids were phosphatidylethanolamine, phosphatidylglycerol and diphosphatidylglycerol. The DNA G+C content was 36.9 mol%. Phylogenetical analyses based on the 16S rRNA gene showed that the bacterium was affiliated with the genus Colwellia within the Alteromonadaceae of the Gammaproteobacteria. The level of 16S rRNA gene sequence similarity between strain A3 and its closest relatives in the genus Colwellia (C. psychrerythraea ATCC 27364 and C. asteriadis KMD 002 ) was 97.5 %. The average nucleotide identity between strain A3 and other members of Colwellia was 78.6-80.5 %, and DNA-DNA hybridization prediction revealed values of less than 23 % relatedness between strain A3 and other Colwellia species. The phenotypic, phylogenetic and genomic analyses support the hypothesis that strain A3 represents a novel species of the genus Colwellia, for which the name Colwellia echini sp. nov. is proposed. The type strain is A3 (=LMG 30125 =NCIMB 15095 ).
[Mh] Termos MeSH primário: Alteromonadaceae/classificação
Filogenia
Strongylocentrotus/microbiologia
[Mh] Termos MeSH secundário: Ágar
Alginatos
Alteromonadaceae/genética
Alteromonadaceae/isolamento & purificação
Animais
Técnicas de Tipagem Bacteriana
Composição de Bases
Carragenina
DNA Bacteriano/genética
Dinamarca
Ácidos Graxos/química
Gammaproteobacteria
Glucanos
Ácido Glucurônico
Ácidos Hexurônicos
Fosfatidiletanolaminas/química
Fosfatidilgliceróis/química
RNA Ribossômico 16S/genética
Sefarose
Análise de Sequência de DNA
Ubiquinona/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alginates); 0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Glucans); 0 (Hexuronic Acids); 0 (Phosphatidylethanolamines); 0 (Phosphatidylglycerols); 0 (RNA, Ribosomal, 16S); 1339-63-5 (Ubiquinone); 39382-08-6 (phosphatidylethanolamine); 8A5D83Q4RW (Glucuronic Acid); 8C3Z4148WZ (alginic acid); 9000-07-1 (Carrageenan); 9002-18-0 (Agar); 9008-22-4 (laminaran); 9012-36-6 (Sepharose); CQA993F7P8 (ubiquinone 8); RRK47DEG6Q (ubiquinone 7)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180202
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002568


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[PMID]:29267353
[Au] Autor:Khan SR; Kuzminov A
[Ad] Endereço:Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois, United States of America.
[Ti] Título:Degradation of RNA during lysis of Escherichia coli cells in agarose plugs breaks the chromosome.
[So] Source:PLoS One;12(12):e0190177, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nucleoid of Escherichia coli comprises DNA, nucleoid associated proteins (NAPs) and RNA, whose role is unclear. We found that lysing bacterial cells embedded in agarose plugs in the presence of RNases caused massive fragmentation of the chromosomal DNA. This RNase-induced chromosomal fragmentation (RiCF) was completely dependent on the presence of RNase around lysing cells, while the maximal chromosomal breakage required fast cell lysis. Cell lysis in plugs without RNAse made the chromosomal DNA resistant to subsequent RNAse treatment. RiCF was not influenced by changes in the DNA supercoiling, but was influenced by growth temperature or age of the culture. RiCF was partially dependent on H-NS, histone-like nucleoid structuring- and global transcription regulator protein. The hupAB deletion of heat-unstable nucleoid protein (HU) caused increase in spontaneous fragmentation that was further increased when combined with deletions in two non-coding RNAs, nc1 and nc5. RiCF was completely dependent upon endonuclease I, a periplasmic deoxyribonuclease that is normally found inhibited by cellular RNA. Unlike RiCF, the spontaneous fragmentation in hupAB nc1 nc5 quadruple mutant was resistant to deletion of endonuclease I. RiCF-like phenomenon was observed without addition of RNase to agarose plugs if EDTA was significantly reduced during cell lysis. Addition of RNase under this condition was synergistic, breaking chromosomes into pieces too small to be retained by the pulsed field gels. RNase-independent fragmentation was qualitatively and quantitatively comparable to RiCF and was partially mediated by endonuclease I.
[Mh] Termos MeSH primário: Cromossomos Bacterianos
Escherichia coli/genética
RNA/metabolismo
Sefarose/química
[Mh] Termos MeSH secundário: Escherichia coli/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
63231-63-0 (RNA); 9012-36-6 (Sepharose)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190177


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[PMID]:29176788
[Au] Autor:Hasegawa Y; Mark Welch JL; Rossetti BJ; Borisy GG
[Ad] Endereço:Josephine Bay Paul Center for Comparative Molecular Biology and Evolution, Marine Biological Laboratory, Woods Hole, Massachusetts, United States of America.
[Ti] Título:Preservation of three-dimensional spatial structure in the gut microbiome.
[So] Source:PLoS One;12(11):e0188257, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Preservation of three-dimensional structure in the gut is necessary in order to analyze the spatial organization of the gut microbiota and gut luminal contents. In this study, we evaluated preparation methods for mouse gut with the goal of preserving micron-scale spatial structure while performing fluorescence imaging assays. Our evaluation of embedding methods showed that commonly used media such as Tissue-Tek Optimal Cutting Temperature (OCT) compound, paraffin, and polyester waxes resulted in redistribution of luminal contents. By contrast, a hydrophilic methacrylate resin, Technovit H8100, preserved three-dimensional organization. Our mouse intestinal preparation protocol optimized using the Technovit H8100 embedding method was compatible with microbial fluorescence in situ hybridization (FISH) and other labeling techniques, including immunostaining and staining with both wheat germ agglutinin (WGA) and 4', 6-diamidino-2-phenylindole (DAPI). Mucus could be visualized whether the sample was fixed with paraformaldehyde (PFA) or with Carnoy's fixative. The protocol optimized in this study enabled simultaneous visualization of micron-scale spatial patterns formed by microbial cells in the mouse intestines along with biogeographical landmarks such as host-derived mucus and food particles.
[Mh] Termos MeSH primário: Microbioma Gastrointestinal
Preservação Biológica
[Mh] Termos MeSH secundário: Animais
Crioultramicrotomia
Formaldeído/química
Vida Livre de Germes
Hibridização in Situ Fluorescente
Metacrilatos
Camundongos Endogâmicos C57BL
Muco/metabolismo
Inclusão em Parafina
Polímeros/química
Sefarose
Fixação de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Methacrylates); 0 (Polymers); 1HG84L3525 (Formaldehyde); 9012-36-6 (Sepharose); Y19UC83H8E (paraform)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188257


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[PMID]:28743396
[Au] Autor:Finetti C; Sola L; Elliott J; Chiari M
[Ad] Endereço:National Research Council of Italy, Institute of Chemistry of Molecular Recognition, Via Mario Bianco 9 20131 Milan, Italy.
[Ti] Título:Synthesis of hydrogel via click chemistry for DNA electrophoresis.
[So] Source:J Chromatogr A;1513:226-234, 2017 Sep 01.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This work introduces a novel sieving gel for DNA electrophoresis using a classical click chemistry reaction, the copper (I)-catalyzed azide-alkyne cycloaddition (CuAAC), to cross-link functional polymer chains. The efficiency of this reaction provides, under mild conditions, hydrogels with near-ideal network connectivity and improved physical properties. Hydrogel formation via click chemistry condensation of functional polymers does not involve the use of toxic monomers and UV initiation. The performance of the new hydrogel in the separation of double stranded DNA fragments was evaluated in the 2200 TapeStation system, an analytical platform, recently introduced by Agilent that combines the advantages of CE in terms of miniaturization and automation with the simplicity of use of slab gel electrophoresis. The click gel enables addition of florescent dyes prior to electrophoresis with considerable improvement of resolution and separation efficiency over conventional cross-linked polyacrylamide gels.
[Mh] Termos MeSH primário: Química Click/métodos
DNA/análise
Eletroforese/métodos
Hidrogel de Polietilenoglicol-Dimetacrilato/química
[Mh] Termos MeSH secundário: Resinas Acrílicas/química
Alquinos/química
Catálise
Polietilenoglicóis/química
Sefarose/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acrylic Resins); 0 (Alkynes); 0 (polyacrylamide gels); 25852-47-5 (Hydrogel, Polyethylene Glycol Dimethacrylate); 30IQX730WE (Polyethylene Glycols); 9007-49-2 (DNA); 9012-36-6 (Sepharose)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE


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[PMID]:28817933
[Au] Autor:Liang Y; Ma X; Zhang L; Li F; Liu Z; Mao X
[Ad] Endereço:College of Food Science and Engineering, Ocean University of China , Qingdao 266003, China.
[Ti] Título:Biochemical Characterization and Substrate Degradation Mode of a Novel Exotype ß-Agarase from Agarivorans gilvus WH0801.
[So] Source:J Agric Food Chem;65(36):7982-7988, 2017 Sep 13.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Agarases are important hydrolytic enzymes for the biodegradation of agar. Understanding the degradation mode and hydrolysis products of agarases is essential for their utilization in oligosaccharide preparations. Herein, we cloned and expressed AgWH50B, a novel neoagarotetraose-forming ß-agarase from Agarivorans gilvus WH0801 that has high specific activity and a fast reaction rate. AgWH50B consists of a C-terminal glycoside hydrolase family 50 catalytic domain with two tandem noncatalytic carbohydrate-binding modules (CBMs) in the N-terminus (residues 45-214 and 236-442). AgWH50B exhibited good enzymatic properties with high specific activity and catalytic efficiency (1523.2 U/mg and a V of 1700 µmol/min/mg) under optimal hydrolysis conditions of pH 7.0 and 40 °C. Analysis of the hydrolysis products revealed that this enzyme is an exotype ß-agarase and that the dominant product of agarose or oligosaccharide degradation was neoagarotetraose. These findings suggest that AgWH50B could be utilized to yield abundant neoagarotetraose.
[Mh] Termos MeSH primário: Alteromonadaceae/enzimologia
Proteínas de Bactérias/química
Glicosídeo Hidrolases/química
Sefarose/metabolismo
[Mh] Termos MeSH secundário: Alteromonadaceae/química
Alteromonadaceae/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Estabilidade Enzimática
Glicosídeo Hidrolases/genética
Glicosídeo Hidrolases/metabolismo
Cinética
Domínios Proteicos
Sefarose/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 9012-36-6 (Sepharose); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.81 (agarase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170819
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01533


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[PMID]:28757372
[Au] Autor:DiScipio RG; Schraufstatter IU
[Ad] Endereço:Torrey Pines Institute for Molecular Studies, 3550 General Atomics Court, San Diego, CA 92122, United States. Electronic address: rdiscipio@ca.tpims.org.
[Ti] Título:Magnetic bead based assays for complement component C5.
[So] Source:J Immunol Methods;450:50-57, 2017 Nov.
[Is] ISSN:1872-7905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Two novel magnetic agarose bead based assays have been developed to measure complement component C5 interaction with C3b and the Factor I Modules (FIMs) of C7. One innovation was to couple C3b onto the magnetic agarose bead using the alternative pathway C3 convertase, which resulted in a linkage of the ligand by a covalent ester bond. A second innovation was to employ nickel ion charged N,N,N'-tris(carboxymethyl)ethylene-diamine-magnetic agarose to capture recombinantly prepared C7 FIMs that were expressed with an oligo-histidine linker followed by an acidic domain that provided a spacer enabling the C7 modules exposure to C5. Detection was brought about by peroxidase coupled to C5. Both assays exhibited adequate statistics suitable for screening. As examples of the utility of these new methods, we chose to examine influence of natural products on C5 interaction. Fucoidan and ß-glucans were observed to inhibit C3b-C5 interaction, and dextran sulfate was similarly active; however, rosmarinic acid had no measurable effect. In contrast only ß-glucans from two species of macrofungi were able to interfere with interaction of C5 with the FIMs of C7.
[Mh] Termos MeSH primário: Ativação do Complemento
Complemento C3b/imunologia
Complemento C5/imunologia
Complemento C7/imunologia
Técnicas Imunológicas
Magnetismo
[Mh] Termos MeSH secundário: Ativação do Complemento/efeitos dos fármacos
Convertases de Complemento C3-C5/metabolismo
Complemento C3b/metabolismo
Complemento C5/metabolismo
Complemento C7/metabolismo
Ensaio de Atividade Hemolítica de Complemento
Inativadores do Complemento/farmacologia
Sulfato de Dextrana/farmacologia
Hemólise
Seres Humanos
Ferro/química
Polissacarídeos/farmacologia
Ligação Proteica
Sefarose/química
beta-Glucanas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Complement C5); 0 (Complement C7); 0 (Complement Inactivating Agents); 0 (Polysaccharides); 0 (beta-Glucans); 80295-43-8 (Complement C3b); 9012-36-6 (Sepharose); 9042-14-2 (Dextran Sulfate); 9072-19-9 (fucoidan); E1UOL152H7 (Iron); EC 3.4.21.- (Complement C3-C5 Convertases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE


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[PMID]:28690181
[Au] Autor:Pandey R; Saluja D
[Ad] Endereço:Medical Biotechnology Laboratory, Dr. B. R Ambedkar Center for Biomedical Research, University of Delhi, Delhi 110007, India.
[Ti] Título:Hydrogen peroxide agarose gels for electrophoretic analysis of RNA.
[So] Source:Anal Biochem;534:24-27, 2017 Oct 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Efficient electrophoretic separation of isolated total RNA utilizes chemicals and agents to aid in nuclease free environment. However cost, extensive pre-run processing protocols as well as toxic byproducts limit the usage of such protocols. Moreover, these treatments affect the overall electrophoretic results by altering the conductivity of the running buffer and weaken the gel strength. We here provide a protocol for RNA visualization that obviates these shortcomings by preparation of agarose gel with hydrogen peroxide using the regular TAE buffer. The simple, inexpensive protocol exhibits superior results in a horizontal agarose gel electrophoresis.
[Mh] Termos MeSH primário: Géis/química
Peróxido de Hidrogênio/química
RNA/análise
Sefarose/química
[Mh] Termos MeSH secundário: Eletroforese em Gel de Ágar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gels); 63231-63-0 (RNA); 9012-36-6 (Sepharose); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE


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[PMID]:28520808
[Au] Autor:Wu XJ; Dinguirard N; Sabat G; Lui HD; Gonzalez L; Gehring M; Bickham-Wright U; Yoshino TP
[Ad] Endereço:Department of Pathobiological Sciences, University of Wisconsin, Madison, WI, United States of America.
[Ti] Título:Proteomic analysis of Biomphalaria glabrata plasma proteins with binding affinity to those expressed by early developing larval Schistosoma mansoni.
[So] Source:PLoS Pathog;13(5):e1006081, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Interactions between early developing Schistosoma mansoni larval stages and the hemolymph of its snail intermediate host represent the first molecular encounter with the snail's immune system. To gain a more comprehensive understanding of this early parasite-host interaction, biotinylated sporocyst tegumental membrane (Mem) proteins and larval transformation proteins (LTP) were affixed to streptavidin-agarose beads and used as affinity matrices to enrich for larval-reactive plasma proteins from susceptible (NMRI) and resistant (BS-90) strains of the snail Biomphalaria glabrata. Nano-LC/MS-MS proteomic analyses of isolated plasma proteins revealed a diverse array of 94 immune-and nonimmune-related plasma proteins. Included among the immune-related subset were pattern recognition receptors (lectins, LPS-binding protein, thioester-containing proteins-TEPs), stress proteins (HSP60 and 70), adhesion proteins (dermatopontins), metalloproteases (A Disintegrin And Metalloproteinase (ADAM), ADAM-related Zn proteinases), cytotoxins (biomphalysin) and a Ca2+-binding protein (neo-calmodulin). Variable immunoglobulin and lectin domain (VIgL) gene family members, including fibrinogen-related proteins (FREPs), galectin-related proteins (GREPs) and C-type lectin-related proteins (CREPs), were the most prevalent of larval-reactive immune lectins present in plasma. FREPs were highly represented, although only a subset of FREP subfamilies (FREP 2, 3 and 12) were identified, suggesting potential selectivity in the repertoire of plasma lectins recognizing larval glycoconjugates. Other larval-binding FREP-like and CREP-like proteins possessing a C-terminal fibrinogen-related domain (FReD) or C-type lectin binding domain, respectively, and an Ig-fold domain also were identified as predicted proteins from the B. glabrata genome, although incomplete sequence data precluded their placement into specific FREP/CREP subfamilies. Similarly, a group of FReD-containing proteins (angiopoeitin-4, ficolin-2) that lacked N-terminal Ig-fold(s) were identified as a distinct group of FREP-like proteins, separate from the VIgL lectin family. Finally, differential appearance of GREPs in BS-90 plasma eluates, and others proteins exclusively found in eluates of the NMRI strain, suggested snail strain differences in the expression of select larval-reactive immune proteins. This hypothesis was supported by the finding that differential gene expression of the GREP in BS-90 and ADAM in NMRI snail strains generally correlated with their patterns of protein expression. In summary, this study is the first to provide a global comparative proteomic analysis of constitutively expressed plasma proteins from susceptible and resistant B. glabrata strains capable of binding early-expressed larval S. mansoni proteins. Identified proteins, especially those exhibiting differential expression, may play a role in determining immune compatibility in this snail host-parasite system. A complete listing of raw peptide data are available via ProteomeXchange using identifier PXD004942.
[Mh] Termos MeSH primário: Biomphalaria/metabolismo
Proteínas Sanguíneas/metabolismo
Proteínas de Helminto/metabolismo
Interações Hospedeiro-Parasita
Proteômica
Schistosoma mansoni/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas de Bactérias
Biomphalaria/imunologia
Biomphalaria/parasitologia
Hemolinfa/metabolismo
Larva
Mapeamento de Interação de Proteínas
Schistosoma mansoni/imunologia
Schistosoma mansoni/metabolismo
Sefarose/análogos & derivados
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Blood Proteins); 0 (Helminth Proteins); 0 (streptavidin-agarose); 9012-36-6 (Sepharose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006081


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[PMID]:28381360
[Au] Autor:Tabani H; Asadi S; Nojavan S; Parsa M
[Ad] Endereço:Department of Environmental Geology, Research Institute of Applied Sciences (ACECR), Shahid Beheshti University, Tehran, Iran. Electronic address: hadi_tabani@yahoo.com.
[Ti] Título:Introduction of agarose gel as a green membrane in electromembrane extraction: An efficient procedure for the extraction of basic drugs with a wide range of polarities.
[So] Source:J Chromatogr A;1497:47-55, 2017 May 12.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Developing green methods for analyte extraction is one of the most important topics in the field of sample preparation. In this study, for the first time, agarose gel was used as membrane in electromembrane extraction (EME) without using any organic solvent, for the extraction of four model basic drugs (rivastigmine (RIV), verapamil (VER), amlodipine (AML), and morphine (MOR)) with a wide polarity window (log P from 0.43 to 3.7). Different variables playing vital roles in the proposed method were evaluated and optimized. As a driving force, a 25V electrical field was applied to make the analyte migrate from sample solution with pH 7.0, through the agarose gel 3% (w/v) with 5mm thickness, into an acceptor phase (AP) with pH 2.0. The best extraction efficiency was obtained with an extraction duration of 25min. With this new methodology, MOR with high polarity (log P=0.43) was efficiently extracted without using any carrier or ion pair reagents. Limits of detection (LODs) and quantification (LOQs) were in the ranges of 1.5-1.8ngmL and 5.0-6.0ngmL , respectively. Finally, the proposed method was successfully applied to determine concentrations of the model drugs in the wastewater sample.
[Mh] Termos MeSH primário: Anlodipino/isolamento & purificação
Química Verde
Membranas Artificiais
Morfina/isolamento & purificação
Rivastigmina/isolamento & purificação
Sefarose
Verapamil/isolamento & purificação
[Mh] Termos MeSH secundário: Anlodipino/química
Eletricidade
Concentração de Íons de Hidrogênio
Limite de Detecção
Morfina/química
Rivastigmina/química
Verapamil/química
Águas Residuais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membranes, Artificial); 0 (Waste Water); 1J444QC288 (Amlodipine); 76I7G6D29C (Morphine); 9012-36-6 (Sepharose); CJ0O37KU29 (Verapamil); PKI06M3IW0 (Rivastigmine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE



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