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1.
Food Chem ; 462: 140926, 2025 Jan 01.
Article de Anglais | MEDLINE | ID: mdl-39208741

RÉSUMÉ

Sturgeon, with 4 times higher lipid content than silver carp (ubiquitously applied for surimi production in China), affects surimi gelling properties. However, how the flesh lipids affect gelling properties remains unclear. This study investigated how flesh lipids impact surimi gelling properties and elucidated the interaction mechanism between lipids and proteins. Results revealed yellow meat contains 7 times higher lipids than white meat. Stronger ionic protein-protein interactions were replaced by weaker hydrophobic forces and hydrogen bonds in protein-lipid interaction. Protein-lipid interaction zones encapsulated lipid particles, changing protein structure from α-helix to ß-sheet structure thereby gel structure becomes flexible and disordered, significantly diminishing surimi gel strength. Docking analysis validated fatty acid mainly binding at Ala577, Ile461, Arg231, Phe165, His665, and His663 of myosin. This study first reported the weakened surimi gelling properties from the perspective of free fatty acids and myosin interactions, offering a theoretical basis for sturgeon surimi production.


Sujet(s)
Protéines de poisson , Poissons , Gels , Lipides , Animaux , Gels/composition chimique , Lipides/composition chimique , Protéines de poisson/composition chimique , Protéines de poisson/métabolisme , Produits de la pêche/analyse , Interactions hydrophobes et hydrophiles , Liaison hydrogène , Myosines/composition chimique , Myosines/métabolisme , Simulation de docking moléculaire , Acides gras/composition chimique , Acides gras/métabolisme , Carpes (poisson)/métabolisme , Liaison aux protéines
2.
Food Chem ; 462: 141017, 2025 Jan 01.
Article de Anglais | MEDLINE | ID: mdl-39216379

RÉSUMÉ

The Atlantic salmon is an extremely popular fish for its nutritional value and unique taste among several fish species. Researchers are focusing on the utilization of Atlantic salmon waste for generating protein hydrolysates rich in peptides and amino acids and investigating their health benefits. Several technological approaches, including enzymatic, chemical, and the recently developed subcritical water hydrolysis, are currently used for the production of Atlantic salmon waste protein hydrolysates. Hydrolyzing various wastes, e.g., heads, bones, skin, viscera, and trimmings, possessing antioxidant, blood pressure regulatory, antidiabetic, and anti-inflammatory properties, resulting in applications in human foods and nutraceuticals, animal farming, pharmaceuticals, cell culture, and cosmetics industries. Furthermore, future applications, constraints several challenges associated with industrial hydrolysate production, including sensory, safety, and economic constraints, which could be overcome by suggested techno processing measures. Further studies are recommended for developing large-scale, commercially viable production methods, focusing on eradicating sensory constraints and facilitating large-scale application.


Sujet(s)
Protéines de poisson , Hydrolysats de protéines , Salmo salar , Animaux , Salmo salar/métabolisme , Hydrolysats de protéines/composition chimique , Protéines de poisson/composition chimique , Protéines de poisson/métabolisme , Humains , Hydrolyse , Déchets/analyse
3.
BMC Genomics ; 25(1): 918, 2024 Oct 02.
Article de Anglais | MEDLINE | ID: mdl-39358679

RÉSUMÉ

BACKGROUND: Thermal stress is a major environmental factor affecting fish development and survival. Common carp (Cyprinus carpio) are susceptible to heat stress in their embryonic and larval phases, but the thermal stress response of alternative splicing during common carp embryogenesis remains poorly understood. RESULTS: Using RNA-seq data from eight developmental stages and four temperatures, we constructed a comprehensive profile of alternative splicing (AS) during the embryogenesis of common carp, and found that AS genes and events are widely distributed among all stages. A total of 5,835 developmental stage-specific AS (SAS) genes, 21,368 temperature-specific differentially expressed genes (TDEGs), and 2,652 temperature-specific differentially AS (TDAS) genes were identified. Hub TDAS genes in each developmental stage, such as taf2, hnrnpa1, and drg2, were identified through protein-protein interaction (PPI) network analysis. The early developmental stages may be more sensitive to temperature, with thermal stress leading to a massive increase in the number of expressed transcripts, TDEGs, and TDAS genes in the morula stage, followed by the gastrula stage. GO and KEGG analyses showed that from the morula stage to the neurula stage, TDAS genes were more involved in intracellular transport, protein modification, and localization processes, while from the optic vesicle stage to one day post-hatching, they participated more in biosynthetic processes. Further subgenomic analysis revealed that the number of AS genes and events in subgenome B was generally higher than that in subgenome A, and the homologous AS genes were significantly enriched in basic life activity pathways, such as mTOR signaling pathway, p53 signaling pathway, and MAPK signaling pathway. Additionally, lncRNAs can play a regulatory role in the response to thermal stress by targeting AS genes such as lmnl3, affecting biological processes such as apoptosis and axon guidance. CONCLUSIONS: In short, thermal stress can affect alternative splicing regulation during common carp embryogenesis at multiple levels. Our work complemented some gaps in the study of alternative splicing at both levels of embryogenesis and thermal stress in C. carpio and contributed to the comprehension of environmental adaptation formation in polyploid fishes during embryogenesis.


Sujet(s)
Épissage alternatif , Carpes (poisson) , Développement embryonnaire , Réaction de choc thermique , Animaux , Carpes (poisson)/génétique , Carpes (poisson)/embryologie , Carpes (poisson)/métabolisme , Développement embryonnaire/génétique , Réaction de choc thermique/génétique , Régulation de l'expression des gènes au cours du développement , Analyse de profil d'expression de gènes , Cartes d'interactions protéiques , Protéines de poisson/génétique , Protéines de poisson/métabolisme
4.
Genes (Basel) ; 15(9)2024 Sep 23.
Article de Anglais | MEDLINE | ID: mdl-39336829

RÉSUMÉ

17α-Methyltestosterone (MT) is a widely used androgen for all-male fish production in aquaculture. However, the molecular mechanism underlying MT-induced masculinization remains unclear. In this study, we aim to identify the key gene responsible for MT-induced masculinization using the Nile tilapia (Oreochromis niloticus) amhy, dmrt1, and gsdf mutants, which exhibit male-to-female sex reversal. Nile tilapia fry from these three mutant lines were treated with 50 µg/g MT from 5 to 30 days after hatching (dah). The results showed that amhy and gsdf mutants, but not dmrt1 mutants, were masculinized by the MT treatment. Gonadal transcriptome analysis revealed that genes involved in steroidogenesis and germ cell development in MT-treated dmrt1 mutants exhibited a similar expression pattern to that of the wild type (WT) XX. In addition, the dmrt1 mutants cannot be masculinized by co-treatment with MT and the aromatase inhibitor fadrozole. The MT treatment completely blocked early steroidogenic enzyme (Star2, Cyp17a2, and Cyp19a1a) expression independent of amhy, gsdf, and dmrt1. A luciferase analysis showed that MT directly suppressed basal and Sf-1-activated cyp19a1a promoter activity through ara and arb in cultured HEK293 cells. Furthermore, MT treatment inhibited germ cell proliferation in amhy and gsdf mutants but not in dmrt1 mutants. Consistently, dmrt1 expression was induced in MT-treated WT XX, -amhy, and -gsdf mutants. Taken together, these results suggest that dmrt1 is indispensable for MT-induced masculinization in Nile tilapia and that MT functions by inhibiting early steroid synthesis and activating dmrt1 to promote testis development.


Sujet(s)
Androgènes , Cichlides , Méthyltestostérone , Facteurs de transcription , Animaux , Facteurs de transcription/génétique , Facteurs de transcription/métabolisme , Mâle , Cichlides/génétique , Cichlides/croissance et développement , Cichlides/métabolisme , Androgènes/métabolisme , Androgènes/pharmacologie , Méthyltestostérone/pharmacologie , Femelle , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Différenciation sexuelle/génétique , Mutation , Humains , Régulation de l'expression des gènes au cours du développement/effets des médicaments et des substances chimiques
5.
J Agric Food Chem ; 72(39): 21301-21317, 2024 Oct 02.
Article de Anglais | MEDLINE | ID: mdl-39297866

RÉSUMÉ

The marine environment is an excellent source for many physiologically active compounds due to its extensive biodiversity. Among these, fish proteins stand out for their unique qualities, making them valuable in a variety of applications due to their diverse compositional and functional properties. Utilizing fish and fish coproducts for the production of protein hydrolysates and bioactive peptides not only enhances their economic value but also reduces their potential environmental harm, if left unutilized. Fish protein hydrolysates (FPHs), known for their excellent nutritional value, favorable amino acid profiles, and beneficial biological activities, have generated significant interest for their potential health benefits. These hydrolysates contain bioactive peptides which are peptide sequences known for their beneficial physiological effects. These biologically active peptides play a role in metabolic regulation/modulation and are increasingly seen as promising ingredients in functional foods, nutraceuticals and pharmaceuticals, with potential to improve human health and prevent disease. This review aims to summarize the current in vitro, cell model (in situ) and in vivo research on the antioxidant, glycaemic management and muscle health enhancement properties of FPHs and their peptides.


Sujet(s)
Antioxydants , Protéines de poisson , Poissons , Protéines du muscle , Peptides , Hydrolysats de protéines , Hydrolysats de protéines/composition chimique , Animaux , Protéines de poisson/composition chimique , Protéines de poisson/métabolisme , Antioxydants/composition chimique , Antioxydants/pharmacologie , Humains , Peptides/composition chimique , Peptides/pharmacologie , Protéines du muscle/composition chimique , Protéines du muscle/métabolisme , Glucose/métabolisme , Glucose/composition chimique
6.
Genomics ; 116(5): 110934, 2024 Sep.
Article de Anglais | MEDLINE | ID: mdl-39236771

RÉSUMÉ

The south China carp (Cyprinus carpio rubrofuscus) is an indigenous and important fish species, widely cultured in south China. However, part of individuals experienced retarded growth, the genetic basis of which has yet to be elucidated. In this study, whole-genome resequencing of 35 fast-growing and 35 retarded-growing south China carp were conducted to identify promising genes associated with retarded growth. Twelve candidate SNPs were detected and annotated to the Gpr75 gene, which has been reported to be related with body weight through regulating insulin homeostasis. RNA-seq analysis of muscle suggested that differentially expressed genes were significantly enriched in the insulin signaling pathway. Additionally, the fasting serum insulin level was significantly lower while the blood glucose level was significantly higher in the retarded-growing group. Our preliminary study provides insights into the genetic basis underlying the retarded growth and may facilitate further genetic improvement of south China carp.


Sujet(s)
Carpes (poisson) , Protéines de poisson , Polymorphisme de nucléotide simple , Récepteurs couplés aux protéines G , Séquençage du génome entier , Animaux , Carpes (poisson)/génétique , Carpes (poisson)/croissance et développement , Carpes (poisson)/métabolisme , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Récepteurs couplés aux protéines G/génétique , Récepteurs couplés aux protéines G/métabolisme , RNA-Seq , Insuline/métabolisme , Insuline/sang , Insuline/génétique , Glycémie/métabolisme
7.
Elife ; 132024 Sep 30.
Article de Anglais | MEDLINE | ID: mdl-39347580

RÉSUMÉ

The incessant arms race between viruses and hosts has led to numerous evolutionary innovations that shape life's evolution. During this process, the interactions between viral receptors and viruses have garnered significant interest since viral receptors are cell surface proteins exploited by viruses to initiate infection. Our study sheds light on the arms race between the MDA5 receptor and 5'ppp-RNA virus in a lower vertebrate fish, Miichthys miiuy. Firstly, the frequent and independent loss events of RIG-I in vertebrates prompted us to search for alternative immune substitutes, with homology-dependent genetic compensation response (HDGCR) being the main pathway. Our further analysis suggested that MDA5 of M. miiuy and Gallus gallus, the homolog of RIG-I, can replace RIG-I in recognizing 5'ppp-RNA virus, which may lead to redundancy of RIG-I and loss from the species genome during evolution. Secondly, as an adversarial strategy, 5'ppp-RNA SCRV can utilize the m6A methylation mechanism to degrade MDA5 and weaken its antiviral immune ability, thus promoting its own replication and immune evasion. In summary, our study provides a snapshot into the interaction and coevolution between vertebrate and virus, offering valuable perspectives on the ecological and evolutionary factors that contribute to the diversity of the immune system.


Before the immune system can eliminate a bacterium, virus or other type of pathogen, it needs to be able to recognize these foreign elements. To achieve this, cells in the immune system have proteins called pattern recognition receptors (PRRs) which can identify distinct molecular features of certain pathogens. One specific group of PRRs is a family of retinoic acid-induced RIG-I-like receptors (RLRs), which help immune cells detect different types of viruses. Members of this family recognize distinct motifs on the genetic material of viruses known as RNA. For instance, RIG-I recognizes a marker known as 5'ppp on the end of single-stranded RNA molecules, whereas MDA5 recognizes long strands of double-stranded RNA. Many vertebrates ­ including various mammals, birds, and fish ­ lost the RIG-I receptor over the course of evolution. However, Geng et al. predicted that some animals lacking the RIG-I receptor may still be able to activate an immune response against viruses that contain the 5'ppp-RNA motif. To investigate this possibility, Geng et al. studied chickens and miiuy croakers (a type of ray-finned fish) which no longer have a RIG-I receptor. They found that both animals can still sense and eliminate two 5'ppp-RNA viruses called VSV and SCRV. Further experiments revealed that these two viruses are detected by a modified MDA5 receptor that had evolved to bind to 5'-ppp and activate the antiviral response. Viruses are also continuously evolving new ways to escape the immune system. This led Geng et al. to investigate whether SCRV, which causes serious harm to marine fish, has evolved a way to evade the MDA5 protection mechanism. Using miiuy croakers as a model, they found that SCRV causes the transcripts that produce the MDA5 protein to contain more molecules of m6a. This molecular tag degrades the transcript, leading to lower levels of MDA5, reducing the antiviral response against SCRV. The findings of Geng et al. offer valuable perspectives on how the immune system adapts over the course of evolution, and highlight the diversity of antiviral responses in vertebrates. Chickens and miiuy croakers are commonly farmed animals, and further work investigating how viruses invade these species could prevent illnesses from spreading and having a negative impact on the economy.


Sujet(s)
Protéine-58 à domaine DEAD , Hélicase IFIH1 inductrice de l'interféron , Animaux , Hélicase IFIH1 inductrice de l'interféron/métabolisme , Hélicase IFIH1 inductrice de l'interféron/génétique , Protéine-58 à domaine DEAD/métabolisme , Protéine-58 à domaine DEAD/génétique , Poissons/virologie , Poissons/génétique , Poissons/immunologie , Virus à ARN/génétique , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Évolution moléculaire
8.
Int J Mol Sci ; 25(18)2024 Sep 18.
Article de Anglais | MEDLINE | ID: mdl-39337521

RÉSUMÉ

Metabotropic glutamate receptor 4 (mGluR4) is widely regarded as an umami receptor activated by L-glutamate to exert essential functions. Numerous studies have shown that umami receptors participate in food intake regulation. However, little is known about mGluR4's role in mediating food ingestion and its possible molecular mechanism. Mandarin fish, a typical carnivorous fish, is sensitive to umami substances and is a promising vertebrate model organism for studying the umami receptor. In this study, we identified the mGluR4 gene and conducted evolutionary analyses from diverse fish species with different feeding habits. mGluR4 of mandarin fish was cloned and functionally expressed to investigate the effects of L-glutamate on mGluR4. We further explored whether the signal pathway mGluR4-Ca2+-ERK1/2 participates in the process in mandarin fish brain cells. The results suggest that L-glutamate could regulate Neuropeptide Y (Npy) via the mGluR4-Ca2+-ERK1/2 signaling pathway in mandarin fish. Our findings unveil the role of mGluR4 in feeding decisions and its possible molecular mechanisms in carnivorous fishes.


Sujet(s)
Protéines de poisson , Acide glutamique , Système de signalisation des MAP kinases , Neuropeptide Y , Récepteurs métabotropes au glutamate , Animaux , Séquence d'acides aminés , Calcium/métabolisme , Protéines de poisson/métabolisme , Protéines de poisson/génétique , Poissons/métabolisme , Poissons/génétique , Acide glutamique/métabolisme , Neuropeptide Y/métabolisme , Neuropeptide Y/génétique , Perciformes/métabolisme , Perciformes/génétique , Phylogenèse , Récepteurs métabotropes au glutamate/métabolisme , Récepteurs métabotropes au glutamate/génétique
9.
FASEB J ; 38(18): e70036, 2024 Sep 30.
Article de Anglais | MEDLINE | ID: mdl-39275940

RÉSUMÉ

Fatty acid-binding protein 1 (FABP1) plays an important role in regulating fatty acid metabolism in liver, which is a potential therapeutic target for diseases such as non-alcoholic fatty liver disease (NAFLD). However, the underlying mechanisms are not well defined. Using complementary experimental models, we discovered FABP1 induction in hepatocytes as a primary mediator of lipogenesis when exposed to fatty acids, especially saturated fatty acids (SFAs). In the feeding trial, palm oil led to excess lipid accumulation in the liver of large yellow croaker (Larimichthys crocea), accompanied by significant induction of FABP1. In cultured cells, palmitic acid (PA), a kind of SFA, triggered the fabp1 expression and increased triglyceride (TG) contents. Knockdown of FABP1 dampened PA-induced TG accumulation through mitigated lipogenesis. The overexpression of FABP1 showed the opposite result. Furthermore, the inactivation of FABP1 led to induction in insulin-induced gene 1 (INSIG1) expression, which attenuated the processing of sterol regulatory element-binding protein 1 (SREBP1) by down-regulating the nuclear-localized SREBP1. These results revealed a previously unrecognized function of FABP1 in response to PA, providing additional evidence for targeting FABP1 in the treatment of NAFLD caused by SFA.


Sujet(s)
Protéines de liaison aux acides gras , Hépatocytes , Lipogenèse , Perciformes , Protéine-1 de liaison à l'élément de régulation des stérols , Animaux , Hépatocytes/métabolisme , Protéine-1 de liaison à l'élément de régulation des stérols/métabolisme , Protéine-1 de liaison à l'élément de régulation des stérols/génétique , Perciformes/métabolisme , Perciformes/génétique , Protéines de liaison aux acides gras/génétique , Protéines de liaison aux acides gras/métabolisme , Triglycéride/métabolisme , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Stéatose hépatique non alcoolique/métabolisme , Stéatose hépatique non alcoolique/génétique , Acide palmitique/pharmacologie , Cellules cultivées
10.
Commun Biol ; 7(1): 1154, 2024 Sep 16.
Article de Anglais | MEDLINE | ID: mdl-39284885

RÉSUMÉ

Fish sex is largely influenced by steroid hormones, especially sex hormones. Here, we established a steroid hormone-free genetic model by mutation of cyp11a1 in Nile tilapia, which was confirmed by EIA assay. Gonadal phenotype and transcriptome analyses showed that the XX mutants displayed sex reversal from female to male but with defective spermatogenesis. Despite the sex reversal, the aromatase encoding gene cyp19a1a was continuously expressed in the gonads of the XX mutants, which might be caused by androgen deficiency. Whole-mount fluorescence in situ hybridization and transcriptome analysis showed that the gonads of the XX mutants firstly developed towards ovary but shifted to testis between 10 to 15 days after hatching. Detailed expression analysis of key sex differentiation pathway genes foxl3 and dmrt1 combined with apoptosis analysis revealed transdifferentiation of germ cells from female to male during sex reversal. Rescue experiments showed that both P5 and E2 treatment rescued the sex reversal of cyp11a1 mutant XX fish. Overall, our results revealed a transient ovary-like stage and transdifferentiation of germ cells from female to male in the early gonads of the steroid hormone-deprived cyp11a1 mutant XX fish.


Sujet(s)
Mutation , Ovaire , Différenciation sexuelle , Animaux , Femelle , Ovaire/métabolisme , Mâle , Différenciation sexuelle/génétique , Cholesterol side-chain cleavage enzyme/génétique , Cholesterol side-chain cleavage enzyme/métabolisme , Cichlides/génétique , Cichlides/métabolisme , Troubles du développement sexuel/génétique , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Hormones sexuelles stéroïdiennes/métabolisme , Tilapia/génétique , Tilapia/métabolisme , Processus de détermination du sexe/génétique
11.
Front Immunol ; 15: 1455457, 2024.
Article de Anglais | MEDLINE | ID: mdl-39301034

RÉSUMÉ

Chemokines are cytokines that mediate leukocyte traffic between the lymphoid organs, the bloodstream, and the site of tissue damage, which is essential for an efficient immune response. In particular, the gamma interferon (IFN- γ) inducible chemokines CXCL9, CXCL10, and CXCL11, and their receptor CXCR3, are involved in T cell and macrophage recruitment to the site of infection. The nature and function of these chemokines and their receptor are well-known in mammals, but further research is needed to achieve a similar level of understanding in fish immunity. Thus, in this study, we seek to identify the genes encoding the components of the Atlantic salmon (Salmo salar) CXCL9, CXCL10, CXCL11/CXCR3 axis (CXCL9-11/CXCR3), predict the protein structure from the amino acid sequence, and explore the regulation of gene expression as well as the response of these chemokines and their receptor to viral infections. The cxcl9, cxcl10, cxcl11, and cxcr3 gene sequences were retrieved from the databases, and the phylogenetic analysis was conducted to determine the evolutionary relationships. The study revealed an interesting pattern of clustering and conservation among fish and mammalian species. The salmon chemokine sequences clustered with orthologs from other fish species, while the mammalian sequences formed separate clades. This indicates a divergent evolution of chemokines between mammals and fish, possibly due to different evolutionary pressures. While the structural analysis of the chemokines and the CXCR3 receptor showed the conservation of critical motifs and domains, suggesting preserved functions and stability throughout evolution. Regarding the regulation of gene expression, some components of the CXCL9-11/CXCR3 axis are induced by recombinant gamma interferon (rIFN-γ) and by Infectious pancreatic necrosis virus (IPNV) infection in Atlantic salmon cells. Further studies are needed to explore the role of Atlantic salmon CXCL9-11 chemokines in regulating immune cell migration and endothelial activation, as seen in mammals. To the best of our knowledge, there have been no functional studies of chemokines to understand these effects in Atlantic salmon.


Sujet(s)
Chimiokine CXCL9 , Phylogenèse , Récepteurs CXCR3 , Salmo salar , Animaux , Salmo salar/immunologie , Salmo salar/génétique , Récepteurs CXCR3/génétique , Récepteurs CXCR3/métabolisme , Chimiokine CXCL9/génétique , Chimiokine CXCL9/métabolisme , Chimiokine CXCL9/immunologie , Régulation de l'expression des gènes , Chimiokine CXCL11/génétique , Chimiokine CXCL11/métabolisme , Protéines de poisson/génétique , Protéines de poisson/immunologie , Protéines de poisson/métabolisme , Maladies des poissons/immunologie , Maladies des poissons/virologie , Chimiokine CXCL10/génétique , Chimiokine CXCL10/métabolisme , Virus de la nécrose pancréatique infectieuse/immunologie
12.
Food Res Int ; 195: 114963, 2024 Nov.
Article de Anglais | MEDLINE | ID: mdl-39277235

RÉSUMÉ

This study aimed to investigate the effect of oxidation on fish gelatin and its emulsifying properties. Fish gelatin was oxidized with varying concentrations of H2O2 (0-30 mM). Increased concentrations of the oxidant led to a decrease in amino acids in the gelatin, including glycine, lysine, and arginine. Additionally, the relative content of ordered secondary structure and triple helix fractions decreased. Zeta potential decreased, while particle size, surface hydrophobicity, and water contact angle increased. Regarding emulsifying behavior, oxidation promoted the adsorption of gelatin to the oil-water interface and reduced interfacial tension. With increased degrees of oxidation, the zeta potential and size of the emulsion droplets decreased. The oxidized gelatin exhibited better emulsifying activity but worse emulsifying stability. Based on these results, a mechanism for how oxidation affects the emulsifying properties of gelatin was proposed: the increase in gelatin's hydrophobicity and the decrease in triple helix structure induced by oxidation reduced the interfacial tension at the oil-water interface. This promoted protein adsorption at the oil-water interface, allowing the formation of smaller oil droplets and enhancing gelatin's emulsifying activity. However, the decrease in electrostatic repulsion between emulsion droplets and the decrease in solution viscosity increased the flocculation and aggregation of oil droplets, ultimately weakening the emulsifying stability of gelatin.


Sujet(s)
Émulsions , Protéines de poisson , Gélatine , Interactions hydrophobes et hydrophiles , Oxydoréduction , Gélatine/composition chimique , Émulsions/composition chimique , Animaux , Protéines de poisson/composition chimique , Taille de particule , Peroxyde d'hydrogène/composition chimique , Viscosité , Acides aminés/composition chimique , Tension superficielle , Émulsifiants/composition chimique , Poissons , Adsorption , Structure secondaire des protéines
13.
Biomolecules ; 14(9)2024 Sep 12.
Article de Anglais | MEDLINE | ID: mdl-39334917

RÉSUMÉ

The original UT-1 transporter gene was initially identified in the spiny dogfish (Squalus acanthias), but localization of the UT-1 protein was not determined. Subsequent UT-1 expression was shown to localize to the collecting tubule (CT) of the shark nephron in other shark species, with expression in a closely related chimaera species also located additionally at a lower level in the intermediate-I segment (IS-I) of the nephron. In spiny dogfish, two UT-1 splice variants are known (UT-1 long and short), and there was also a second UT-1 gene described (here termed Brain UT). In this study, a second splice variant of the second Brain UT gene was discovered. Expression profiles (mRNA) of UT-1 long and short and Brain UT were determined in a number of spiny dogfish tissues. Quantitative PCR in kidney samples showed that the level of the short variant of UT-1 was around 100 times higher than the long variant, which was itself expressed around 10 times higher than Brain UT cDNA/mRNA (in kidney). For the long variant, there was a significantly higher level of mRNA abundance in fish acclimatized to 75% seawater. Ultimately, three UT-1 antibodies were made that could bind to both the UT-1 short and long variant proteins. The first two of these showed bands of appropriate sizes on Western blots of around 52.5 and 46 kDa. The second antibody had some additional lower molecular weight bands. The third antibody was mainly bound to the 46 kDa band with faint 52.5 kDa staining. Both the 52.5 and 46 kDa bands were absent when the antibodies were pre-blocked with the peptide antigens used to make them. Across the three antibodies, there were many similarities in localization but differences in subcellular localization. Predominantly, antibody staining was greatest in the intermediate segment 1 (IS-I) and proximal (PIb) segments of the first sinus zone loop of the nephron, with reasonably strong expression also found at the start and middle of the late distal tubule (LDT; second sinus zone loop). While some expression in the collecting tubule (CT) could not be ruled out, the level of staining seemed to be low or non-existent in convoluted bundle zone nephron segments such as the CT. Hence, this suggests that spiny dogfish have a fundamentally different mode of urea absorption in comparison to that found in other shark species, potentially focused more on the nephron sinus zone loops than the CT.


Sujet(s)
Protéines de transport membranaire , Squalus acanthias , Animaux , Squalus acanthias/métabolisme , Squalus acanthias/génétique , Protéines de transport membranaire/métabolisme , Protéines de transport membranaire/génétique , Requins/métabolisme , Requins/génétique , ARN messager/métabolisme , ARN messager/génétique , , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Séquence d'acides aminés , Encéphale/métabolisme
14.
Genes (Basel) ; 15(9)2024 Sep 16.
Article de Anglais | MEDLINE | ID: mdl-39336802

RÉSUMÉ

Background/Objectives: Stearoyl-coenzyme A desaturase 1 (SCD1) plays a crucial role in fatty acid metabolism. However, its roles in the feeding habit transformation of mandarin fish (Siniperca chuatsi) remain largely unknown. Methods: Juvenile mandarin fish (10.37 ± 0.54)g were trained to feed on an artificial diet and then divided into artificial diet feeders and nonfeeders according to their feed preference. Afterwards, the scd1 gene of mandarin fish (Sc-scd1) was identified and characterized, and its transcription difference was determined between S. chuatsi fed live artificial diets and those fed prey fish. Results: Our results show that Sc-scd1 coding sequence is 1002 bp long, encoding 333 amino acids. The assumed Sc-SCD1 protein lacks a signal peptide, and it contains 1 N-linked glycosylation site, 24 phosphorylation sites, 4 transmembrane structures, and 3 conserved histidine elements. We found that Sc-SCD1 exhibits a high similarity with its counterparts in other fish by multiple alignments and phylogenetic analysis. The expression level of Sc-scd1 was detected with different expression levels in all tested tissues between male and female individuals fed either live prey fish or artificial diets. Conclusions: In particular, the Sc-scd1 expression level was the highest in the liver of both male and female mandarin fish fed artificial diets, indicating that scd1 genes may be associated with feed adaption of mandarin fish. Taken together, our findings offer novel perspectives on the potential roles of scd1 in specific domestication, and they provide valuable genetic information on feeding habits for the domestication of mandarin fish.


Sujet(s)
Clonage moléculaire , Protéines de poisson , Acyl-(acyl-carrier-protein)desaturase , Animaux , Acyl-(acyl-carrier-protein)desaturase/génétique , Acyl-(acyl-carrier-protein)desaturase/métabolisme , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Femelle , Mâle , Régime alimentaire/médecine vétérinaire , Aliment pour animaux , Phylogenèse , Perciformes/génétique , Perciformes/métabolisme , Comportement alimentaire
15.
Fish Shellfish Immunol ; 153: 109876, 2024 Oct.
Article de Anglais | MEDLINE | ID: mdl-39236861

RÉSUMÉ

Interleukin-8 (IL-8), a CXC chemokine, exerts pivotal effect on cell migration, inflammatory response, and immune regulation. In this study, we examined the immunological characteristics of an IL-8 like homologue (PoIL8-L) in Japanese flounder (Paralichthys olivaceus). PoIL8-L contains a conserved chemokine CXC domain and 105 amino acid residues. PoIL8-L expression in tissues was constitutive, and significantly regulated by V. havieri or E. tarda infection. In vitro, rPoIL8-L could bind to eight tested bacteria, exhibited bacteriostatic and bactericidal effects against certain bacteria, and could bind to the targeted bacterial Ⅳ pilin protein rPilA of E. tarda. Furthermore, rPoIL8-L could attach to peripheral blood leukocytes, and enhance their immune genes expression, respiratory burst, chemotaxis, proliferation, acid phosphatase activity, and phagocytic activity. Additionally, rPoIL8-L induce neutrophils to extrude neutrophil extracellular traps. In vivo, rPoIL8-L could promote host resistance to E. tarda infection. In summary, these findings provide fresh perspectives on the immunological antibacterial properties of IL-8 in teleost.


Sujet(s)
Edwardsiella tarda , Infections à Enterobacteriaceae , Maladies des poissons , Protéines de poisson , Poissons plats , Immunité innée , Interleukine-8 , Leucocytes , Animaux , Maladies des poissons/immunologie , Protéines de poisson/immunologie , Protéines de poisson/génétique , Edwardsiella tarda/physiologie , Leucocytes/immunologie , Interleukine-8/génétique , Interleukine-8/immunologie , Poissons plats/immunologie , Infections à Enterobacteriaceae/immunologie , Infections à Enterobacteriaceae/médecine vétérinaire , Régulation de l'expression des gènes/immunologie , Vibrio/physiologie , Séquence d'acides aminés , Phylogenèse , Iridoviridae/physiologie , Alignement de séquences/médecine vétérinaire , Analyse de profil d'expression de gènes/médecine vétérinaire
16.
J Agric Food Chem ; 72(38): 21122-21135, 2024 Sep 25.
Article de Anglais | MEDLINE | ID: mdl-39269985

RÉSUMÉ

Protein glutaminases (PG; EC = 3.5.1.44) are enzymes known for enhancing protein functionality. In this study, we cloned and expressed the gene chryb3 encoding protein glutaminase PG3, exhibiting 39.4 U/mg specific activity. Mature-PG3 featured a substrate channel surrounded by aromatic and hydrophobic amino acids at positions 38-45 and 78-84, with Val81 playing a pivotal role in substrate affinity. The dynamic opening and closing motions between Gly65, Thr66, and Cys164 at the catalytic cleft greatly influence substrate binding and product release. Redesigning catalytic pocket and cocatalytic region produced combinatorial mutant MT6 showing a 2.69-fold increase in specific activity and a 2.99-fold increase at t65 °C1/2. Furthermore, MT6 boosted fish myofibrillar protein (MP) solubility without NaCl. Key residues such as Thr3, Asn54, Val81, Tyr82, Asn107, and Ser108 were vital for PG3-myosin interaction, particularly Asn54 and Asn107. This study sheds light on the catalytic mechanism of PG3 and guided its rational engineering and utilization in low-salt fish MP product production.


Sujet(s)
Protéines de poisson , Glutaminase , Myofibrilles , Ingénierie des protéines , Glutaminase/métabolisme , Glutaminase/génétique , Glutaminase/composition chimique , Animaux , Protéines de poisson/génétique , Protéines de poisson/composition chimique , Protéines de poisson/métabolisme , Myofibrilles/composition chimique , Myofibrilles/métabolisme , Myofibrilles/génétique , Protéines du muscle/génétique , Protéines du muscle/composition chimique , Protéines du muscle/métabolisme , Cinétique
17.
J Agric Food Chem ; 72(39): 21731-21740, 2024 Oct 02.
Article de Anglais | MEDLINE | ID: mdl-39298279

RÉSUMÉ

ß-Enolase is a cross-allergen commonly found in fungi, plants, and aquatic products. Although studies on the allergenicity of fish enolase have been reported in recent years, they are still limited to a few species of marine fish. Therefore, the detection of freshwater fish in the food industry requires more studies of the molecular characterization as well as the allergenicity of enolase. In this study, the nucleotide sequence of ß-enolase from grass carp was obtained by molecular cloning technology. Structural domain analysis showed that it contained the characteristic structural domains of the enolase superfamily, and homology analysis indicated that enolases are highly conserved evolutionarily. Recombinant ß-enolase was obtained by prokaryotic expression, and its allergenicity was assessed by ß-enolase-sensitized mice, which confirmed the ability of ß-enolase to trigger an allergic response and cause a rise in Th1 and Th2 immune responses in mice. These results suggest that ß-enolase could be used as a characterizing substance for the detection of fish allergens in the food industry as well as the preparation of drugs for allergy-related studies.


Sujet(s)
Allergènes , Carpes (poisson) , Clonage moléculaire , Protéines de poisson , Enolase , Animaux , Carpes (poisson)/immunologie , Carpes (poisson)/génétique , Enolase/immunologie , Enolase/génétique , Enolase/composition chimique , Allergènes/immunologie , Allergènes/génétique , Allergènes/composition chimique , Souris , Protéines de poisson/immunologie , Protéines de poisson/génétique , Protéines de poisson/composition chimique , Souris de lignée BALB C , Femelle , Séquence d'acides aminés , Expression des gènes , Humains , Hypersensibilité alimentaire/immunologie , Alignement de séquences
18.
Mol Biol Rep ; 51(1): 990, 2024 Sep 17.
Article de Anglais | MEDLINE | ID: mdl-39287730

RÉSUMÉ

BACKGROUND: Oxidative stress, a condition characterized by excessive production of reactive oxygen species (ROS), can cause significant damage to cellular macromolecules, leading to neurodegeneration. This underscores the need for effective antioxidant therapies that can mitigate oxidative stress and its associated neurodegenerative effects. KC14 peptide derived from liver-expressed antimicrobial peptide-2 A (LEAP 2 A) from Cyprinus carpio L. has been identified as a potential therapeutic agent. This study focuses on the antioxidant and neuroprotective properties of the KC14 peptide is to evaluate its effectiveness against oxidative stress and neurodegeneration. METHODS: The antioxidant capabilities of KC14 were initially assessed through in silico docking studies, which predicted its potential to interact with oxidative stress-related targets. Subsequently, the peptide was tested at concentrations ranging from 5 to 45 µM in both in vitro and in vivo experiments. In vivo studies involved treating H2O2-induced zebrafish larvae with KC14 peptide to analyze its effects on oxidative stress and neuroprotection. RESULTS: KC14 peptide showed a protective effect against the developmental malformations caused by H2O2 stress, restored antioxidant enzyme activity, reduced neuronal damage, and lowered lipid peroxidation and nitric oxide levels in H2O2-induced larvae. It enhanced acetylcholinesterase activity and significantly reduced intracellular ROS levels (p < 0.05) dose-dependently. Gene expression studies showed up-regulation of antioxidant genes with KC14 treatment under H2O2 stress. CONCLUSIONS: This study highlights the potent antioxidant activity of KC14 and its ability to confer neuroprotection against oxidative stress can provide a novel therapeutic agent for combating neurodegenerative diseases induced by oxidative stress.


Sujet(s)
Antioxydants , Carpes (poisson) , Peroxyde d'hydrogène , Neuroprotecteurs , Stress oxydatif , Espèces réactives de l'oxygène , Danio zébré , Animaux , Stress oxydatif/effets des médicaments et des substances chimiques , Antioxydants/pharmacologie , Antioxydants/métabolisme , Carpes (poisson)/métabolisme , Neuroprotecteurs/pharmacologie , Espèces réactives de l'oxygène/métabolisme , Peroxyde d'hydrogène/métabolisme , Maladies neurodégénératives/métabolisme , Maladies neurodégénératives/traitement médicamenteux , Peroxydation lipidique/effets des médicaments et des substances chimiques , Simulation de docking moléculaire , Protéines de poisson/pharmacologie , Protéines de poisson/métabolisme , Protéines de poisson/génétique , Peptides antimicrobiens cationiques/pharmacologie , Peptides antimicrobiens cationiques/métabolisme , Peptides/pharmacologie , Monoxyde d'azote/métabolisme , Larve/effets des médicaments et des substances chimiques , Larve/métabolisme
19.
BMC Genomics ; 25(1): 848, 2024 Sep 09.
Article de Anglais | MEDLINE | ID: mdl-39251938

RÉSUMÉ

BACKGROUND: Temperature is a crucial environmental determinant for the vitality and development of teleost fish, yet the underlying mechanisms by which they sense temperature fluctuations remain largely unexplored. Transient receptor potential (TRP) proteins, renowned for their involvement in temperature sensing, have not been characterized in teleost fish, especially regarding their temperature-sensing capabilities. RESULTS: In this study, a genome-wide analysis was conducted, identifying a total of 28 TRP genes in the mandarin fish Siniperca chuatsi. These genes were categorized into the families of TRPA, TRPC, TRPP, TRPM, TRPML, and TRPV. Despite notable variations in conserved motifs across different subfamilies, TRP family members shared common structural features, including ankyrin repeats and the TRP domain. Tissue expression analysis showed that each of these TRP genes exhibited a unique expression pattern. Furthermore, examination of the tissue expression patterns of ten selected TRP genes following exposure to both high and low temperature stress indicated the expression of TRP genes were responsive to temperatures changes. Moreover, the expression profiles of TRP genes in response to mandarin fish virus infections showed significant upregulation for most genes after Siniperca chuatsi rhabdovirus, mandarin fish iridovirus and infectious spleen and kidney necrosis virus infection. CONCLUSIONS: This study characterized the TRP family genes in mandarin fish genome-wide, and explored their expression patterns in response to temperature stress and virus infections. Our work will enhance the overall understanding of fish TRP channels and their possible functions.


Sujet(s)
Perciformes , Phylogenèse , Canaux cationiques TRP , Animaux , Canaux cationiques TRP/génétique , Canaux cationiques TRP/métabolisme , Perciformes/génétique , Perciformes/métabolisme , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Analyse de profil d'expression de gènes , Famille multigénique , Génome , Température , Infections à virus à ADN/génétique , Infections à virus à ADN/médecine vétérinaire , Maladies des poissons/génétique , Maladies des poissons/virologie , Régulation de l'expression des gènes , Iridoviridae
20.
Mol Genet Genomics ; 299(1): 88, 2024 Sep 24.
Article de Anglais | MEDLINE | ID: mdl-39313603

RÉSUMÉ

Nanog is a crucial regulatory factor in maintaining the self-renewal and pluripotency of embryonic stem cells. It is involved in various biological processes, such as early embryonic development, cell reprogramming, cell cycle regulation, the proliferation and migration of primordial germ cells. While research on this gene has primarily focused on mammals, there has been a growing interest in studying nanog in fish. However, there is a notable lack of comprehensive reviews regarding this gene in fish, which is essential for guiding future research. This review aims to provide a thorough summary of the gene's structure, expression patterns, functions and regulatory mechanisms in fish. The findings suggest that nanog probably has both conserved and divergent functions in regulating cell pluripotency, early embryonic development, and germ cell development in teleosts compared to other species, including mammals. These insights lay the foundation for future research and applications of the nanog gene, providing a new perspective for understanding the evolution and conserved charactristics of teleost nanog.


Sujet(s)
Protéines de poisson , Poissons , Protéine homéotique Nanog , Animaux , Développement embryonnaire/génétique , Cellules souches embryonnaires/métabolisme , Évolution moléculaire , Protéines de poisson/génétique , Protéines de poisson/métabolisme , Poissons/génétique , Régulation de l'expression des gènes au cours du développement , Protéine homéotique Nanog/génétique , Protéine homéotique Nanog/métabolisme , Cellules souches pluripotentes/métabolisme
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