BUSCADOR RECOLECTA

(A-C) Double immunolocalization of SaAqp1ab1-WT, Flag-tagged HhAqp1ab1-WT or Flag-tagged SsAqp1ab2-WT (green) with the respective HA-tagged splice forms in X. laevis oocytes as indicated. Oocytes expressing SsAqp1ab2-WT and splice forms were co-injected with halibut YwhazLb and exposed to FSK. In all panels, the plasma membrane is indicated by an arrowhead, whereas the co-localization of WT aquaporins and splice forms is indicated by arrows. Scale bars, 10 μm. (D-F) Representative immunoblots of total (TM) and plasma (PM) membrane protein extracts from oocytes injected with water (W) or co-expressing the different aquaporin WT channels with increasing amounts of the splice forms as indicated. (G-I) Illustrative immunoblots of precipitated proteins from oocytes treated as in A-C using anti-SaAqp1ab1 or anti-Flag (for HhAqp1ab1 and SsAqp1ab2) antibodies, and revealed with antibodies against SaAqp1ab1, Flag or HA. In D-I, upper blots were probed with SaAqp1ab1 (D and G) or Flag (E, F, H and I) antibodies, whereas in all panels the lower blots were probed with HA antibodies. Molecular mass markers (kDa) are on the left. The arrowhead in F and I indicate potential post-translational modifications of the SsAqp1ab1_v2 isoform., Peer reviewed

1 file, Supplementary material for the article https://doi.org/10.3390/foods9091239, Figure S1: Culture kinetics of Lb 1.-- Figure S2: Culture kinetics of Ln.-- Figure S3: Culture kinetics of Lb 3.-- Figure S4: Economical evaluation of Lb 2 bioproduction costs.-- Figure S5: Economical evaluation of Ln bioproduction costs.-- Figure S6: Economical evaluation of Lb 3 bioproduction costs.-- Table S1: Parameter kinetics of Lb 2 cultures.-- Table S2: Continuation of Table S2.-- Table S3: Parameter kinetics of Ln cultures.-- Table S4: Continuation of Table S3.-- Table S5: Parameter kinetics of Lb 3 cultures.-- Table S6: Continuation of Table S5.-- Table S7: Ranges of productive yields.-- Table S8: Amino acids content of fish discard peptones.-- Table S9: Continuation of Table S8, Peer reviewed

(A) Amino acid sequence alignment of SsAqp1ab2-WT, SsAqp1ab2_v1 and SsAqp1ab2_v2 splice forms highlighting the sequences employed for the production of the sole-specific Aqp1ab2 and Aqp1ab2_v1 antibodies (α-Aqp1ab2-Nt and α-Aqp1ab2_v1, in red and blue color, respectively). The N- and C-termini of the WT channel, the six transmembrane helices (TM1-TM6) and the two conserved NPA motifs are also indicated. (B) Immunoblots of X. laevis oocytes injected with water or expressing Aqp1ab2-WT, SsAqp1ab2_v1 or SsAqp1ab2_v2 and probed with the α-Aqp1ab2-Nt or α-Aqp1ab2_v1 antisera separately. (C) Representative photomicrographs of sole ovarian follicles at different developmental stages during oocyte growth and maturation. PG, primary growth stage; CA, cortical alveoli stage. Scale bars, 50 and 250 μm. (D) Immunoblots of Aqp1ab2-WT, Aqp1ab2_v1 and Aqp1ab2_v2 in protein extracts from previtellogenic (Pv), vitellogenic (Vt), hydrating (H) and mature (Mt) follicle-enclosed oocytes, as well as from ovulated oocytes (Ov), using the generated antisera. Alpha tubulin (Tuba) was used as loading control. Duplicated blots (right) were run in parallel and incubated with the primary antibodies preadsorbed by the antigenic peptide to test for specificity. The brackets indicate potential post-translational modifications. (E) Hoechst staining of intact vitellogenic follicles and defolliculated oocytes. Scale bar, 100 μm. (F) Immunoblots of Aqp1ab2 isoforms in total protein extracts from intact or defolliculated vitellogenic follicles (+/- follicle cells, Fc). In B, D and E, the arrowheads indicate aquaporin monomers, whereas the asterisks in D and E indicate cross-reactive polypeptides revealed with the Aqp1ab2_v1 antiserum. In all blots, molecular mass markers (kDa) are on the left., Peer reviewed

(A, D, G. J) Representative histological sections of follicle-enclosed oocytes at previtellogenesis, including the primary growth (A) and cortical alveoli (D) stages, vitellogenic (G) and maturing and hydrating (J) stage stained with hematoxylin and eosin. (B-C, E-F, H-I, K-L) Bright field (BF) images and immunostaining of total Aqp1ab2 or Aqp1ab2_v1 (red) in follicles in each of the different stages using the sole-specific α-Aqp1ab2-Nt and α-Aqp1ab2_v1 antisera. Sections were counterstained with 4′,6-diamidino-2-phenylindole (DAPI; blue) and wheat germ agglutinin (WGA; green). Control sections incubated with preabsorbed antisera were negative (S1 Fig). The arrows and arrowheads, indicate granulosa and theca cells, respectively, surrounding the oocyte. Abbreviations: o, oocyte; y, yolk globule; gv, germinal vesicle; ve, vitelline envelope; cp, capillary; ca, cortical alveoli. Scale bars, 10 μm (A-D, H, I, L, K, and inset in I and L), 50 μm (G, J), 20 μm (E, F), 5 μm (inset in E and F)., Peer reviewed

Supplementary Note 1: Mobility data.-- Supplementary Note 2: The statistical description of empirical trajectories.-- Supplementary Note 3: The geographical city center as RP.-- Supplementary Note 4: Relationship between ρ and the field.-- Supplementary Note 5: Unbalance of empirical trajectories in NYC and further Chinese cities.-- Supplementary Note 6: Rand model flux results.-- Supplementary Note 7: Sensitivity analysis with the d-rand model for different D(r).-- Supplementary Note 8: d-rand-d model ρ results.-- Supplementary Note 9: Sensitivity analysis for the d-mix model for R and L.-- Supplementary Note 10: The empirical mobility field.-- Supplementary Note 11: Features of mobility field with Foursquare check-ins data.-- Supplementary Note 12: Fit of the average distance ℓc for the d-mix model., Peer reviewed

Summary of synthesis conditions and yields. Crystallographic parameters of selected samples. Complementary XRD patterns for selected Fe-MIL-88B-NH2 samples obtained at different residence times. Comparison between continuous and discontinuous synthesis results. Cumulative particle size distribution of Fe-MIL-88B-NH2 at 55, 75, and 95 °C. XRD patterns of materials after moisture exposure. TGA curves of as-made and activated materials., Peer reviewed

(A) Representative immunoblots of protein extracts from follicles at the previtellogenic, vitellogenic), hydrating, and mature stage (2.5 follicle equivalents/lane) using the α-Aqp1ab2-Nt antisera. The blots show extracts from three different pools of follicles collected from three different females. The arrowheads indicate the Aqp1ab2-WT, Aqp1ab2_v1 and Aqp1ab2_v2 proteins according to their apparent molecular masses. In all blots, molecular mass markers (kDa) are on the left. (B) Relative amount of the Aqp1ab2_v1 (left) and Aqp1ab2_v2 (right) isoforms with respect to the Aqp1ab2-WT at the different development stages based on the blots shown in A. Bars (mean ± SEM; n = 3 fish) with different superscript are statistically significant (one-way ANOVA; P < 0.05)., Peer reviewed

Synthesis of 4-((4-((4-ethynylphenyl)ethynyl)phenyl)ethynyl)benzoic acid (HOPEA). Full description of the material., Peer reviewed

Additional file 1: Supplementary Table 1. Detailed sequencing data obtained in this study., Horizon 2020 Framework Programme Ministerio de Ciencia e Innovación Generalitat Valenciana Consejo Superior de Investigaciones Cientificas (CSIC), Peer reviewed

Aquaculture is the fastest-growing food production sector and nowadays provides more food than extractive fishing. Studies focused on the understanding of how teleost growth is regulated are essential to improve fish production. Cysteamine (CSH) is a novel feed additive that can improve growth through the modulation of the GH/IGF axis; however, the underlying mechanisms and the interaction between tissues are not well understood. This study aimed to investigate the effects of CSH inclusion in diets at 1.65 g/kg of feed for 9 weeks and 1.65 g/kg or 3.3 g/kg for 9 weeks more, on growth performance and the GH/IGF-1 axis in plasma, liver, stomach, and white muscle in gilthead sea bream (Sparus aurata) fingerlings (1.8 ± 0.03 g) and juveniles (14.46 ± 0.68 g). Additionally, the effects of CSH stimulation in primary cultured muscle cells for 4 days on cell viability and GH/IGF axis relative gene expression were evaluated. Results showed that CSH-1.65 improved growth performance by 16% and 26.7% after 9 and 18 weeks, respectively, while CSH-3.3 improved 32.3% after 18 weeks compared to control diet (0 g/kg). However, no significant differences were found between both experimental doses. CSH reduced the plasma levels of GH after 18 weeks and increased the IGF-1 ones after 9 and 18 weeks. Gene expression analysis revealed a significant upregulation of the ghr-1, different igf-1 splice variants, igf-2 and the downregulation of the igf-1ra and b, depending on the tissue and dose. Myocytes stimulated with 200 µM of CSH showed higher cell viability and mRNA levels of ghr1, igf-1b, igf-2 and igf-1rb compared to control (0 µM) in a similar way to white muscle. Overall, CSH improves growth and modulates the GH/IGF-1 axis in vivo and in vitro toward an anabolic status through different synergic ways, revealing CSH as a feasible candidate to be included in fish feed., Peer reviewed