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{"title"=>"Macronutrient Composition of the Diet Affects the Feeding-Mediated Down Regulation of Autophagy in Muscle of Rainbow Trout (O. mykiss)", "type"=>"journal", "authors"=>[{"first_name"=>"Ikram", "last_name"=>"Belghit", "scopus_author_id"=>"55855557600"}, {"first_name"=>"Stéphane", "last_name"=>"Panserat", "scopus_author_id"=>"7004125650"}, {"first_name"=>"Bastien", "last_name"=>"Sadoul", "scopus_author_id"=>"55154663000"}, {"first_name"=>"Karine", "last_name"=>"Dias", "scopus_author_id"=>"36536796900"}, {"first_name"=>"Sandrine", "last_name"=>"Skiba-Cassy", "scopus_author_id"=>"16204169900"}, {"first_name"=>"Iban", "last_name"=>"Seiliez", "scopus_author_id"=>"6506731881"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"369822281", "sgr"=>"84884185135", "pmid"=>"24069294", "scopus"=>"2-s2.0-84884185135", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "doi"=>"10.1371/journal.pone.0074308", "issn"=>"19326203"}, "id"=>"8cb7358f-8dba-3449-8cd7-cae2c6edaacd", "abstract"=>"Autophagy functions as an important catabolic mechanism by mediating the turnover of intracellular organelles and protein complexes through a lysosome dependent degradative pathway. Although the induction of autophagy by starvation has been extensively studied, we still know very little about how autophagy is regulated under normal nutritional conditions. The purpose of the present study was to characterize both in vivo and in vitro the response of the autophagy-lysosomal degradative pathway to nutrient (amino acids and carbohydrates) availability in the muscle of the carnivorous rainbow trout. We report that meal feeding is accompanied by a rapid activation of Akt, FoxO1 and the Target of Rapamycin (TOR) signaling pathways and a concomitant decrease of autophagosome formation. We also show that this effect occurs only when the proportion of dietary proteins increases at the expense of carbohydrates. Concurrently, our in vitro study on primary culture of trout muscle cells demonstrates an opposite effect of amino acids and glucose on the regulation of autophagy-lysosomal pathways. More specifically, the addition of amino acids in cell culture medium inhibited the formation of autophagosomes, whereas the addition of glucose had an opposite effect. The effect of amino acids was accompanied by an activation of TOR, considered as an important regulator of autophagosomal formation. However, the mechanisms involved in the effect of glucose were independent of Akt, TOR and AMPK and remain to be determined. Together, these results demonstrated the specific role of macronutrients as well as that of their interactions in the regulation of autophagy and highlight the interest to consider the macronutrient composition of the diets in the control of this degradative pathway.", "link"=>"http://www.mendeley.com/research/macronutrient-composition-diet-affects-feedingmediated-down-regulation-autophagy-muscle-rainbow-trou", "reader_count"=>23, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Librarian"=>1, "Researcher"=>5, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>2, "Student > Master"=>1, "Student > Bachelor"=>4, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Librarian"=>1, "Researcher"=>5, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>2, "Student > Master"=>1, "Student > Bachelor"=>4, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>5, "Materials Science"=>1, "Agricultural and Biological Sciences"=>15, "Medicine and Dentistry"=>1}, "reader_count_by_subdiscipline"=>{"Materials Science"=>{"Materials Science"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>15}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"Canada"=>1, "Hungary"=>1}, "group_count"=>0}

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• http://doi.org/10.1016/j.cbpb.2014.11.009
• http://doi.org/10.1017/S000711452000313X
• http://doi.org/10.1007/s11626-020-00490-1
• http://doi.org/10.1152/ajpregu.00370.2014
• http://doi.org/10.1016/j.aquaculture.2016.04.009
• http://doi.org/10.1016/j.fsi.2015.12.041
• http://doi.org/10.1038/s41598-019-45500-9
• http://doi.org/10.1016/j.biopha.2015.06.003
• http://doi.org/10.1080/15548627.2020.1798064
• http://doi.org/10.1016/j.aquaculture.2015.02.031
• http://doi.org/10.1152/ajpregu.00402.2017
• http://doi.org/10.1007/s10695-019-00664-z
• http://doi.org/10.1016/j.cbpb.2017.09.001
• http://doi.org/10.1038/cddiscovery.2015.65
• http://doi.org/10.1017/S0007114514001226

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/1203252"], "description"=>"<p>Four-day-old cells were incubated in minimal medium (MM) supplemented or not with amino acids (AA) and/or 25 mM Glucose (Glu) in presence or absence of Bafilomycine A1 (Baf A1). After 4 h of incubation, cell lysates (10 µg) were analyzed by western blot with the indicate antibodies. The representative blot is shown. Graphs represent the ratio between LC3-II and β-actin. Results are means ± SE, <i>n = </i>3 (mean of 2 replications). Different letters represent significantly different values (p<0.05).</p>", "links"=>[], "tags"=>["amino", "acids", "glucose", "autophagy", "trout"], "article_id"=>798540, "categories"=>["Biological Sciences"], "users"=>["Ikram Belghit", "Stéphane Panserat", "Bastien Sadoul", "Karine Dias", "Sandrine Skiba-Cassy", "Iban Seiliez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0074308.g004", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Antagonistic_role_of_amino_acids_and_glucose_in_the_regulation_of_autophagy_in_trout_muscle_cell_culture_/798540", "title"=>"Antagonistic role of amino acids and glucose in the regulation of autophagy in trout muscle cell culture.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-09-12 03:19:30"}
• {"files"=>["https://ndownloader.figshare.com/files/1203249"], "description"=>"<p>Six trout were sampled for each time point, starting with unfed fish (T0) and following feeding at 4, 12 and 24 h. Muscle lysates (40 µg) were analysed by Western blot with the indicated antibodies. Representative blots are shown. For LC3b, the graph represents the ratio between LC3-II (lipidated form of LC3b) and β-tubulin used as loading control. For other proteins, graphs represent the ratio between the phosphorylated protein and the total amount of the targeted protein. Results are means ± SE (<i>n = </i>6). Different letters represent significantly different values (p<0.05).</p>", "links"=>[], "tags"=>["autophagosomal", "lc3-ii", "s6k1", "ampk", "proteins", "trout"], "article_id"=>798537, "categories"=>["Biological Sciences"], "users"=>["Ikram Belghit", "Stéphane Panserat", "Bastien Sadoul", "Karine Dias", "Sandrine Skiba-Cassy", "Iban Seiliez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0074308.g002", "stats"=>{"downloads"=>2, "page_views"=>30, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Postprandial_response_of_the_autophagosomal_marker_LC3_II_and_Akt_FoxO1_S6K1_and_AMPK_signaling_proteins_in_trout_muscle_/798537", "title"=>"Postprandial response of the autophagosomal marker LC3-II and Akt, FoxO1, S6K1 and AMPK signaling proteins in trout muscle.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-09-12 03:19:30"}
• {"files"=>["https://ndownloader.figshare.com/files/1203247"], "description"=>"<p>Results are means ± SE (n = 6). Different letters represent significantly different values (p<0.05).</p>", "links"=>[], "tags"=>["triglyceride", "amino", "acids", "rainbow", "trout", "fasted", "48", "refed", "libitum", "sampled", "12", "24"], "article_id"=>798535, "categories"=>["Biological Sciences"], "users"=>["Ikram Belghit", "Stéphane Panserat", "Bastien Sadoul", "Karine Dias", "Sandrine Skiba-Cassy", "Iban Seiliez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0074308.g001", "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Plasma_triglyceride_A_and_amino_acids_B_levels_in_rainbow_trout_fasted_for_48_h_T0_and_refed_ad_libitum_with_a_commercial_diet_and_sampled_4_12_and_24_h_after_the_meal_/798535", "title"=>"Plasma triglyceride (A) and amino acids (B) levels in rainbow trout fasted for 48 h (T0) and refed ad libitum with a commercial diet and sampled 4, 12 and 24 h after the meal.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-09-12 03:19:30"}
• {"files"=>["https://ndownloader.figshare.com/files/1203255"], "description"=>"<p>Four-day-old cells were preincubated for 30 min with or without 100 nM rapamycin. The culture mediums were then remplaced for 30 min or 4 h with the amino acid free medium (minimal medium group, MM and rapamycin group Rap) or a medium containing amino acids (amino acids group AA and amino acids plus rapamycin group AA-Rap) with or without Bafilomycine A1 (Baf A1). Cell lysates (10 µg) were analyzed by western blot with the indicated antibodies. Graphs represent the ratio between the phosphorylated protein and the total amount of S6K1 (A) and the ratio between LC3-II and β-tubulin (B). Results are means ± SE, n = 6 (mean of 2 replications). Different letters represent significantly different values (p<0.05).</p>", "links"=>[], "tags"=>["aa", "rapamycin", "s6k1", "phosphorylation", "lc3", "lipidation", "trout"], "article_id"=>798543, "categories"=>["Biological Sciences"], "users"=>["Ikram Belghit", "Stéphane Panserat", "Bastien Sadoul", "Karine Dias", "Sandrine Skiba-Cassy", "Iban Seiliez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0074308.g006", "stats"=>{"downloads"=>6, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_AA_with_or_without_rapamycin_on_S6K1_phosphorylation_and_LC3_lipidation_in_trout_muscle_cell_culture_/798543", "title"=>"Effect of AA with or without rapamycin on S6K1 phosphorylation and LC3 lipidation in trout muscle cell culture.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-09-12 03:19:30"}
• {"files"=>["https://ndownloader.figshare.com/files/1203256"], "description"=>"1<p>Casein (Sigma-Aldrich, USA).</p>2<p>Casein hydrolysat (Sigma-Aldrich, USA).</p>3<p>L-arginine (Sigma-Aldrich, USA).</p>4<p>Dextrine (Sigma-Aldrich, USA).</p>5<p>Soy Lecithine (Louis François, St Maur des Fossés, France).</p>6<p>Feedoil (North sea fish oil, Sopropèche, Boulogne-sur-Mer, France).</p>7<p>CaHPO4.2H20 (18%P) (Sigma-Aldrich, USA).</p>8<p>Glucosamine 0,5 g; Taurine 0,3 g; Betaine 0,3 g; Glycine 0,2 g; Alanine 0,2 g/100 g feed.</p>9<p>Mineral mixture (g or mg/kg diet) : calcium carbonate (40%Ca), 2.15 g; magnesium oxide (60% Mg), 1.24 g; ferric citrate, 0.2 g;potassium iodide (75% I), 0.4 mg; zinc sulphate (36% Zn), 0.4 g; copper sulphate (25% Cu), 0.3 g; manganese sulphate (33% Mib), 0.3 g; dibasic calcium phosphate (20%Ca, 18%P), 5 g; cobalt sulphate, 2 mg; sodium selenite (30% Se), 3 mg; KCl, 0.9 g; NaCl, 0.4 g (UPAE (unité de préparation des aliments expérimentaux, Jouy, Inra, France)).</p>10<p>Vitamin mixture (IU or mg/kg diet): DL-a tocopherol acetate, 60 IU; sodium menadione bisulphate, 5 mg; retinyl acetate, 15 000 IU; DL-cholecalciferol, 3000 IU; thiamin, 15 mg; riboflavin, 30 mg; pyridoxine, 15 mg; B12, 0.05 mg; nicotinic acid, 175 mg; folic acid, 500 mg; inositol, 1000 mg; biotin, 2.5 mg; calcium panthotenate, 50 mg; choline chloride, 2000 mg(UPAE (unité de préparation des aliments expérimentaux, Jouy, Inra, France)).</p>11<p>Nitrogen-free extract (Carbohydrate) : 100– (crude protein+crude fat+crude fiber+moisture+ash).</p>", "links"=>[], "tags"=>[], "article_id"=>798544, "categories"=>["Biological Sciences"], "users"=>["Ikram Belghit", "Stéphane Panserat", "Bastien Sadoul", "Karine Dias", "Sandrine Skiba-Cassy", "Iban Seiliez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0074308.t001", "stats"=>{"downloads"=>2, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Composition_of_the_experimental_diets_/798544", "title"=>"Composition of the experimental diets.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-09-12 03:19:30"}
• {"files"=>["https://ndownloader.figshare.com/files/1203254"], "description"=>"<p>Four-day-old cells were incubated in minimal medium (MM) supplemented or not with amino acids (AA) and/or 25 mM Glucose (Glu). After 30 min incubation, cell lysates (10 µg) were analyzed by western blot with the indicated antibodies. A representative blot is shown. Graphs represent the ratio between the phosphorylated protein and the total amount of the targeted protein. Results are means ± SE, n = 3 (mean of 2 replications). Different letters represent significantly different values (p<0.05).</p>", "links"=>[], "tags"=>["aa-", "glu-mediated", "autophagy", "trout"], "article_id"=>798542, "categories"=>["Biological Sciences"], "users"=>["Ikram Belghit", "Stéphane Panserat", "Bastien Sadoul", "Karine Dias", "Sandrine Skiba-Cassy", "Iban Seiliez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0074308.g005", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mechanisms_involved_in_AA_and_Glu_mediated_regulation_of_autophagy_in_trout_muscle_cell_culture_/798542", "title"=>"Mechanisms involved in AA- and Glu-mediated regulation of autophagy in trout muscle cell culture.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-09-12 03:19:30"}
• {"files"=>["https://ndownloader.figshare.com/files/1203250"], "description"=>"<p>Muscle lysates (40 µg) were analysed by Western blot with the indicated antibodies. Representative blots are shown. For LC3b, the graph represents the ratio between LC3-II (lipidated form of LC3b) and β-tubulin used as loading control. For other proteins, graphs represent the ratio between the phosphorylated protein and the total amount of the targeted protein. Results are means ± SE (<i>n = </i>6). Different letters represent significantly different values (p<0.05).</p>", "links"=>[], "tags"=>["blot", "lc3-ii", "s6k1", "ampk", "phosphorylation", "fasted", "mpmc", "lphc", "diets", "2h-refed", "rainbow"], "article_id"=>798538, "categories"=>["Biological Sciences"], "users"=>["Ikram Belghit", "Stéphane Panserat", "Bastien Sadoul", "Karine Dias", "Sandrine Skiba-Cassy", "Iban Seiliez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0074308.g003", "stats"=>{"downloads"=>1, "page_views"=>99, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Western_blot_analysis_of_LC3_II_processing_and_Akt_FoxO1_S6K1_and_AMPK_phosphorylation_in_fasted_T0_and_HPLC_MPMC_and_LPHC_diets_2h_refed_rainbow_trout_/798538", "title"=>"Western blot analysis of LC3-II processing and Akt, FoxO1, S6K1 and AMPK phosphorylation in fasted (T0) and HPLC, MPMC and LPHC diets 2h-refed rainbow trout.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-09-12 03:19:30"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime