02528nas a2200277 4500008004100000022001400041245014300055210006900198260007100267300001400338490000700352520148300359653002501842653001601867653003201883653002601915653000801941653003701949100002501986700002502011700002102036700002402057700002002081700002102101856012802122 2012 eng d a1535-389300aProteome profiling of flax (linum usitatissimum) seed: characterization of functional metabolic pathways operating during seed development0 aProteome profiling of flax linum usitatissimum seed characteriza a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcDEC a6264-62760 v113 a

Flax (Linum usitatissimum L.) seeds are an important source of food and feed due to the presence of various health promoting compounds, making it a nutritionally and economically important plant. An in-depth analysis of the proteome of developing flax seed is expected to provide significant information with respect to the regulation and accumulation of such storage compounds. Therefore, a proteomic analysis of seven seed developmental stages (4, 8, 12, 16, 22, 30, and 48 days after anthesis) in a flax variety, NL-97 was carried out using a combination of ID-SDS-PAGE and LC-MSE methods. A total 1716 proteins were identified and their functional annotation revealed that a majority of them were involved in primary metabolism, protein destination, storage and energy. Three carbon assimilatory pathways appeared to operate in flax seeds. Reverse transcription quantitative PCR of selected 19 genes was carried out to understand their roles during seed development. Besides storage proteins, methionine synthase, RuBisCO and S-adenosylmethionine synthetase were highly expressed transcripts, highlighting their importance in flax seed development. Further, the identified proteins were mapped onto developmental seed specific expressed sequence tag (EST) libraries of flax to obtain transcriptional evidence and 81% of them had detectable expression at the mRNA level. This study provides new insights into the complex seed developmental processes operating in flax.

10aalpha-linolenic acid10acarbon flux10aDigital expression analysis10aflax seed development10aMSE10asecoisolariciresinol diglucoside1 aBarvkar, Vitthal, T.1 aPardeshi, Varsha, C.1 aKale, Sandip, M.1 aKadoo, Narendra, Y.1 aGiri, Ashok, P.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/proteome-profiling-flax-linum-usitatissimum-seed-characterization-functional-metabolic-002078nas a2200229 4500008004100000022001400041245008100055210006900136260000900205300001200214490000800226520130500234653002501539653002401564653002001588653002101608653002301629100002601652700001801678700003601696856011601732 2021 eng d a0141-813000aAlpha-Linolenic acid inhibits Tau aggregation and modulates Tau conformation0 aAlphaLinolenic acid inhibits Tau aggregation and modulates Tau c cJAN  a687-6930 v1663 a

Alzheimer's disease is characterized by important patho-proteins, which being composed of Amyloid-beta, plaques and intracellular neurofibrillary tangles of Tau. Intrinsically disordered protein tau has several interacting partners, which are necessary for its normal functioning. Tau has been shown to interact with various proteins, nucleic acid, and lipids. alpha-Linolenic acid (ALA) a plant-based omega-3 fatty acid has been studied for its role as neuroprotective and beneficial fatty add in the brain. In this study, we are focusing on the ability of ALA to induce spontaneous assembly in tau protein. ALA inhibited the Tau aggregation as indicated by reduced ThS fluorescence kinetics, which indicates no aggregation of Tau. Similarly, SDS-PAGE analysis supported that ALA exposure inhibited the aggregation as no higher-order tau species were observed. Along with its ability to impede the aggregation of Tau, ALA also maintains a native random coiled structure, which was estimated by CD spectroscopy. Finally, TEM analysis showed that the formation of Tau fibrils was found to be discouraged by ALA. Hence, conclusion of the study suggested that ALA profoundly inhibited aggregation of Tau and maintained it's the random-coil structure. (C) 2020 Elsevier B.V. All rights reserved.

10aalpha-linolenic acid10aAlzheimer's disease10aFree fatty adds10aTau conformation10aTau fibrillization1 aDesale, Smita, Eknath1 aDubey, Tushar1 aChinnathambi, Subashchandrabose uhttps://library.ncl.res.in/content/alpha-linolenic-acid-inhibits-tau-aggregation-and-modulates-tau-conformation02613nas a2200229 4500008004100000022001400041245010500055210006900160260000900229300001100238490000700249520182300256653002502079653002202104653001602126653002402142653001702166653001402183100002602197700003602223856012402259 2021 eng d a1933-691800aAlpha-Linolenic acid modulates phagocytosis and endosomal pathways of extracellular Tau in microglia0 aAlphaLinolenic acid modulates phagocytosis and endosomal pathway cJAN  a84-1000 v153 a

Microglia, the resident immune cells, were found to be activated to inflammatory phenotype in Alzheimer's disease (AD). The extracellular burden of amyloid-beta plaques and Tau seed fabricate the activation of microglia. The seeding effect of extracellular Tau species is an emerging aspect to study about Tauopathies in AD. Tau seeds enhance the propagation of disease along with its contribution to microglia-mediated inflammation. The excessive neuroinflammation cumulatively hampers phagocytic function of microglia reducing the clearance of extracellular protein aggregates. Omega-3 fatty acids, especially docosahexaenoic acid and eicosapentaenoic acid, are recognized to induce anti-inflammatory phenotype of microglia. In addition to increased cytokine production, omega-3 fatty acids enhance phagocytic receptors expression in microglia. In this study, we have observed the phagocytosis of extracellular Tau in the presence of alpha-linolenic acid (ALA). The increased phagocytosis of extracellular Tau monomer and aggregates have been observed upon ALA exposure to microglia cells. After internalization, the degradation status of Tau has been studied with early and late endosomal markers Rab5 and Rab7. Further, the lysosome-mediated degradation of internalized Tau was studied with LAMP-2A, a lysosome marker. The enhanced migratory ability in the presence of ALA could be beneficial for microglia to access the target and clear it. The increased migration of microglia was found to induce the microtubule-organizing center repolarization. The data indicate that the dietary fatty acids ALA could significantly enhance phagocytosis and intracellular degradation of internalized Tau. Our results suggest that microglia could be influenced to reduce extracellular Tau seed with dietary fatty acids.

10aalpha-linolenic acid10aendosomal markers10aFatty acids10aMTOC repolarization10aPhagocytosis10aTauopathy1 aDesale, Smita, Eknath1 aChinnathambi, Subashchandrabose uhttps://library.ncl.res.in/content/alpha-linolenic-acid-modulates-phagocytosis-and-endosomal-pathways-extracellular-tau