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[PMID]: 29524694
[Au] Autor:Zhu Y; Li Z; Wang P; Shen L; Zhang D; Yamaguchi Y
[Ad] Address:Engineering Research Center of Optical Instrument and System, Ministry of Education, Shanghai Key Lab of Modern Optical System, University of Shanghai for Science and Technology, No. 516 JunGong Road, Shanghai 200093, China.
[Ti] Title:Factors affecting the separation performance of proteins in capillary electrophoresis.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1083:63-67, 2018 Mar 03.
[Is] ISSN:1873-376X
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Capillary electrophoresis (CE) is an effective tool for protein separation and analysis. Compared with capillary gel electrophoresis (CGE), non-gel sieving capillary electrophoresis (NGSCE) processes the superiority on operation, repeatability and automaticity. Herein, we investigated the effect of polymer molecular weight and concentration, electric field strength, and the effective length of the capillary on the separation performance of proteins, and find that (1) polymer with high molecular weight and concentration favors the separation of proteins, although concentrated polymer hinders its injection into the channel of the capillary due to its high viscosity. (2) The resolution between the adjacent proteins decreases with the increase of electric field strength. (3) When the effective length of the capillary is long, the separation performance improves at the cost of separation time. (4) 1.4% (w/v) hydroxyethyl cellulose (HEC), 100 V/cm voltage and 12 cm effective length offers the best separation for the proteins with molecular weight from 14,400 Da to 97,400 Da. Finally, we employed the optimal electrophoretic conditions to resolve Lysozyme, Ovalbumin, BSA and their mixtures, and found that they were baseline resolved within 15 min.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  2 / 340168 MEDLINE  
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[PMID]: 29524566
[Au] Autor:Uchida N; Haro-Mora JJ; Demirci S; Fujita A; Raines L; Hsieh MM; Tisdale JF
[Ad] Address:Molecular and Clinical Hematology Branch, National Heart Lung and Blood Institutes (NHLBI) / National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK), National Institutes of Health (NIH), Bethesda, Maryland (MD) USA. Electronic address: uchidan@nhlbi.nih.gov.
[Ti] Title:High-level embryonic globin production with efficient erythroid differentiation from a k562 erythroleukemia cell line.
[So] Source:Exp Hematol;, 2018 Mar 07.
[Is] ISSN:1873-2399
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:A reliable cell line capable of robust in vitro erythroid differentiation would be useful to investigate red blood cell (RBC) biology and genetic strategies for RBC diseases. K562 cells are widely utilized for erythroid differentiation; however, current differentiation methods are insufficient to analyze globin proteins. In this study, we sought to improve erythroid differentiation from K562 cells to enable protein-level globin analysis. K562 cells were exposed to a variety of reagents including hemin, rapamycin, imatinib, and/or decitabine (known erythroid inducers), and cultured in basic culture media or erythropoietin-based differentiation media. All single reagents induced observable erythroid differentiation with higher glycophorin A (GPA) expression, but were insufficient to produce detectable globin proteins. We then evaluated various combinations of these reagents, and developed a method incorporating imatinib pre-exposure and an erythropoietin-based differentiation culture containing both rapamycin and decitabine capable of efficient erythroid differentiation, high-level GPA expression (>90%), and high-level globin production at protein levels detectable by hemoglobin electrophoresis and high performance liquid chromatography. Additionally, -globin gene transfer resulted in detectable adult hemoglobin. In summary, we developed an in vitro K562 erythroid differentiation model with high-level globin production. This model provides a practical evaluation tool for hemoglobin production in human erythroid cells.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  3 / 340168 MEDLINE  
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[PMID]: 29524489
[Au] Autor:Wang J; Zhu Z; Wang X; Yang L; Liu L; Wang J; Igbinigie E; Liu X; Li J; Qiu L; Li YQ; Jiang P
[Ad] Address:School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou 213164, Jiangsu, People's Republic of China.
[Ti] Title:A novel monitoring approach of antibody-peptide binding using "bending" capillary electrophoresis.
[So] Source:Int J Biol Macromol;, 2018 Mar 07.
[Is] ISSN:1879-0003
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Recently, the in-capillary electrophoresis assay has been applied to variety kinds of analyses owing to its multiple functional integrating features, including mixing of samples, reaction process of the mixtures, and the separation and detection in one capillary system. However, the micro-reactor still has its limitations to the currently available applications, especially the mixing step of the samples inside the capillary could not be well controlled automatically or manually. Herein, we have developed a novel capillary electrophoresis assay for the detection of antibody-peptide binding inside a bending capillary. Its efficacy was monitored using an anti-FLAG M2 antibody and its ligand conjugated with FAM dye (FAM-DYKD). The antibody and the peptide were mixed inside the bending capillary with sequential injections. It was found that the numbers of semi-circle on the capillary interfered by the antibody and peptide binding dynamic. Additionally, an online competition assay was performed, which further validated the efficacy of the bending capillary device on monitoring the dynamic binding between the antigen and antibody. In summary, our data suggests that the novel assay is a practical approach in monitoring the antibody-antigen complex formation at a nano-scale. It could be applied to detect any biomolecule-biomolecule interaction as a general strategy.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  4 / 340168 MEDLINE  
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[PMID]: 29524430
[Au] Autor:Abidi M; Khan MS; Ahmad S; Kausar T; Nayeem SM; Islam S; Ali A; Alam K; Moinuddin
[Ad] Address:Department of Biochemistry, Jawaharlal Nehru Medical College, AMU, Aligarh, India.
[Ti] Title:Biophysical and biochemical studies on glycoxidatively modified human low density lipoprotein.
[So] Source:Arch Biochem Biophys;, 2018 Mar 07.
[Is] ISSN:1096-0384
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Methylglyoxal (MGO), a reactive dicarbonyl metabolite is a potent arginine directed glycating agent which has implications for diabetes-related complications. Dicarbonyl metabolites are produced endogenously and in a state of misbalance, they contribute to cell and tissue dysfunction through protein and DNA modifications causing dicarbonyl stress. MGO is detoxified by glyoxalase 1 (GLO1) system in the cytoplasm. Reactive oxygen species (ROS) are known to aggravate the glycation process. Both the processes are closely linked, and their combined activity is often referred to as "glycoxidation" process. Glycoxidation of proteins has several consequences such as type 2 diabetes mellitus (T2DM), aging etc. In this study, we have investigated the glycation of low-density lipoprotein (LDL) using different concentrations of MGO for varied incubation time periods. The structural perturbations induced in LDL were analyzed by UV-Vis, fluorescence, circular dichroism spectroscopy, molecular docking studies, polyacrylamide gel electrophoresis, FTIR, thermal denaturation studies, Thioflavin T assay and isothermal titration calorimetry. The ketoamine moieties, carbonyl content and HMF content were quantitated in native and glycated LDL. Simulation studies were also done to see the effect of MGO on the secondary structure of the protein. We report structural perturbations, increased carbonyl content, ketoamine moieties and HMF content in glycated LDL as compared to native analog (native LDL). We report the structural perturbations in LDL upon modification with MGO which could obstruct its normal physiological functions and hence contribute to disease pathogenesis and associated complications.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  5 / 340168 MEDLINE  
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[PMID]: 29510721
[Au] Autor:Gill AJ; Garza R; Ambegaokar SS; Gelman BB; Kolson DL
[Ad] Address:Department of Neurology, Perelman School of Medicine, University of Pennsylvania, 415 Curie Boulevard, 280C Clinical Research Building, Philadelphia, PA, 19104, USA.
[Ti] Title:Heme oxygenase-1 promoter region (GT)n polymorphism associates with increased neuroimmune activation and risk for encephalitis in HIV infection.
[So] Source:J Neuroinflammation;15(1):70, 2018 Mar 06.
[Is] ISSN:1742-2094
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Heme oxygenase-1 (HO-1) is a critical cytoprotective enzyme that limits oxidative stress, inflammation, and cellular injury within the central nervous system (CNS) and other tissues. We previously demonstrated that HO-1 protein expression is decreased within the brains of HIV+ subjects and that this HO-1 reduction correlates with CNS immune activation and neurocognitive dysfunction. To define a potential CNS protective role for HO-1 against HIV, we analyzed a well-characterized HIV autopsy cohort for two common HO-1 promoter region polymorphisms that are implicated in regulating HO-1 promoter transcriptional activity, a (GT)n dinucleotide repeat polymorphism and a single nucleotide polymorphism (A(-413)T). Shorter HO-1 (GT)n repeats and the 'A' SNP allele associate with higher HO-1 promoter activity. METHODS: Brain dorsolateral prefrontal cortex tissue samples from an autopsy cohort of HIV-, HIV+, and HIV encephalitis (HIVE) subjects (n = 554) were analyzed as follows: HO-1 (GT)n polymorphism allele lengths were determined by PCR and capillary electrophoresis, A(-413)T SNP alleles were determined by PCR with allele specific probes, and RNA expression of selected neuroimmune markers was analyzed by quantitative PCR. RESULTS: HIV+ subjects with shorter HO-1 (GT)n alleles had a significantly lower risk of HIVE; however, shorter HO-1 (GT)n alleles did not correlate with CNS or peripheral viral loads. In HIV+ subjects without HIVE, shorter HO-1 (GT)n alleles associated significantly with lower expression of brain type I interferon response markers (MX1, ISG15, and IRF1) and T-lymphocyte activation markers (CD38 and GZMB). No significant correlations were found between the HO-1 (GT)n repeat length and brain expression of macrophage markers (CD163, CD68), endothelial markers (PECAM1, VWF), the T-lymphocyte marker CD8A, or the B-lymphocyte maker CD19. Finally, we found no significant associations between the A(-413)T SNP and HIVE diagnosis, HIV viral loads, or any neuroimmune markers. CONCLUSION: Our data suggest that an individual's HO-1 promoter region (GT)n polymorphism allele repeat length exerts unique modifying risk effects on HIV-induced CNS neuroinflammation and associated neuropathogenesis. Shorter HO-1 (GT)n alleles increase HO-1 promoter activity, which could provide neuroprotection through decreased neuroimmune activation. Therapeutic strategies that induce HO-1 expression could decrease HIV-associated CNS neuroinflammation and decrease the risk for development of HIV neurological disease.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Data-Review
[do] DOI:10.1186/s12974-018-1102-z

  6 / 340168 MEDLINE  
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[PMID]: 29506551
[Au] Autor:Szentpteri A; Lorincz H; Somodi S; Varga VE; Paragh G; Seres I; Paragh G; Harangi M
[Ad] Address:Department of Internal Medicine, Faculty of Medicine, University of Debrecen, Nagyerdei krt. 98, Debrecen, H-4032, Hungary.
[Ti] Title:Serum obestatin level strongly correlates with lipoprotein subfractions in non-diabetic obese patients.
[So] Source:Lipids Health Dis;17(1):39, 2018 Mar 05.
[Is] ISSN:1476-511X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Obestatin is a ghrelin-associated peptide, derived from preproghrelin. Although many of its effects are unclear, accumulating evidence supports positive actions on both metabolism and cardiovascular function. To date, level of obestatin and its correlations to the lipid subfractions in non-diabetic obese (NDO) patients have not been investigated. METHODS: Fifty NDO patients (BMI: 41.96 8.6kg/m ) and thirty-two normal-weight, age- and gender-matched healthy controls (BMI: 24.16 3.3kg/m ) were enrolled into our study. Obestatin level was measured by ELISA. Low-density lipoprotein (LDL) and high-density lipoprotein (HDL) subfractions, intermediate density lipoprotein (IDL) and very low-density lipoprotein (VLDL) levels and mean LDL size were detected by nongradient polyacrylamide gel electrophoresis (Lipoprint). RESULTS: Serum level of obestatin was significantly lower in NDO patients compared to controls (3.01 0.5 vs. 3.29 0.6g/ml, p < 0.05). We found significant negative correlations between the level of obestatin and BMI (r = - 0.33; p < 0.001), level of serum glucose (r = - 0.27, p < 0.05), HbA1c (r = - 0.38; p < 0.001) and insulin (r = - 0.34; p < 0.05). Significant positive correlation was found between obestatin level and the levels of ApoA1 (r = 0.25; p < 0.05), large HDL subfraction ratio and level (r = 0.23; p < 0.05 and r = 0.24; p < 0.05), IDL (r = 0.25 p < 0.05) and mean LDL size (r = 0.25; p < 0.05). Serum VLDL ratio and level negatively correlated with obestatin (r = - 0.32; p < 0.01 and r = - 0.21; p = 0.05). In multiple regression analysis obestatin was predicted only by VLDL level. CONCLUSIONS: Based on our data, measurement of obestatin level in obesity may contribute to understand the interplay between gastrointestinal hormone secretion and metabolic alterations in obesity.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Process
[do] DOI:10.1186/s12944-018-0691-y

  7 / 340168 MEDLINE  
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[PMID]: 29494954
[Au] Autor:Khadsai S; Seeja N; Deepuppha N; Rutnakornpituk M; Vilaivan T; Nakkuntod M; Rutnakornpituk B
[Ad] Address:Department of Chemistry and Center of Excellence in Biomaterials, Faculty of Science, Naresuan University, Phitsanulok 65000, Thailand.
[Ti] Title:Poly(acrylic acid)-grafted magnetite nanoparticle conjugated with pyrrolidinyl peptide nucleic acid for specific adsorption with real DNA.
[So] Source:Colloids Surf B Biointerfaces;165:243-251, 2018 Feb 19.
[Is] ISSN:1873-4367
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Magnetite nanoparticle conjugated with pyrrolidinyl peptide nucleic acid (MNP@PNA) was synthesized for use as both a magnetic nano-support and a probe for specific adsorption with complementary deoxyribonucleic acid (DNA). MNP@PNA with the size ranging between 120 and 170 nm in diameter was prepared via a free radical polymerization of acrylic acid in the presence of acrylamide-grafted MNP to obtain negatively charged magnetic nanoclusters, followed by ionic adsorption with PNA. According to fluorescence spectrophotometry and gel electrophoresis, this MNP@PNA can differentiate between fully matched, single-base mismatched and fully mismatched synthetic DNAs tagged with different fluorophores. UV-vis spectrophotometry and gel electrophoresis indicated that MNP@PNA can be used for specific adsorption with real DNA (zein gene of maize) having complementary sequence with the PNA probe. This novel anionic MNP conjugated with the PNA probe might be potentially applicable for use as a magnetic support for DNA base discrimination and might be a promising tool for testing genetic modification.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  8 / 340168 MEDLINE  
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[PMID]: 29481950
[Au] Autor:Ahmed A; Shamsi A; Khan MS; Husain FM; Bano B
[Ad] Address:Department of Biochemistry, F/O Life Sciences, Aligarh Muslim University, Aligarh, India.
[Ti] Title:Methylglyoxal induced glycation and aggregation of human serum albumin: Biochemical and biophysical approach.
[So] Source:Int J Biol Macromol;113:269-276, 2018 Feb 23.
[Is] ISSN:1879-0003
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Serum protein glycation and formation of advanced glycation end products (AGEs) correlates with many diseases viz. diabetes signifying the importance of studying the glycation pattern of serum proteins. In our present study, methylglyoxal was investigated for its effect on the structure of human serum albumin (HSA); exploring the formation of AGEs and aggregates of HSA. The analytical tools employed includes intrinsic and extrinsic fluorescence, UV spectroscopy, far UV circular dichroism, Thioflavin T fluorescence, congo red binding, polyacrylamide gel electrophoresis (PAGE). UV and fluorescence spectroscopy revealed the structural transition of native HSA evident by new peaks and increased absorbance in UV spectra and quenched fluorescence in the presence of MG. Far UV CD spectroscopy revealed MG induced secondary structural alteration evident by reduced α-helical content. AGEs formation was confirmed by AGEs specific fluorescence. Increased ThT fluorescence and CR absorbance of 10mM MG incubated HSA suggests that glycated HSA results in the formation of aggregates of HSA. SEM and TEM were reported to have an insight of these aggregates. Molecular docking was also utilized to see site specific interaction of MG-HSA. This study is clinically significant as HSA is a clinically relevant protein which plays a crucial role in many diseases.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  9 / 340168 MEDLINE  
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[PMID]: 29481774
[Au] Autor:Christ JJ; Blank LM
[Ad] Address:Institute of Applied Microbiology, Worringer Weg 1, RWTH Aachen University, Aachen, Germany.
[Ti] Title:Enzymatic quantification and length determination of polyphosphate down to a chain length of two.
[So] Source:Anal Biochem;548:82-90, 2018 Feb 24.
[Is] ISSN:1096-0309
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Polyacrylamide gel electrophoresis, being the current method of choice for length determination of inorganic polyphosphate (polyP), requires a sequencing apparatus, relies on commercially not available polyP length standards and yields only a chain length distribution. State of the art polyP quantification involves enzymatic hydrolysis of polyP to orthophosphate with the Saccharomyces cerevisiae exopolyphosphatase 1 (scPpx1p) and subsequent colorimetric orthophosphate detection. Because scPpx1p leaves one pyrophosphate per polyP, short chain polyPs are only partially detected. To overcome this analytical limitation, a method involving both the scPpx1p and the S. cerevisiae inorganic pyrophosphatase (scIpp1p) is proposed. Differential enzymatic hydrolysis of polyP with scPpx1p, and a combination of scIpp1p and scPpx1p allows not only for comprehensive quantification of polyP (excluding cyclic polyP) down to a chain length of two, but also absolute average chain length determination in the range of two to approximately 80. An optimized one-reagent method for rapid (2 min) orthophosphate quantification is part of the assay. Biological phosphorous containing molecules at equimolar phosphorous concentrations regarding polyP do not interfere. The method requires 1.5 g polyP and calls only for a plate reader. This is the first enzymatic method for simultaneous average polyP chain length determination as well as comprehensive quantification.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  10 / 340168 MEDLINE  
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[PMID]: 29474927
[Au] Autor:Cav T; Grgoire MC; Brazeau MA; Boissonneault G
[Ad] Address:Department of Biochemistry, Faculty of Medicine and Health Sciences, Universit de Sherbrooke, Sherbrooke, Quebec, Canada.
[Ti] Title:Post-meiotic DNA double-strand breaks are conserved in fission yeast.
[So] Source:Int J Biochem Cell Biol;98:24-28, 2018 Feb 21.
[Is] ISSN:1878-5875
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:In mammals, spermiogenesis is characterized by transient formation of DNA double-strand breaks (DSBs) in the whole population of haploid spermatids. DSB repair in such haploid context may represent a mutational transition. Using a combination of pulsed-field gel electrophoresis and specific labelling of DSBs at 3'OH DNA ends, we showed that post-meiotic, enzyme-induced DSBs are also observed in the synchronizable pat1-114 mutant of Shizosaccharomyces pombe as well as in a wild-type strain, while DNA repair is observed at later stages. This transient DNA fragmentation arises in the whole cell population and is seemingly independent of the caspase apoptotic pathway. Because histones are still present in spores, the transient DSBs do not require a major change in chromatin structure. These observations confirm the highly-conserved nature of the process in eukaryotes and provide a powerful model to study the underlying mechanism and its impact on the genetic landscape and adaptation.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher


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