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  1 / 1807 MEDLINE  
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PMID:29227076
Autor:Danylovych HV
Título:Evaluation of functioning of mitochondrial electron transport chain with NADH and FAD autofluorescence
Fonte:Ukr Biochem J; 88(1):31-43, 2016 Jan-Feb.
ISSN:2409-4943
País de publicação:Ukraine
Idioma:eng
Resumo:We prove the feasibility of evaluation of mitochondrial electron transport chain function in isolated mitochondria of smooth muscle cells of rats from uterus using fluorescence of NADH and FAD coenzymes. We found the inversely directed changes in FAD and NADH fluorescence intensity under normal functioning of mitochondrial electron transport chain. The targeted effect of inhibitors of complex I, III and IV changed fluorescence of adenine nucleotides. Rotenone (5 µM) induced rapid increase in NADH fluorescence due to inhibition of complex I, without changing in dynamics of FAD fluorescence increase. Antimycin A, a complex III inhibitor, in concentration of 1 µg/ml caused sharp increase in NADH fluorescence and moderate increase in FAD fluorescence in comparison to control. NaN3 (5 mM), a complex IV inhibitor, and CCCP (10 µM), a protonophore, caused decrease in NADH and FAD fluorescence. Moreover, all the inhibitors caused mitochondria swelling. NO donors, e.g. 0.1 mM sodium nitroprusside and sodium nitrite similarly to the effects of sodium azide. Energy-dependent Ca2+ accumulation in mitochondrial matrix (in presence of oxidation substrates and Mg-ATP2- complex) is associated with pronounced drop in NADH and FAD fluorescence followed by increased fluorescence of adenine nucleotides, which may be primarily due to Ca2+- dependent activation of dehydrogenases of citric acid cycle. Therefore, the fluorescent signal of FAD and NADH indicates changes in oxidation state of these nucleotides in isolated mitochondria, which may be used to assay the potential of effectors of electron transport chain.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Enzyme Inhibitors); 0 (Uncoupling Agents); 03L9OT429T (Rotenone); 0U46U6E8UK (NAD); 146-14-5 (Flavin-Adenine Dinucleotide); 169D1260KM (Nitroprusside); 555-60-2 (Carbonyl Cyanide m-Chlorophenyl Hydrazone); 642-15-9 (Antimycin A); 968JJ8C9DV (Sodium Azide); EC 1.10.2.2 (Electron Transport Complex III); EC 1.6.5.3 (Electron Transport Complex I); EC 1.9.3.1 (Electron Transport Complex IV); M0KG633D4F (Sodium Nitrite); SY7Q814VUP (Calcium)


  2 / 1807 MEDLINE  
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PMID:28636676
Autor:Newman M; Halter L; Lim A; Lardelli M
Endereço:Alzheimer's Disease Genetics Laboratory, Centre for Molecular Pathology, School of Biological Sciences, University of Adelaide, Adelaide, South Australia, Australia.
Título:Mitochondrion to endoplasmic reticulum apposition length in zebrafish embryo spinal progenitors is unchanged in response to perturbations associated with Alzheimer's disease.
Fonte:PLoS One; 12(6):e0179859, 2017.
ISSN:1932-6203
País de publicação:United States
Idioma:eng
Resumo:Mutations in the human genes PRESENILIN1 (PSEN1), PRESENILIN2 (PSEN2) and AMYLOID BETA A4 PRECURSOR PROTEIN (APP) have been identified in familial Alzheimer's disease (AD). The length of mitochondrion-endoplasmic reticulum (M-ER) appositions is increased in Psen1-/-/Psen2-/- double knockout murine embryonic fibroblasts and in fibroblasts from AD-affected individuals. Development of an easily accessible, genetically manipulable, in vivo system for studying M-ER appositions would be valuable so we attempted to manipulate M-ER apposition length in zebrafish (Danio rerio) embryos. We injected fertilized zebrafish eggs with antisense morpholino oligonucleotides (MOs) that inhibit expression of zebrafish familial AD gene orthologues psen1 and psen2. Furthermore, we treated zebrafish embryos with DAPT (a highly specific γ-secretase inhibitor) or with sodium azide (to mimic partially hypoxic conditions). We then analyzed M-ER apposition in an identified, presumably proliferative neural cell type using electron microscopy. Our analysis showed no significant differences in M-ER apposition lengths at 48 hours post fertilization (hpf) between psen1 & psen2 MO co-injected embryos, embryos treated with DAPT, or sodium azide, and control embryos. Instead, the distribution of M-ER apposition lengths into different length classes was close to identical. However, this indicates that it is feasible to reproducibly measure M-ER size distributions in zebrafish embryos. While our observations differ from those of murine and human studies, this may be due to differences in cellular differentiation and metabolic state, cell age, or species-specific responses. In particular, by focusing on a presumably proliferative embryonic cell type, we may have selected a cell heavily already reliant on anaerobic glycolysis and less responsive to factors affecting M-ER apposition. Future examination of more differentiated, more secretory cell types may reveal measurable responses of M-ER apposition to environmental and genetic manipulation.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (24-diamino-5-phenylthiazole); 0 (Diamines); 0 (Oligonucleotides, Antisense); 0 (Presenilin-1); 0 (Presenilin-2); 0 (Thiazoles); 0 (Zebrafish Proteins); 0 (presenilin 1 protein, zebrafish); 0 (presenilin 2 protein, zebrafish); 968JJ8C9DV (Sodium Azide); EC 3.4.- (Amyloid Precursor Protein Secretases)


  3 / 1807 MEDLINE  
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PMID:28605976
Autor:Mansour HA; Mahfouz H; Maher N
Endereço:Botany Department, Faculty of Science, Ain Shams University , Abassia, Cairo , Egypt.
Título:Anti-mutagenic potential of algal extracts on chromosomal aberrations in Allium cepa L.
Fonte:Acta Biol Hung; 68(2):137-149, 2017 Jun.
ISSN:0236-5383
País de publicação:Hungary
Idioma:eng
Resumo:In the present study, sodium azide (SA) toxicity and the anti-mutagenic effects of different algal extracts at 0.1% and 0.2% concentrations were studied on the mitotic index (MI), chromosomal and nuclear aberrations using Allium cepa L. root assay. Moreover, phytochemical screening of photosynthetic pigments, antioxidants compounds, total antioxidant, DPPH scavenging activity, polysaccharides, and phenolic contents were done for two red seaweeds (Laurencia obtusa (Hudson) Lamouroux and Polysiphonia morrowii Harvey) and for one brown seaweed (Dictyopteris delicatula Lamouroux). Treatment with 300 µg/ml sodium azide (SA) induced the highest number of aberrations in A. cepa root. A highly significant decrease in the MI appeared after treatment with SA, whereas its value increased following different algal extracts treatments. The highest anti-mutagenic inhibition activity of Dictyopteris delicatula added at 0.2% concentration was 72.96%, 69.84%, 56.89% and 43.59% with the algal polyphenol, polysaccharide, aqueous and methanol extract treatments, respectively. The different algal extracts minimized the genotoxicity and exhibited anti-mutagenic potential against SA in a dose-dependent manner. Phytochemical studies showed that Dictyopteris delicatula contained the highest total phenol, chlorophyll-a and carotenoid quantity. Moreover it exhibited the highest total antioxidant and DPPH scavenging activities. Total polysaccharides and the weight percentage of sulphated polysaccharides were relatively higher in Polysiphonia morrowii followed by Laurencia obtusa. Hydroquinone and bromophenol were detected only in the studied brown and red seaweeds, respectively. Polysiphonia morrowii and Laurencia obtusa contained the highest quantity of galactose, rhmnose and xylose, while Dictyopteris delicatula contained fucose and mannitol as main monosaccharide units. In conclusion, the studied seaweeds may be considered as rich sources of natural antioxidants. Meanwhile the investigated different algal extracts can minimize the genotoxicity in a dose-dependent manner and exhibit anti-mutagenic potential against the mutagenic substance sodium azide.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Antimutagenic Agents); 0 (Free Radical Scavengers); 0 (Plant Extracts); 968JJ8C9DV (Sodium Azide)


  4 / 1807 MEDLINE  
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PMID:28403618
Autor:Cooperstein MA; Nguyen PA; Canavan HE
Endereço:Department of Chemical and Nuclear Engineering, Center for Biomedical Engineering, 1 University of New Mexico, MSC01 1141, Albuquerque, New Mexico 87131-0001.
Título:Poly(N-isopropyl acrylamide)-coated surfaces: Investigation of the mechanism of cell detachment.
Fonte:Biointerphases; 12(2):02C401, 2017 Apr 12.
ISSN:1559-4106
País de publicação:United States
Idioma:eng
Resumo:Although there is a great deal of research focused on cell sheet engineering from polymers such as poly(N-isopropyl acrylamide) (pNIPAM), the biocompatibility of pNIPAM surfaces and the nature of cellular detachment from this polymer is still unclear. The most extensive study of the mechanism of detachment proposed a two-step process, with a first (passive) phase involving hydration of pNIPAM chains, and the second (active) phase involving cellular metabolism. However, a number of studies performed successful cell sheet detachment from pNIPAM-grafted surfaces at low temperatures which calls this hypothesis into question. Furthermore, although it has been demonstrated that low-temperature cell sheet detachment using pNIPAM-grafted surfaces is less destructive than other methods of detachment, it has not been investigated if cell sheet detachment removes a portion of pNIPAM from the surfaces as well. It is essential to know if any fragments of the polymer are removed along with the cells, as small polymer fragments could have cytotoxic effects on the cells. This is especially important if these cells are used for the generation of tissues used for transplantation. In this work, the mechanism of cell detachment from pNIPAM coated surfaces is investigated by testing how temperature and presence of an adenosine triphosephase inhibitor affect cellular detachment. Surface initiated atom transfer polymerization (ATRP) was utilized to synthesize thermoresponsive atrpNIPAM surfaces. pNIPAM surfaces were labeled to assess whether cell sheet detachment from pNIPAM is accompanied by the removal of pNIPAM from the substrate itself. Using a semipermeable superstrate, cell sheets were transferred to a secondary culture dish to assess whether cell detachment resulted in any pNIPAM removal. In addition, the function of the transplanted bovine aortic endothelial cells was assessed by determining whether they would proliferate and grow on a new secondary substrate.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Acrylic Resins); 0 (Coated Materials, Biocompatible); 25189-55-3 (poly-N-isopropylacrylamide); 968JJ8C9DV (Sodium Azide)


  5 / 1807 MEDLINE  
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PMID:28391993
Autor:Park CY; Heo JN; Suk K; Lee WH
Endereço:School of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea.
Título:Sodium azide suppresses LPS-induced expression MCP-1 through regulating IκBζ and STAT1 activities in macrophages.
Fonte:Cell Immunol; 315:64-70, 2017 May.
ISSN:1090-2163
País de publicação:Netherlands
Idioma:eng
Resumo:Sodium azide (NaN ) is a chemical compound with multiple toxic effects on vascular and neuronal systems, causing hypotension and neurotoxicity, respectively. In order to test its effects on the immune system, human and mouse macrophage-like cell lines were treated with nontoxic doses of NaN and the changes in LPS-induced inflammatory activation was measured. Interestingly, the LPS-induced expression of monocyte chemoattractant protein (MCP)-1 was suppressed by NaN without affecting the expression of IL-8 and TNF-α. Further analysis of cellular signaling mediators involved in the expression of these cytokines revealed that NaN suppressed the LPS-induced activation of signal transducers and activator of transcription (STAT)1 and inhibitor of κB (IκB) ς, which are involved in the LPS-induced expression of MCP-1, while the LPS-induced activation of nuclear factor κ-light-chain-enhancer of activated B cells (NF-κB) was not affected. The LPS-induced expression of MCP-2 and CXCL10, which are also regulated by STAT1, was suppressed by NaN . Similarly, the LPS-induced expression of IL-6, which is regulated by IκBζ, was suppressed by NaN . These results demonstrate that NaN selectively suppresses the LPS-induced expression of pro-inflammatory mediators through the suppression of STAT1 and IκBζ activation. These new findings about the activity of NaN may contribute to the development of specific regulators of macrophage activity during acute and chronic inflammation.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Adaptor Proteins, Signal Transducing); 0 (CCL2 protein, human); 0 (Ccl2 protein, mouse); 0 (Chemokine CCL2); 0 (I-kappa B Proteins); 0 (Inflammation Mediators); 0 (Interleukin-8); 0 (Lipopolysaccharides); 0 (NF-kappa B); 0 (NFKBIZ protein, human); 0 (Nfkbiz protein, mouse); 0 (Nuclear Proteins); 0 (STAT1 Transcription Factor); 0 (STAT1 protein, human); 0 (Stat1 protein, mouse); 0 (Tumor Necrosis Factor-alpha); 968JJ8C9DV (Sodium Azide)


  6 / 1807 MEDLINE  
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PMID:28348078
Autor:Lin S; Voyton C; Morris MT; Ackroyd PC; Morris JC; Christensen KA
Endereço:From the Departments of Chemistry and.
Título:pH regulation in glycosomes of procyclic form .
Fonte:J Biol Chem; 292(19):7795-7805, 2017 May 12.
ISSN:1083-351X
País de publicação:United States
Idioma:eng
Resumo:Here we report the use of a fluorescein-tagged peroxisomal targeting sequence peptide (F-PTS1, acetyl-C{K(FITC)}GGAKL) for investigating pH regulation of glycosomes in live procyclic form When added to cells, this fluorescent peptide is internalized within vesicular structures, including glycosomes, and can be visualized after 30-60 min. Using F-PTS1 we are able to observe the pH conditions inside glycosomes in response to starvation conditions. Previous studies have shown that in the absence of glucose, the glycosome exhibits mild acidification from pH 7.4 ± 0.2 to 6.8 ± 0.2. Our results suggest that this response occurs under proline starvation as well. This pH regulation is found to be independent from cytosolic pH and requires a source of Na ions. Glycosomes were also observed to be more resistant to external pH changes than the cytosol; placement of cells in acidic buffers (pH 5) reduced the pH of the cytosol by 0.8 ± 0.1 pH units, whereas glycosomal pH decreases by 0.5 ± 0.1 pH units. This observation suggests that regulation of glycosomal pH is different and independent from cytosolic pH regulation. Furthermore, pH regulation is likely to work by an active process, because cells depleted of ATP with 2-deoxyglucose and sodium azide were unable to properly regulate pH. Finally, inhibitor studies with bafilomycin and EIPA suggest that both V-ATPases and Na /H exchangers are required for glycosomal pH regulation.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Macrolides); 0 (Protozoan Proteins); 116764-51-3 (bafilomycin A); 7DZO8EB0Z3 (Amiloride); 8L70Q75FXE (Adenosine Triphosphate); 968JJ8C9DV (Sodium Azide); 9DLQ4CIU6V (Proline); 9G2MP84A8W (Deoxyglucose); IY9XDZ35W2 (Glucose); KOO5CM684H (Digitonin); RWP5GA015D (Potassium); VW50CE070T (ethylisopropylamiloride)


  7 / 1807 MEDLINE  
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PMID:28298333
Autor:Shaw A; Jeromson S; Watterson KR; Pediani JD; Gallagher IJ; Whalley T; Dreczkowski G; Brooks N; Galloway SD; Hamilton DL
Endereço:Physiology, Exercise and Nutrition Research Group, Faculty of Health Sciences and Sport, University of Stirling, Stirling, United Kingdom.
Título:Multiple AMPK activators inhibit l-carnitine uptake in C2C12 skeletal muscle myotubes.
Fonte:Am J Physiol Cell Physiol; 312(6):C689-C696, 2017 Jun 01.
ISSN:1522-1563
País de publicação:United States
Idioma:eng
Resumo:Mutations in the gene that encodes the principal l-carnitine transporter, OCTN2, can lead to a reduced intracellular l-carnitine pool and the disease Primary Carnitine Deficiency. l-Carnitine supplementation is used therapeutically to increase intracellular l-carnitine. As AMPK and insulin regulate fat metabolism and substrate uptake, we hypothesized that AMPK-activating compounds and insulin would increase l-carnitine uptake in C2C12 myotubes. The cells express all three OCTN transporters at the mRNA level, and immunohistochemistry confirmed expression at the protein level. Contrary to our hypothesis, despite significant activation of PKB and 2DG uptake, insulin did not increase l-carnitine uptake at 100 nM. However, l-carnitine uptake was modestly increased at a dose of 150 nM insulin. A range of AMPK activators that increase intracellular calcium content [caffeine (10 mM, 5 mM, 1 mM, 0.5 mM), A23187 (10 µM)], inhibit mitochondrial function [sodium azide (75 µM), rotenone (1 µM), berberine (100 µM), DNP (500 µM)], or directly activate AMPK [AICAR (250 µM)] were assessed for their ability to regulate l-carnitine uptake. All compounds tested significantly inhibited l-carnitine uptake. Inhibition by caffeine was not dantrolene (10 µM) sensitive despite dantrolene inhibiting caffeine-mediated calcium release. Saturation curve analysis suggested that caffeine did not competitively inhibit l-carnitine transport. To assess the potential role of AMPK in this process, we assessed the ability of the AMPK inhibitor Compound C (10 µM) to rescue the effect of caffeine. Compound C offered a partial rescue of l-carnitine uptake with 0.5 mM caffeine, suggesting that AMPK may play a role in the inhibitory effects of caffeine. However, caffeine likely inhibits l-carnitine uptake by alternative mechanisms independently of calcium release. PKA activation or direct interference with transporter function may play a role.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Enzyme Activators); 0 (Insulin); 0 (Organic Cation Transport Proteins); 0 (Protein Isoforms); 0 (Ribonucleotides); 0 (Slc22a5 protein, mouse); 0 (Solute Carrier Family 22 Member 5); 03L9OT429T (Rotenone); 0I8Y3P32UF (Berberine); 360-97-4 (Aminoimidazole Carboxamide); 37H9VM9WZL (Calcimycin); 3G6A5W338E (Caffeine); 968JJ8C9DV (Sodium Azide); EC 2.7.11.31 (AMP-Activated Protein Kinases); F0X88YW0YK (AICA ribonucleotide); F64QU97QCR (Dantrolene); S7UI8SM58A (Carnitine); SY7Q814VUP (Calcium)


  8 / 1807 MEDLINE  
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PMID:28272030
Autor:Pedrouso A; Val Del Río A; Campos JL; Méndez R; Mosquera-Corral A
Endereço:Department of Chemical Engineering, School of Engineering, Universidade de Santiago de Compostela, Santiago de Compostela E-15705, Spain E-mail: alba.pedrouso@usc.es.
Título:Biomass aggregation influences NaN short-term effects on anammox bacteria activity.
Fonte:Water Sci Technol; 75(5-6):1007-1013, 2017 03.
ISSN:0273-1223
País de publicação:England
Idioma:eng
Resumo:The main bottleneck to maintain the long-term stability of the partial nitritation-anammox processes, especially those operated at low temperatures and nitrogen concentrations, is the undesirable development of nitrite oxidizing bacteria (NOB). When this occurs, the punctual addition of compounds with the capacity to specifically inhibit NOB without affecting the process efficiency might be of interest. Sodium azide (NaN ) is an already known NOB inhibitor which at low concentrations does not significantly affect the ammonia oxidizing bacteria (AOB) activity. However, studies about its influence on anammox bacteria are unavailable. For this reason, the objective of the present study was to evaluate the effect of NaN on the anammox activity. Three different types of anammox biomass were used: granular biomass comprising AOB and anammox bacteria (G1), anammox enriched granules (G2) and previous anammox granules disaggregated (F1). No inhibitory effect of NaN was measured on G1 sludge. However, the anammox activity decreased in the case of G2 and F1. Granular biomass activity was less affected (IC 90 mg/L, G2) than flocculent one (IC 5 mg/L, F1). Summing up, not only does the granular structure protect the anammox bacteria from the NaN inhibitory effect, but also the AOB act as a barrier decreasing the inhibition.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Ammonium Compounds); 968JJ8C9DV (Sodium Azide); K50XQU1029 (Nitrous Oxide)


  9 / 1807 MEDLINE  
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PMID:28217922
Autor:Doleski PH; Adefegha SA; Cabral FL; Leal DB
Endereço:Program of Biochemistry and Molecular Biology, Federal University of Santa Maria, Santa Maria, RS, Brazil.
Título:Characterization of E-NTPDase (EC 3.6.1.5) activity in hepatic lymphocytes: A different activity profile from peripheral lymphocytes.
Fonte:Cell Biochem Funct; 35(2):105-112, 2017 Mar.
ISSN:1099-0844
País de publicação:England
Idioma:eng
Resumo:The activity of ectonucleoside triphosphate diphosphohydrolase (E-NTPDase; EC 3.6.1.5) was characterized in hepatic lymphocytes (HL) of rats. For this purpose, a specific method for the isolation of lymphocytes from hepatic tissue was developed. Subsequently, E-NTPDase activity of rat HL was compared with that of rat peripheral lymphocytes. The HL showed high cell count and viability. Also, the characterization test revealed that the optimal E-NTPDase activities were attained at 37°C and pH 8.0 in the presence of Ca . In addition, in the presence of specific E-NTPDase inhibitors (20mM sodium azide and 0.3mM suramin), there were significant inhibitions in nucleotide hydrolysis. However, there was no significant change in adenosine triphosphate (ATP) or adenosine diphosphate (ADP) hydrolysis in the presence of inhibitors of other E-ATPase (0.1mM Ouabain, 0.5mM orthovanadate, and 1mM, 5mM, and 10mM sodium azide). Furthermore, the kinetic behavior of the enzyme in HL showed apparent Km of 134.90 ± 0.03µM and 214.40 ± 0.06µM as well as Vmax of 345.0 ± 28.32 and 242.0 ± 27.55 Æžmol Pi/min/mg of protein for ATP and ADP, respectively. The Chevillard plot revealed that ATP and ADP were hydrolyzed at the same active site of the enzyme. Our results suggest that the degradation of extracellular nucleotides in HL may have been primarily accomplished by E-NTPDase. The higher E-NTPDase activity observed in HL may be attributed to the important physiological functions of ATP and ADP in HL. SIGNIFICANCE OF THE STUDY: Extracellular purine nucleotides are able to interact with specific receptors and trigger a number of important physiological functions in cells. This interaction is controlled by ectonucleoside triphosphate diphosphohydrolase (E-NTPDase), enzyme that present their catalytic site at the extracellular space and degrades nucleotides. This purinergic signaling has important functions in peripheral lymphocytes and may represent an important new therapeutic target for the treatment of immunological diseases. However, there is dearth of information on the involvement of E-NTPDase in liver lymphocytes. The liver is an important organ, which performs both metabolic and toxicological roles in living organism, and hepatic lymphocytes may play crucial action in the regulation of immune responses in the liver tissue. Furthermore, various chronic diseases such as cirrhosis may be treated with novel pharmacotherapy by targeting the modulation of hepatic lymphocytes. Thus, the significance of this study is to evaluate the activity of E-NTPDase in liver lymphocyte and compare its activity with the peripheral lymphocytes.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Antigens, CD); 0 (Cations, Divalent); 0 (Enzyme Inhibitors); 3WHH0066W5 (Vanadates); 5ACL011P69 (Ouabain); 6032D45BEM (Suramin); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); 968JJ8C9DV (Sodium Azide); EC 3.6.1.5 (Apyrase); EC 3.6.1.5 (CD39 antigen); SY7Q814VUP (Calcium)


  10 / 1807 MEDLINE  
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PMID:28196091
Autor:Rizwan M; Aslam M; Asghar MJ; Abbas G; Shah TM; Shimelis H
Endereço:Nuclear Institute for Agriculture and Biology, Faisalabad, Pakistan.
Título:Pre-breeding of lentil (Lens culinaris Medik.) for herbicide resistance through seed mutagenesis.
Fonte:PLoS One; 12(2):e0171846, 2017.
ISSN:1932-6203
País de publicação:United States
Idioma:eng
Resumo:Lentil is a poor competitor of weeds and its sensitivity to herbicides is a major hurdle for large scale production. The present study was conducted to select herbicide resistant lentil genotypes through seed mutagenesis. Seeds of three advanced lentil genotypes (LPP 11001, LPP 11100 and LPP 11116) were treated with two different concentrations of ethyl methanesulfonate (EMS; 0.1 and 0.2%), hydrazine hydrate (HH; 0.02 and 0.03%) and sodium azide (SA; 0.01 and 0.02%) to develop M1 seed. The M2 was screened against two herbicides including Ally Max 28.6% SG (X = 34.58 g/ha and 1.5X = 51.87 g/ha) and Atlantis 3.6% WG (X = 395.2 g/ha and 1.5X = 592.8 g/ha) using the following three screening methods: post plant emergence (PPE), pre-plant incorporation (PPI) and seed priming (SP). Data were recorded on survival index and survival percentage from each experimental unit of every population. Plants in all populations were categorized following their reaction to herbicides. The newly developed populations showed greater variation for herbicide resistance when compared to their progenitors. Phenotypic traits were significantly reduced in all the screening environments. Overall, 671 herbicide resistant mutants were selected from all testing environments. The seeds from selected plants were re-mutagenized at 150 Gy of gamma radiation and evaluated against higher dose of herbicides. This allowed selection of 134 herbicide resistant mutants. The selected mutants are useful germplasm for herbicide resistance breeding of lentil.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Carcinogens); 0 (Herbicides); 0 (Hydrazines); 0 (Mutagens); 27RFH0GB4R (hydrazine); 968JJ8C9DV (Sodium Azide); 9H154DI0UP (Ethyl Methanesulfonate)



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