BUSCADOR RECOLECTA

1 table. -- Real activity (measured at physiological conditions) and total activity (measured at optimal enzymatic conditions) of the major digestive enzymes in the stomach (pepsin) and pyloric caeca (trypsin, chymotrypsin, leucine aminopeptidase and lipase) of S. dumerili., The study of fish digestive biochemistry is essential to understand factors that affect the net efficiency of food transformation and growth, and therefore aquaculture profitability. The aim of the present study was to assess the activity and functional characteristics of key digestive enzymes in juveniles of greater amberjack (Seriola dumerili), as well as the possible modulation of their relative importance by water temperature. For that, a combination of biochemical assays and substrate-SDS-PAGE were used. Under physiological conditions pepsin activity was negligible. Chymotrypsin was the most active enzyme in the digestive tract of the greater amberjack, while lipase was the enzyme with lower activity, though both enzymes in addition to trypsin were responsive to water temperature as revealed by discriminant analysis. Seriola dumerili showed to have pH-sensitive and, except for chymotrypsin, thermally robust proteases. Inhibition assays showed the major importance of serine proteases and revealed inverse trypsin and chymotrypsin responses to environmental temperature, with higher trypsin contribution in 26°C-fish while higher chymotrypsin contribution in 18°C-fish. Zymograms revealed three isotrypsin and three isochymotrypsin enzymes, with no variation in the presence of particular isoforms among rearing temperatures. However, they confirmed the role of chymotrypsin activity in providing digestive plasticity, with one of the isoforms being more active at lower temperatures. Thus, results indicate that variation in the relative contribution of chymotrypsin isoenzymes to a particular environmental temperature occurs due to different physic-chemical features of isoforms as a source of functional flexibility. This study assessed for the first time the effects of rearing temperature on greater amberjack digestive enzymes, increasing the knowledge on its digestive biochemistry, and aiding in the improvement of management practices for this species industrialization., Peer reviewed

The extreme currents matrix E and the explicite xtreme currents of KNS-LES, KNSCI and KNSCI-LES models., Peer reviewed

1 figure. -- Effect of Ph on the stability of trypsin (TRY), chymotripsin (CHY), leucine aminopeptidase (LAP), lipase (LIP) and pepsin (PP) activities from pyloric caeca and stomach of S. Dumerili adapted to different rearing temperatures (18, 22 and 26º C)., The study of fish digestive biochemistry is essential to understand factors that affect the net efficiency of food transformation and growth, and therefore aquaculture profitability. The aim of the present study was to assess the activity and functional characteristics of key digestive enzymes in juveniles of greater amberjack (Seriola dumerili), as well as the possible modulation of their relative importance by water temperature. For that, a combination of biochemical assays and substrate-SDS-PAGE were used. Under physiological conditions pepsin activity was negligible. Chymotrypsin was the most active enzyme in the digestive tract of the greater amberjack, while lipase was the enzyme with lower activity, though both enzymes in addition to trypsin were responsive to water temperature as revealed by discriminant analysis. Seriola dumerili showed to have pH-sensitive and, except for chymotrypsin, thermally robust proteases. Inhibition assays showed the major importance of serine proteases and revealed inverse trypsin and chymotrypsin responses to environmental temperature, with higher trypsin contribution in 26°C-fish while higher chymotrypsin contribution in 18°C-fish. Zymograms revealed three isotrypsin and three isochymotrypsin enzymes, with no variation in the presence of particular isoforms among rearing temperatures. However, they confirmed the role of chymotrypsin activity in providing digestive plasticity, with one of the isoforms being more active at lower temperatures. Thus, results indicate that variation in the relative contribution of chymotrypsin isoenzymes to a particular environmental temperature occurs due to different physic-chemical features of isoforms as a source of functional flexibility. This study assessed for the first time the effects of rearing temperature on greater amberjack digestive enzymes, increasing the knowledge on its digestive biochemistry, and aiding in the improvement of management practices for this species industrialization., Peer reviewed

eAppendix. Additional acknowledgments eMethods. eFigure 1. Flowchart describing the number of individuals remaining at each filtering steps eFigure 2. V236E and R251G are associated with decreased AD risk across dataset in APOE-stratified sensitivity analyses eFigure 3. APOE ε3/ε3[V236E] individuals have a lower AD risk than APOE ε2/ε3 individuals and APOE ε3/ε4[R251G] have a risk equivalent to ε2/ε3 carriers despite carrying 1 ε4 allele, regardless of the EUR ancestry cutoff for admixed Europeans and Europeans eTable 1. Queried cohort overview to identify admixed and European ancestry individuals in the ADSP discovery and ADGC internal replication eTable 2. Overview of ADSP studies with whole-exome sequencing (WES) and/or whole-genome sequencing (WGS) available at NIAGADS DSS (NG00067) eTable 3. Demographic characteristics of the cohorts queried for discovery and internal replication samples eTable 4. Missense variants on the APOE canonical transcript reported in gnomADv.3.1 eTable 5. Demographic characteristics per cohort in ADSP discovery and ADGC internal replication after ancestry selection, quality control, and duplicates removal eTable 6. APOE missense variants rs769452-C (APOE[L28P]), rs199768005-A (APOE[V236E]), and rs267606661-G (APOE[R251G]) allelic breakdown by APOE main genotype eTable 7. V236E and R251G association in primary and secondary analyses, nonstratified and APOE stratified eTable 8. Nonstratified sensitivity analyses at various European ancestry cutoffs eTable 9. Sensitivity analysis, including all dementia in the CCHS and CGPS data set, slightly strengthens the V236E and R251G associations with decreased AD risk eTable 10. Sensitivity analysis, excluding the UK Biobank proxy-AD phenotype from the meta-analysis, results in slight worsening of the P values of the V236E and R251G associations with decreased AD risk eReferences. Supplemental Online Content: Nonauthor Collaborators., Data for this study were prepared, archived, and distributed by the National Institute on Aging Alzheimer’s Disease Data Storage Site (NIAGADS) at the University of Pennsylvania (U24-AG041689), funded by the National Institute on Aging., Peer reviewed

1 figure. -- Effect of Ph on the stability of trypsin (TRY), chymotripsin (CHY), leucine aminopeptidase (LAP), lipase (LIP) and pepsin (PP) activities from pyloric caeca and stomach of S. Dumerili adapted to different rearing temperatures (18, 22 and 26º C)., The study of fish digestive biochemistry is essential to understand factors that affect the net efficiency of food transformation and growth, and therefore aquaculture profitability. The aim of the present study was to assess the activity and functional characteristics of key digestive enzymes in juveniles of greater amberjack (Seriola dumerili), as well as the possible modulation of their relative importance by water temperature. For that, a combination of biochemical assays and substrate-SDS-PAGE were used. Under physiological conditions pepsin activity was negligible. Chymotrypsin was the most active enzyme in the digestive tract of the greater amberjack, while lipase was the enzyme with lower activity, though both enzymes in addition to trypsin were responsive to water temperature as revealed by discriminant analysis. Seriola dumerili showed to have pH-sensitive and, except for chymotrypsin, thermally robust proteases. Inhibition assays showed the major importance of serine proteases and revealed inverse trypsin and chymotrypsin responses to environmental temperature, with higher trypsin contribution in 26°C-fish while higher chymotrypsin contribution in 18°C-fish. Zymograms revealed three isotrypsin and three isochymotrypsin enzymes, with no variation in the presence of particular isoforms among rearing temperatures. However, they confirmed the role of chymotrypsin activity in providing digestive plasticity, with one of the isoforms being more active at lower temperatures. Thus, results indicate that variation in the relative contribution of chymotrypsin isoenzymes to a particular environmental temperature occurs due to different physic-chemical features of isoforms as a source of functional flexibility. This study assessed for the first time the effects of rearing temperature on greater amberjack digestive enzymes, increasing the knowledge on its digestive biochemistry, and aiding in the improvement of management practices for this species industrialization., Peer reviewed

1 figure. -- 13% substrate SDS-PAGE showing caseinolysc activity bands in pyloric caeca extracts of individual S. dumerili adapted to different rearing temperatures (18, 22 and 26º C). Get incubation temperature 37º C., The study of fish digestive biochemistry is essential to understand factors that affect the net efficiency of food transformation and growth, and therefore aquaculture profitability. The aim of the present study was to assess the activity and functional characteristics of key digestive enzymes in juveniles of greater amberjack (Seriola dumerili), as well as the possible modulation of their relative importance by water temperature. For that, a combination of biochemical assays and substrate-SDS-PAGE were used. Under physiological conditions pepsin activity was negligible. Chymotrypsin was the most active enzyme in the digestive tract of the greater amberjack, while lipase was the enzyme with lower activity, though both enzymes in addition to trypsin were responsive to water temperature as revealed by discriminant analysis. Seriola dumerili showed to have pH-sensitive and, except for chymotrypsin, thermally robust proteases. Inhibition assays showed the major importance of serine proteases and revealed inverse trypsin and chymotrypsin responses to environmental temperature, with higher trypsin contribution in 26°C-fish while higher chymotrypsin contribution in 18°C-fish. Zymograms revealed three isotrypsin and three isochymotrypsin enzymes, with no variation in the presence of particular isoforms among rearing temperatures. However, they confirmed the role of chymotrypsin activity in providing digestive plasticity, with one of the isoforms being more active at lower temperatures. Thus, results indicate that variation in the relative contribution of chymotrypsin isoenzymes to a particular environmental temperature occurs due to different physic-chemical features of isoforms as a source of functional flexibility. This study assessed for the first time the effects of rearing temperature on greater amberjack digestive enzymes, increasing the knowledge on its digestive biochemistry, and aiding in the improvement of management practices for this species industrialization., Peer reviewed

Composition of experimental WD; sensitivity and inter/intra assay precision of the assays used in this study; primer sequences and qPCR conditions; flow cytometry antibodies characteristics; amino acid composition of LPH; raw data of antioxidant parameters; representative standard curve of the antioxidant assays used in this study; body weight monitored over time; and cell proliferation and cell viability., Peer reviewed

14 pages. -- Supplementary description of methods: 1.1. Chemical analysis of pesticides: extraction procedure and LC-MS/MS analysis; 1.2. Acetylcholinesterase (AChE) activity. -- Table S1. MRM conditions used in UPLC-MS/MS determination of pesticides selected. Two transitions (precursor ion →product ion) of each compound were analyzed. -- Table S2. Ranges of nominal and quantified concentrations in μg/L for the two pesticides used and the metabolite analyzed in the colonization assays. -- Table S3. Results of the Chi-square test to check statistically significant differences between the percentage of colonization achieved by the organisms in each chamber at 48h in the pesticide experiments and the expected value (100%). -- Table S4. Results of the within-group Kruskal-Wallis test to check statistically significant differences between chambers (source of variation) for the percentage of colonization of D. magna achieved at 48h in each pesticide experiment, together with the significant results of the pairwise post hoc test. -- Table S5. Results of the between-group Kruskal-Wallis test to check statistically significant differences between colonization experiments and chambers (sources of variation) for the percentage of colonization of D. magna at 48h, together with the significant results of the pairwise post hoc test. -- Table S6. Mean, standard error (SE), maximum and minimum values obtained for the mobility variables analyzed in D. magna after 48 h of exposure to the different study treatments. -- Table S7. Results of PERMANOVA ONE-WAY test to check statistically significant differences between study treatments for the mobility variables evaluated, together with the significant results of the pairwise post hoc test. -- Table S8. Results of Kruskal-Wallis test to check statistically significant differences between study treatments for the average vertical speed (study variable with non-normal distribution according to Shapiro-Wilk test), together with the significant results of the pairwise post hoc test and Dunn´s multiple comparisons test (specific comparisons with the control treatment). -- Table S9. One-way ANOVA test to check statistically significant differences among treatments for the remaining mobility variables evaluated, together with the significant results of the pairwise post hoc test and Dunnett´s multiple comparisons test (specific comparisons with the control treatment). -- Table S10. Mean, standard error (SE), maximum and minimum values obtained for the AChE activity in D. magna after 48 h of exposure to the different study treatments. -- Table S11. One-way ANOVA test to check statistically significant differences among treatments for the acetylcholinesterase (AChE) activity, together with the significant results of the pairwise post hoc test. -- Fig. S1. HeMHAS – Heterogeneous Multi-Habitat Assay System (version #3) used in the colonization experiments. -- Fig. S2. Detail of one of the compartments of the HeMHAS together with two gates that connect it to the adjacent chambers throughout a rotary locking system. -- Fig. S3. Picture of D. magna individually disposed in four wells of culture plates for analysis of horizontal swimming behavior. -- Fig. S4. Percentage of organisms (A) and colonization response (B) achieved in each chamber in the control test at 48h with ±SE of four replicates. -- Fig. S5. PCA analysis of the responses obtained for the mobility variables analysed in D. magna exposed to the different study treatments., Peer reviewed

Table S1 Concentrations (ng/g) of organochlorine compounds in tissue (blood and adipose) of caracals in the Greater Cape Town area, South Africa in terms of wet weight (w.w.) and lipid weight (l.w.). Table S2 Spatial covariates considered for models of organochlorine exposure in caracal in the Greater Cape Town area, South Africa. Fig. S3 Boxplots (diamonds = means) of organochlorine compound concentrations (ng/g, logged) in whole blood and adipose of caracals in the Greater Cape Town area, South Africa. Table S4 Estimates (SE) of top linear mixed effects models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and spatial predictors in caracal in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S5 Estimates (SE) of top linear mixed effects models (based on AICc) of adipose organochlorine levels (ng/g, logged) and spatial predictors in caracal in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S6 Diet proportions in several prey groupings for caracals around Cape Town, South Africa as determined by through integrating diet datasets from scat and prey remains found at GPS clusters. Table S7 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (biomass) for broad taxonomic groups for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S8 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (FO) for broad taxonomic groups for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S9 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (biomass) for prey functional groups for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S10 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (FO) for prey functional groups for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S11 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (biomass) for prey foraging habitat for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S12 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (FO) for prey foraging habitat for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S13 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (biomass) for exotic prey groups for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S14 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and diet (FO) for exotic prey groups for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S15 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and blood cell count for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S16 Estimates (SE) for top models (based on AICc) of whole blood organochlorine levels (ng/g, logged) and serum biochemistry measures for caracals in the Greater Cape Town area, South Africa (*P < 0.1; **P < 0.05; ***P < 0.01). Table S17 Comparison of DDT concentrations (ng/g) ± SE in wild terrestrial mammalian predators from published studies. Where possible, like tissue was compared with like, but where not, serum/plasma was compared with caracal whole blood and liver/kidney was compared with caracal adipose. Table S18 Comparison of PCB concentrations (ng/g) ± SE in wild terrestrial mammalian predators from published studies. Where possible, like tissue was compared with like, but where not, serum/plasma was compared with caracal whole blood and liver/kidney was compared with caracal adipose., Peer reviewed

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