Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 91
Filtrar
1.
Sci Data ; 11(1): 902, 2024 Aug 20.
Artigo em Inglês | MEDLINE | ID: mdl-39164259

RESUMO

The mariculture industry has seen a rapid expansion in recent years due to the increasing global demand for seafood. However, the industry faces challenges from climate change and increased pathogen pressure. Additionally, the chemicals used to enhance mariculture productivity are changing ocean ecosystems. This study analyzed 36 surface-water metagenomes from South Korean mussel, oyster, scallop, and shrimp farms to expand our understanding of aquaculture microbial genetic resources and the potential impacts of these anthropogenic inputs. We recovered 240 non-redundant species-level metagenome-assembled genomes (MAGs), comprising 224 bacteria, 13 archaea, and three eukaryotes. Most MAGs were assigned to Proteobacteria, Bacteroidota, and Actinobacteriota, with 40.7% remaining unclassified at the species level. Among the three eukaryotic MAGs, one was identified as a novel lineage of green algae, highlighting the uncharacterized genetic diversity in mariculture environments. Additionally, 22 prokaryotic MAGs harbored 26 antibiotic and metal resistance genes, with MAGs carrying beta-lactamases being particularly prevalent in most farms. The obtained microbiome data from mariculture environments can be utilized in future studies to foster healthy, sustainable mariculture practices.


Assuntos
Aquicultura , Metagenoma , República da Coreia , Animais , Bactérias/genética , Bactérias/classificação , Microbiota , Ostreidae/microbiologia , Archaea/genética , Pectinidae/microbiologia , Pectinidae/genética , Penaeidae/microbiologia , Penaeidae/genética
2.
J Hazard Mater ; 476: 135247, 2024 Sep 05.
Artigo em Inglês | MEDLINE | ID: mdl-39029196

RESUMO

Azaspiracids (AZAs) are lipid biotoxins produced by the marine dinoflagellates Azadinium and Amphidoma spp. that can accumulate in shellfish and cause food poisoning in humans. However, the mechanisms underlying the tolerance of shellfish to high levels of such toxins remain poorly understood. This study investigated the combined effects of detoxification metabolism and stress-related responses in scallops Chlamys farreri exposed to AZA. Scallops accumulated a maximum of 361.81 µg AZA1 eq/kg and 41.6 % AZA residue remained after 21 days of exposure. A range of AZA2 metabolites, including AZA19, AZA11, and AZA23, and trace levels of AZA2-GST, were detected. Total hemocyte counts significantly increased and ROS levels remained consistently high until gradually decreasing. Immune system activation mediated mitochondrial dysfunction and severe energy deficiency. DEGs increased over time, with key genes CYP2J6 and GPX6 contributing to AZA metabolism. These transcriptome and metabolic results identify the regulation of energy metabolism pathways, including inhibition of the TCA cycle and activation of carbohydrates, amino acids, and lipids. AZA also induced autophagy through the MAPK-AMPK signaling pathways, and primary inhibited PI3K/AKT to decrease mTOR pathway expression. Our results provide additional insights into the resistance of C. farreri to AZA, characterized by re-establishing redox homeostasis toward a more oxidative state.


Assuntos
Toxinas Marinhas , Pectinidae , Compostos de Espiro , Animais , Toxinas Marinhas/toxicidade , Compostos de Espiro/toxicidade , Pectinidae/efeitos dos fármacos , Pectinidae/metabolismo , Pectinidae/imunologia , Espécies Reativas de Oxigênio/metabolismo , Metabolismo Energético/efeitos dos fármacos , Transcriptoma/efeitos dos fármacos , Toxinas de Poliéter
3.
Fish Shellfish Immunol ; 151: 109743, 2024 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-38964433

RESUMO

Adenosine Deaminases Acting on RNA (ADARs) are evolutionarily conserved enzymes known to convert adenosine to inosine in double-stranded RNAs and participate in host-virus interactions. Conducting a meta-analysis of available transcriptome data, we identified and characterised eight ADAR transcripts in Chlamys farreri, a farmed marine scallop susceptible to Acute viral necrosis virus (AVNV) infections and mortality outbreaks. Accordingly, we identified six ADAR genes in the Zhikong scallop genome, revised previous gene annotations, and traced alternative splicing variants. In detail, each ADAR gene encodes a unique combination of functional domains, always including the Adenosine deaminase domain, RNA binding domains and, in one case, two copies of a Z-DNA binding domain. After phylogenetic analysis, five C. farreri ADARs clustered in the ADAR1 clade along with sequences from diverse animal phyla. Gene expression analysis indicated CF051320 as the most expressed ADAR, especially in the eye and male gonad. The other four ADAR1 genes and one ADAR2 gene exhibited variable expression levels, with CF105370 and CF051320 significantly increasing during early scallop development. ADAR-mediated single-base editing, evaluated across adult C. farreri tissues and developmental stages, was mainly detectable in intergenic regions (83 % and 85 %, respectively). Overall, the expression patterns of the six ADAR genes together with the editing and hyper-editing values computed on scallops RNA-seq samples support the adaptive value of ADAR1-mediated editing, particularly in the pre-settling larval stages.


Assuntos
Adenosina Desaminase , Pectinidae , Filogenia , Edição de RNA , Animais , Adenosina Desaminase/genética , Adenosina Desaminase/metabolismo , Pectinidae/genética , Pectinidae/imunologia , Imunidade Inata/genética , Perfilação da Expressão Gênica , Regulação da Expressão Gênica/imunologia , Sequência de Aminoácidos , Transcriptoma , Alinhamento de Sequência/veterinária
4.
Int J Biol Macromol ; 275(Pt 1): 133645, 2024 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-38964686

RESUMO

Fas-associated protein with death domain (FADD) was initially identified as a crucial adaptor protein in the apoptotic pathway mediated by death receptor (DR). Subsequently, many studies have confirmed that FADD plays a vital role in innate immunity and inflammatory responses in animals. However, the function of this pleiotropic molecule in mollusk species has not been well explored. In this study, we successfully verified the gene sequence of FADD in the Zhikong scallop (Chlamys farreri) and designated it as CfFADD. The CfFADD protein contains a conserved death effector and death domains. Phylogenetic analysis showed that CfFADD is a novel addition to the molluscan FADD family with a close evolutionary relationship with molluscan FADD subfamily proteins. CfFADD mRNA expression in various scallop tissues was significantly induced by challenge with pathogen-associated molecular patterns (lipopolysaccharide, peptidoglycan, and poly(I:C)), suggesting its role in innate immunity in scallops. Co-immunoprecipitation showed that CfFADD interacted with the scallop DR (tumor necrosis factor receptor) and a signaling molecule involved in the Toll-like receptor pathway (interleukin-1 receptor-associated kinase), confirming that CfFADD may be involved in DR-mediated apoptosis and innate immune signaling pathways. Further studies showed that CfFADD interacted with CfCaspase-8 and activated caspase-3. HEK293T cells exhibited distinct apoptotic features after transfection with a CfFADD-expression plasmid, suggesting a functional DR-FADD-caspase apoptotic pathway in scallops. Overexpression of CfFADD led to a significant dose-dependent activation of interferon ß and nuclear factor-κB reporter genes, demonstrating the key role of CfFADD in innate immunity. In summary, our research has confirmed the critical roles of CfFADD in innate immunity and apoptosis and provides valuable information for developing comparative immunology theories.


Assuntos
Apoptose , Proteína de Domínio de Morte Associada a Fas , Imunidade Inata , Transdução de Sinais , Animais , Humanos , Sequência de Aminoácidos , Proteína de Domínio de Morte Associada a Fas/metabolismo , Proteína de Domínio de Morte Associada a Fas/genética , Regulação da Expressão Gênica , Moluscos/imunologia , Moluscos/genética , Pectinidae/imunologia , Pectinidae/genética , Filogenia
5.
Dev Comp Immunol ; 159: 105227, 2024 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-38986890

RESUMO

Calcium/calmodulin dependent protein kinase kinase (CaMKK), a highly conserved protein kinase, is involved in the downstream processes of various biological activities by phosphorylating and activating 5'-AMP-activated protein kinase (AMPK) in response to the increase of cytosolic-free calcium (Ca2+). In the present study, a CaMKKI was identified from Yesso scallop Patinopecten yessoensis. Its mRNA was ubiquitously expressed in haemocytes and all tested tissues with the highest expression level in mantle. The expression level of PyCaMKKI mRNA in adductor muscle was significantly upregulated at 1, 3 and 6 h after high temperature treatment (25 °C), which was 3.43-fold (p < 0.05), 5.25-fold (p < 0.05), and 5.70-fold (p < 0.05) of that in blank group, respectively. At 3 h after high temperature treatment (25 °C), the protein level of PyAMPKα, as well as the phosphorylation level of PyAMPKα at Thr170 in adductor muscle, and the positive co-localized fluorescence signals of PyCaMKKI and PyAMPKα in haemocyte all increased significantly (p < 0.05) compared to blank group (18 °C). The pull-down assay showed that rPyCaMKKI and rPyAMPKα could bind each other in vitro. After PyCaMKKI was silenced by siRNA, the mRNA and protein levels of PyCaMKKI and PyAMPKα, and the phosphorylation level of PyAMPKα at Thr170 in adductor muscle were significantly down-regulated (p < 0.05) compared with the negative control group receiving an injection of siRNA-NC. These results collectively suggested that PyCaMKKI was involved in the activation of PyAMPKα in response to high temperature stress and would be helpful for understanding the function of PyCaMKKI-PyAMPKα pathway in maintaining energy homeostasis under high temperature stress in scallops.


Assuntos
Proteínas Quinases Ativadas por AMP , Quinase da Proteína Quinase Dependente de Cálcio-Calmodulina , Pectinidae , Animais , Pectinidae/imunologia , Pectinidae/genética , Proteínas Quinases Ativadas por AMP/metabolismo , Proteínas Quinases Ativadas por AMP/genética , Quinase da Proteína Quinase Dependente de Cálcio-Calmodulina/metabolismo , Quinase da Proteína Quinase Dependente de Cálcio-Calmodulina/genética , Fosforilação , Resposta ao Choque Térmico , Hemócitos/metabolismo , RNA Interferente Pequeno/genética , Temperatura Alta , Estresse Fisiológico
6.
Ultrason Sonochem ; 107: 106935, 2024 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-38850642

RESUMO

Myofibrillar proteins (MPs) have a notable impact on the firmness and flexibility of gel-based products. Therefore, enhancing the gelation and emulsification properties of scallop MPs is of paramount significance for producing high-quality scallop surimi products. In this study, we investigated the effects of high-intensity ultrasound on the physicochemical and gelation properties of MPs from bay scallops (Argopecten irradians). The carbonyl content of MPs significantly increased with an increase in ultrasound power (150, 350, and 550 W), indicating ultrasound-induced MP oxidation. Meanwhile, high-intensity ultrasound treatment (550 W) enhanced the emulsifying capacity and the short-term stability of MPs (up to 72.05 m2/g and 153.05 min, respectively). As the ultrasound power increased, the disulfide bond content and surface hydrophobicity of MPs exhibited a notable increase, indicating conformational changes in MPs. Moreover, in the secondary structure of MPs, the α-helix content significantly decreased, whereas the ß-sheet content increased, thereby suggesting the ultrasound-induced stretching and flexibility of MP molecules. Sodium-dodecyl sulfate-polyacrylamide gel electrophoresis and scanning electron microscopy analysis further elucidated that high-intensity ultrasound induced MP oxidation, leading to modification of amino acid side chains, intra- and intermolecular cross-linking, and MP aggregation. Consequently, high-intensity ultrasound treatment was found to augment the viscoelasticity, gel strength, and water-holding capacity of MP gels, because ultrasound treatment facilitated the formation of a stable network structure in protein gels. Thus, this study offers theoretical insights into the functional modification of bay scallop MPs and the processing of its surimi products.


Assuntos
Géis , Proteínas Musculares , Pectinidae , Pectinidae/química , Animais , Géis/química , Proteínas Musculares/química , Ondas Ultrassônicas , Fenômenos Químicos , Interações Hidrofóbicas e Hidrofílicas , Emulsões/química
7.
Toxins (Basel) ; 16(6)2024 May 27.
Artigo em Inglês | MEDLINE | ID: mdl-38922142

RESUMO

Previous studies have shown that feeding mice with food containing mantle tissue from Japanese scallops results in aggravated liver and kidney damage, ultimately resulting in mortality within weeks. The aim of this study is to evaluate the toxicity of scallop mantle in China's coastal areas and explore the impact of scallop mantle toxins (SMT) on intestinal barrier integrity and gut microbiota in mice. The Illumina MiSeq sequencing of V3-V4 hypervariable regions of 16S ribosomal RNA was employed to study the alterations in gut microbiota in the feces of SMT mice. The results showed that intestinal flora abundance and diversity in the SMT group were decreased. Compared with the control group, significant increases were observed in serum indexes related to liver, intestine, inflammation, and kidney functions among SMT-exposed mice. Accompanied by varying degrees of tissue damage observed within these organs, the beneficial bacteria of Muribaculaceae and Marinifilaceae significantly reduced, while the harmful bacteria of Enterobacteriaceae and Helicobacter were significantly increased. Taken together, this article elucidates the inflammation and glucose metabolism disorder caused by scallop mantle toxin in mice from the angle of gut microbiota and metabolism. SMT can destroy the equilibrium of intestinal flora and damage the intestinal mucosal barrier, which leads to glucose metabolism disorder and intestinal dysfunction and may ultimately bring about systemic toxicity.


Assuntos
Microbioma Gastrointestinal , Mucosa Intestinal , Pectinidae , Animais , Microbioma Gastrointestinal/efeitos dos fármacos , Pectinidae/microbiologia , Mucosa Intestinal/efeitos dos fármacos , Mucosa Intestinal/microbiologia , Mucosa Intestinal/metabolismo , Camundongos , Toxinas Marinhas/toxicidade , Masculino , Bactérias/efeitos dos fármacos , Bactérias/genética , Intestinos/microbiologia , Intestinos/efeitos dos fármacos , Fezes/microbiologia , RNA Ribossômico 16S/genética , Função da Barreira Intestinal
8.
Fish Shellfish Immunol ; 151: 109697, 2024 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-38871139

RESUMO

Myeloid differentiation factor-88 (MyD88) is a key adaptor of the toll-like receptor (TLR) signaling pathway and plays a crucial role in innate immune signal transduction in animals. However, the MyD88-mediated signal transduction mechanism in shellfish has not been well studied. In this study, a new MyD88 gene, CfMyD88-2, was identified in the Zhikong scallop, Chlamys farreri. The 1779 bp long open reading frame encodes 592 amino acids. The N-terminus of CfMyD88-2 contains a conserved death domain (DD), followed by a TIR (TLR/Interleukin-1 Receptor) domain. The results of the multi-sequence comparison showed that the TIR domain sequences were highly conserved. Phylogenetic analysis revealed that CfMyD88-2 was first associated with Mizuhopecten yessoensis MyD88-4 and Argopecten irradians MyD88-4. CfMyD88-2 mRNA was expressed in all scallop tissues, as detected by qRT-PCR, and the expression level was the highest in the mantle and hepatopancreas. In addition, CfMyD88-2 mRNA expression significantly increased after pathogen-associated molecular patterns (PAMPs, such as lipopolysaccharide, peptidoglycan, or polyinosinic-polycytidylic acid) stimulation. The results of the co-immunoprecipitation experiments in HEK293T cells showed that both CfMyD88-1 and CfMyD88-2 interacted with the TLR protein of scallops, suggesting the existence of more than one functional TLR-MyD88 signaling axis in scallops. Dual luciferase reporter gene assays indicated that the overexpressed CfMyD88-2 in HEK293T cells activated interferon (IFN) α, IFN-ß, IFN-γ, and NF-κB reporter genes, indicating that the protein has multiple functions. The results of the subcellular localization experiment uncovered that CfMyD88-2 was mainly localized in the cytoplasm of human cells. In summary, the novel identified CfMyD88-2 can respond to the challenge of PAMPs, participate in TLR immune signaling, and may activate downstream effector genes such as NF-κB gene. These research results will be useful in advancing the theory of innate immunity in invertebrates and provide a reference for the selection of disease-resistant scallops in the future.


Assuntos
Sequência de Aminoácidos , Regulação da Expressão Gênica , Imunidade Inata , Fator 88 de Diferenciação Mieloide , Pectinidae , Filogenia , Alinhamento de Sequência , Receptores Toll-Like , Animais , Imunidade Inata/genética , Fator 88 de Diferenciação Mieloide/genética , Fator 88 de Diferenciação Mieloide/imunologia , Fator 88 de Diferenciação Mieloide/metabolismo , Pectinidae/imunologia , Pectinidae/genética , Receptores Toll-Like/genética , Receptores Toll-Like/imunologia , Receptores Toll-Like/química , Alinhamento de Sequência/veterinária , Regulação da Expressão Gênica/imunologia , Perfilação da Expressão Gênica/veterinária , Transdução de Sinais/imunologia , Humanos , Células HEK293 , Sequência de Bases
9.
J Food Sci ; 89(7): 4047-4063, 2024 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-38778558

RESUMO

Scallops are rich in eicosapentaenoic acid (EPA) and docosahexaenoic acid but perishable due to their microbial growth and lipid oxidation. In this study, gelatin/dextran films containing cinnamaldehyde and α-tocopherol (0% + 0%, 0.3% + 0.3%, 0.6% + 0.6%, 0.9% + 0.9%, and 1.2% + 1.2%, w/w) as active fillers were developed by solution casting method, and their preservation effects on scallop adductor muscle refrigerated at 4°C for 0, 3, 6, 9, and 12 days were evaluated. Inclusion of the two active fillers did not influence the thermal stability of the films but created heterogenous and discontinuous film microstructure and increased the film hydrophobicity. Increase in the concentrations of active fillers lowered the mechanical properties and water vapor permeability of the films but increased their crystallinity, thickness, water contact angle, opacity, antibacterial property, and antioxidant property. The longest release times for both cinnamaldehyde and α-tocopherol were found in 95% (v/v) ethanol solution. The gelatin/dextran films containing 1.2% (w/w) of active fillers (Gelatin [Ge]/Dextran [Dx]/1.2 film) improved the chemical stability of refrigerated scallop adductor muscle. The total viable count (TVC) of the unpackaged scallop adductor muscle exceeded the recommended limit of 7 lg CFU/g on day 6 (7.07 ± 0.50 lg CFU/g), whereas the TVC of the Ge/Dx/1.2 film-packaged scallop adductor muscle was still below the limit on day 9 (5.60 ± 0.50 lg CFU/g). Thus, the Ge/Dx/1.2 film can extend the shelf life of refrigerated scallop adductor muscle by at least 3 days. Overall, the developed gelatin/dextran active packaging films are promising for the preservation of aquatic food products.


Assuntos
Acroleína , Dextranos , Embalagem de Alimentos , Conservação de Alimentos , Gelatina , Pectinidae , alfa-Tocoferol , Gelatina/química , Pectinidae/química , Animais , Acroleína/análogos & derivados , Acroleína/farmacologia , Acroleína/química , Dextranos/química , Dextranos/farmacologia , alfa-Tocoferol/farmacologia , alfa-Tocoferol/química , Conservação de Alimentos/métodos , Embalagem de Alimentos/métodos , Antioxidantes/farmacologia , Permeabilidade , Frutos do Mar/análise , Interações Hidrofóbicas e Hidrofílicas
10.
Int J Mol Sci ; 25(9)2024 Apr 26.
Artigo em Inglês | MEDLINE | ID: mdl-38731961

RESUMO

Recently, the increase in marine temperatures has become an important global marine environmental issue. The ability of energy supply in marine animals plays a crucial role in avoiding the stress of elevated temperatures. The investigation into anaerobic metabolism, an essential mechanism for regulating energy provision under heat stress, is limited in mollusks. In this study, key enzymes of four anaerobic metabolic pathways were identified in the genome of scallop Chlamys farreri, respectively including five opine dehydrogenases (CfOpDHs), two aspartate aminotransferases (CfASTs) divided into cytoplasmic (CfAST1) and mitochondrial subtype (CfAST2), and two phosphoenolpyruvate carboxykinases (CfPEPCKs) divided into a primitive type (CfPEPCK2) and a cytoplasmic subtype (CfPEPCK1). It was surprising that lactate dehydrogenase (LDH), a key enzyme in the anaerobic metabolism of the glucose-lactate pathway in vertebrates, was absent in the genome of scallops. Phylogenetic analysis verified that CfOpDHs clustered according to the phylogenetic relationships of the organisms rather than substrate specificity. Furthermore, CfOpDHs, CfASTs, and CfPEPCKs displayed distinct expression patterns throughout the developmental process and showed a prominent expression in muscle, foot, kidney, male gonad, and ganglia tissues. Notably, CfASTs displayed the highest level of expression among these genes during the developmental process and in adult tissues. Under heat stress, the expression of CfASTs exhibited a general downregulation trend in the six tissues examined. The expression of CfOpDHs also displayed a downregulation trend in most tissues, except CfOpDH1/3 in striated muscle showing significant up-regulation at some time points. Remarkably, CfPEPCK1 was significantly upregulated in all six tested tissues at almost all time points. Therefore, we speculated that the glucose-succinate pathway, catalyzed by CfPEPCK1, serves as the primary anaerobic metabolic pathway in mollusks experiencing heat stress, with CfOpDH3 catalyzing the glucose-opine pathway in striated muscle as supplementary. Additionally, the high and stable expression level of CfASTs is crucial for the maintenance of the essential functions of aspartate aminotransferase (AST). This study provides a comprehensive and systematic analysis of the key enzymes involved in anaerobic metabolism pathways, which holds significant importance in understanding the mechanism of energy supply in mollusks.


Assuntos
Glucose , Resposta ao Choque Térmico , Pectinidae , Filogenia , Animais , Pectinidae/metabolismo , Pectinidae/genética , Glucose/metabolismo , Resposta ao Choque Térmico/fisiologia , Anaerobiose , Ácido Succínico/metabolismo , Redes e Vias Metabólicas , Aspartato Aminotransferases/metabolismo , Aspartato Aminotransferases/genética
11.
Int J Mol Sci ; 25(9)2024 Apr 28.
Artigo em Inglês | MEDLINE | ID: mdl-38732036

RESUMO

Bivalves hold an important role in marine aquaculture and the identification of growth-related genes in bivalves could contribute to a better understanding of the mechanism governing their growth, which may benefit high-yielding bivalve breeding. Somatostatin receptor (SSTR) is a conserved negative regulator of growth in vertebrates. Although SSTR genes have been identified in invertebrates, their involvement in growth regulation remains unclear. Here, we identified seven SSTRs (PySSTRs) in the Yesso scallop, Patinopecten yessoensis, which is an economically important bivalve cultured in East Asia. Among the three PySSTRs (PySSTR-1, -2, and -3) expressed in adult tissues, PySSTR-1 showed significantly lower expression in fast-growing scallops than in slow-growing scallops. Then, the function of this gene in growth regulation was evaluated in dwarf surf clams (Mulinia lateralis), a potential model bivalve cultured in the lab, via RNA interference (RNAi) through feeding the clams Escherichia coli containing plasmids expressing double-stranded RNAs (dsRNAs) targeting MlSSTR-1. Suppressing the expression of MlSSTR-1, the homolog of PySSTR-1 in M. lateralis, resulted in a significant increase in shell length, shell width, shell height, soft tissue weight, and muscle weight by 20%, 22%, 20%, 79%, and 92%, respectively. A transcriptome analysis indicated that the up-regulated genes after MlSSTR-1 expression inhibition were significantly enriched in the fat digestion and absorption pathway and the insulin pathway. In summary, we systemically identified the SSTR genes in P. yessoensis and revealed the growth-inhibitory role of SSTR-1 in bivalves. This study indicates the conserved function of somatostatin signaling in growth regulation, and ingesting dsRNA-expressing bacteria is a useful way to verify gene function in bivalves. SSTR-1 is a candidate target for gene editing in bivalves to promote growth and could be used in the breeding of fast-growing bivalves.


Assuntos
Bivalves , Pectinidae , Receptores de Somatostatina , Animais , Pectinidae/genética , Pectinidae/crescimento & desenvolvimento , Pectinidae/metabolismo , Bivalves/genética , Bivalves/crescimento & desenvolvimento , Bivalves/metabolismo , Receptores de Somatostatina/genética , Receptores de Somatostatina/metabolismo , Filogenia , Interferência de RNA , Regulação da Expressão Gênica no Desenvolvimento
12.
Food Chem ; 451: 139493, 2024 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-38703728

RESUMO

Iron chelating peptides have been widely utilized as iron supplements due to their excellent absorption capacity, However, the high cost and cumbersome manufacturing process of these peptides significantly limit their industrial application. In this study, fermentation was used for the first time to prepare iron chelating peptides. Bacillus altitudinis 3*1-3 was selected as the most suitable strain from 50 strains. The hydrolysates of fermented scallop skirts showed excellent iron-chelating capacity (9.39 mg/g). Aspartic acid, glutamic acid, and histidine are crucial for the binding of peptides to ferrous ions. The heptapeptide (FEDPEFE) forms six binding bonds with ferrous irons. Compared with ferrous sulfate, peptide-ferrous chelate showed more stability in salt solution and simulated gastrointestinal juice (p < 0.05). Furthermore, the fermentation method could save >50% of the cost compared with the enzymatic method. The results can provide a theoretical basis for the preparation of ferrous-chelated peptides using the fermentation method.


Assuntos
Bacillus , Fermentação , Quelantes de Ferro , Pectinidae , Peptídeos , Animais , Pectinidae/química , Pectinidae/metabolismo , Pectinidae/microbiologia , Peptídeos/química , Peptídeos/metabolismo , Quelantes de Ferro/química , Quelantes de Ferro/metabolismo , Bacillus/metabolismo , Bacillus/química , Ferro/química , Ferro/metabolismo
13.
Artigo em Inglês | MEDLINE | ID: mdl-38781887

RESUMO

The bay scallop is a eurythermal species with high economic value and now represents the most cultured bivalve species in China. Two subspecies of the bay scallop, the northern subspecies Argopecten irradians irradians Korean population (KK) and the southern subspecies Argopecten irradians concentricus (MM), exhibited distinct adaptations to heat stress. However, the molecular mechanism of heat resistance of the two subspecies remains unclear. In this study, we compared the transcriptomic responses of the two subspecies to heat stress and identified the involved differentially expressed genes (DEGs) and pathways. More DEGs were found in the KK than in the MM when exposed to high temperatures, indicating elevated sensitivity to thermal stress in the KK. Enrichment analysis suggests that KK scallops may respond to heat stress more swiftly by regulating GTPase activity. Meanwhile, MM scallops exhibited higher resistance to heat stress mainly by effective activation of their antioxidant system. Chaperone proteins may play different roles in responses to heat stress in the two subspecies. In both subspecies, the expression levels of antioxidants such as GST were significantly increased; the glycolysis process regulated by PC and PCK1 was greatly intensified; and both apoptotic and anti-apoptotic systems were significantly activated. The pathways related to protein translation and hydrolysis, oxidoreductase activity, organic acid metabolism, and cell apoptosis may also play pivotal roles in the responses to heat stress. The results of this study may provide a theoretical basis for marker-assisted breeding of heat-resistant strains.


Assuntos
Perfilação da Expressão Gênica , Pectinidae , Transcriptoma , Animais , Pectinidae/genética , Pectinidae/fisiologia , Termotolerância/genética , Resposta ao Choque Térmico
14.
PLoS One ; 19(5): e0302225, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38739607

RESUMO

Global scallop fisheries are economically important but are associated with environmental impacts to seabed communities resulting from the direct physical contact of the fishing gear with the seabed. Gear modifications attempting to reduce this contact must be economically feasible such that the catch numbers for the target species is maintained or increased. This study investigated the outcome of reducing seabed contact on retained catch of scallops and bycatch by the addition of skids to the bottom of the collecting bag of scallop dredges. We used a paired control experimental design to investigate the impact of the gear modification in different habitat types. The modified skid dredge generally caught more marketable scallops per unit area fished compared with the standard dredge (+5%). However, the skid dredge also retained more bycatch (+11%) and more undersize scallops (+16%). The performance of the two dredges was habitat specific which indicates the importance of adjusting management measures in relation to habitat type. To realize the potential environmental benefits associated with the improvement in catchability of this gear modification, further gear modification is required to reduce the catch of undersize scallops and bycatch. Furthermore we advocate that technical gear innovations in scallop dredging need to be part of a comprehensive and effective fisheries management system.


Assuntos
Ecossistema , Pesqueiros , Pectinidae , Animais , Conservação dos Recursos Naturais/métodos
15.
Int J Mol Sci ; 25(7)2024 Apr 02.
Artigo em Inglês | MEDLINE | ID: mdl-38612756

RESUMO

Carotenoids are essential nutrients for humans and animals, and carotenoid coloration represents an important meat quality parameter for many farmed animals. Increasingly, studies have demonstrated that vertebrate carotenoid cleavage oxygenases (CCOs) are essential enzymes in carotenoid metabolism and are therefore potential candidate genes for improving carotenoid deposition. However, our understanding of carotenoid bioavailability and CCOs functions in invertebrates, particularly marine species, is currently quite limited. We previously identified that a CCO homolog, PyBCO-like 1, was the causal gene for carotenoid coloration in the 'Haida golden scallop', a variety of Yesso scallop (Patinopecten yessoensis) characterized by carotenoid enrichment. Here, we found that another CCO-encoding gene named PyBCO2 (ß-carotene oxygenase 2) was widely expressed in P. yessoensis organs/tissues, with the highest expression in striated muscle. Inhibiting BCO2 expression in P. yessoensis through RNA interference led to increased carotenoid (pectenolone and pectenoxanthin) deposition in the striated muscle, and the color of the striated muscle changed from white to light orange. Our results indicate that PyBCO2 might be a candidate gene used for improving carotenoid content in normal Yesso scallops, and also in 'Haida golden scallops'.


Assuntos
Dioxigenases , Pectinidae , Animais , Humanos , beta Caroteno , Músculo Esquelético , Carotenoides , Pectinidae/genética , Dioxigenases/genética
16.
Toxicon ; 243: 107710, 2024 May 28.
Artigo em Inglês | MEDLINE | ID: mdl-38579982

RESUMO

For food safety, the concentrations and profiles of paralytic shellfish toxins (PSTs) and tetrodotoxin were examined in economically important scallops and bloody clams collected from the coast of the Miyagi Prefecture, Japan. PSTs were the major toxins in both species. The tetrodotoxin concentration in scallops increased in summer, although the highest value (18.7 µg/kg) was lower than the European Food Safety Authority guideline threshold (44 µg/kg). This confirmed the safety for tetrodotoxin in this area.


Assuntos
Bivalves , Pectinidae , Tetrodotoxina , Animais , Tetrodotoxina/análise , Pectinidae/química , Japão , Bivalves/química , Toxinas Marinhas/análise , Saxitoxina/análise , Saxitoxina/análogos & derivados , Intoxicação por Frutos do Mar , Estações do Ano , Contaminação de Alimentos/análise
17.
Int J Biol Macromol ; 267(Pt 2): 131636, 2024 May.
Artigo em Inglês | MEDLINE | ID: mdl-38641287

RESUMO

Although bioactive peptides enhancing bone healing have demonstrated effectiveness in treating bone defects, in vivo instability poses a challenge to their clinical application. Currently reported peptide delivery systems do not meet the demands of bone tissue repair regarding stability and peptide release efficacy. Herein, the self-assembling recombinant chimeric protein (Sbp5-2RGD) is developed by genetic engineering with cell adhesion peptide RGD as the targeted peptide and a newly discovered scallop byssal-derived protein Sbp5-2 that can assemble into wet stable films as the structural domain. In vitro studies show that the Sbp5-2RGD film exhibits excellent extensibility and biocompatibility. In vitro and in vivo degradation experiments demonstrate that the film remains stable due to the layer-by-layer degradation mode, resulting in sustained delivery of RGD in situ for up to 4 weeks. Consequently, the film can effectively promote osteogenesis, which accelerates bone defect healing and the implants osseointegration. Cell-level studies further show that the film up-regulates the expression of genes and proteins (ALP, OCN, OSX, OPN, RUNX2, VEGF) associated with osteogenesis and angiogenesis. Overall, this novel protein film represents an intelligent platform for peptide immobilization, protection, and release through its self-assembly, dense structure, and degradation mode, providing a therapeutic strategy for bone repair.


Assuntos
Engenharia Genética , Oligopeptídeos , Animais , Humanos , Camundongos , Sistemas de Liberação de Medicamentos , Engenharia Genética/métodos , Oligopeptídeos/química , Oligopeptídeos/farmacologia , Osseointegração/efeitos dos fármacos , Osteogênese/efeitos dos fármacos , Pectinidae , Ratos Sprague-Dawley , Masculino , Ratos
18.
Harmful Algae ; 133: 102607, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38485441

RESUMO

Domoic acid (DA) is a potent neurotoxin produced by diatoms of the genus Pseudo-nitzschia and is responsible for Amnesic Shellfish Poisoning (ASP) in humans. Some fishery resources of high commercial value, such as the king scallop Pecten maximus, are frequently exposed to toxic Pseudo-nitzschia blooms and are capable of accumulating high amounts of DA, retaining it for months or even a few years. This poses a serious threat to public health and a continuous economical risk due to fishing closures of this resource in the affected areas. Recently, it was hypothesized that trapping of DA within autophagosomic-vesicles could be one reason explaining the long retention of the remaining toxin in P. maximus digestive gland. To test this idea, we follow the kinetics of the subcellular localization of DA in the digestive glands of P. maximus during (a) the contamination process - with sequential samplings of scallops reared in the field during 234 days and naturally exposed to blooms of DA-producing Pseudo-nitzschia australis, and (b) the decontamination process - where highly contaminated scallops were collected after a natural bloom of toxic P. australis and subjected to DA-depuration in the laboratory for 60 days. In the digestive gland, DA-depuration rate (0.001 day-1) was much slower than contamination kinetics. The subcellular analyses revealed a direct implication of early autophagy in DA sequestration throughout contamination (r = 0.8, P < 0.05), while the presence of DA-labeled residual bodies (late autophagy) appeared to be strongly and significantly related to slow DA-depuration (r = -0.5) resembling an analogous DA-tattooing in the digestive glands of P. maximus. This work provides new evidence about the potential physiological mechanisms involved in the long retention of DA in P. maximus and represents the baseline to explore procedures to accelerate decontamination in this species.


Assuntos
Diatomáceas , Ácido Caínico/análogos & derivados , Pecten , Pectinidae , Intoxicação por Frutos do Mar , Tatuagem , Animais , Humanos , Toxinas Marinhas
19.
J Hazard Mater ; 469: 133896, 2024 May 05.
Artigo em Inglês | MEDLINE | ID: mdl-38428300

RESUMO

Paralytic shellfish toxins (PSTs) produced by some marine dinoflagellates can cause severe human intoxication via vectors like bivalves. Toxic dinoflagellate Gymnodinium catenatum produce a novel group of hydroxybenzoate PSTs named GC toxins, but their biokinetics in bivalves haven't been well examined. In this experiment, we analyzed PSTs in bay scallops Argopecten irradians exposed to G. catenatum (strain MEL11) to determine their accumulation, elimination, anatomical distribution, and biotransformation. To our surprise, up to 30% of the PSTs were accumulated in the adductor muscle of scallops at the end of the experiment, and the toxicity of adductor muscle exceeded the regulatory limit of 800 µg STXeq/kg in only 6 days. High concentration of toxins in the adductor muscle are likely linked to the rapid transfer of GC toxins from viscera to other tissues. Moreover, most GC toxins in scallops were found rapidly transformed to decarbamoyl toxins through enzyme-mediated hydrolysis, which was further supported by the in vitro incubation experiments. Our study demonstrates that GC toxins actively participate in toxin distribution and transformation in scallops, which may increase the risks of food poisoning associated with the consumption of scallop adductor muscle. ENVIRONMENTAL IMPLICATION: The negative impacts of harmful algal blooms (HABs) have become a global environmental concern under the joint effects of cultural eutrophication and climate change. Our study, targeted on the biokinetics of paralytic shellfish toxins in scallops exposed to Gymnodinium catenatum producing unique GC toxins, aims to elucidate potential risks of seafood poisoning associated with GC toxins. The findings of this study will help us to understand the roles of GC toxins in seafood poisoning, and to develop effective management strategies against toxic algal blooms and phycotoxins.


Assuntos
Bivalves , Dinoflagellida , Pectinidae , Intoxicação por Frutos do Mar , Animais , Humanos , Toxinas Marinhas/toxicidade , Intoxicação por Frutos do Mar/etiologia , Pectinidae/metabolismo , Bivalves/metabolismo , Hidroxibenzoatos/metabolismo , Alimentos Marinhos , Frutos do Mar
20.
Food Chem ; 447: 138985, 2024 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-38507952

RESUMO

Myofibrillar protein (MP) is susceptible to the effect of ionic strength and ultra-high pressure (UHP) treatment, respectively. However, the impact of UHP combined with ionic strength on the structure and in vitro digestibility of MP from scallop mantle (Patinopecten yessoensis) is not yet clear. Therefore, it is particularly important to analyze the structural properties and enhance the in vitro digestibility of MP by NaCl and UHP treatment. The findings demonstrated that as ionic strength increased, the α-helix and ß-sheet gradually transformed into ß-turn and random coil. The decrease of endogenous fluorescence intensity indicated the formation of a more stable tertiary structure. Additionally, the exposure of internal sulfhydryl groups increased the amount of total sulfhydryl content, and reactive sulfhydryl groups gradually transformed into disulfide bonds. Moreover, it reduces aggregation through increased solubility, decreased turbidity, particle sizes, and a relatively dense and uniform microstructure. When MP from the scallop mantle was treated with 0.5 mol/L ionic strength and 200 MPa UHP treatment, it had the highest solubility (90.75 ± 0.13%) and the lowest turbidity (0.41 ± 0.03). The scallop mantle MP with NaCl of 0.3 mol/L and UHP treatment had optimal in vitro digestibility (95.14 ± 2.01%). The findings may offer a fresh perspectives for developing functional foods for patients with dyspepsia and a theoretical foundation for the comprehensive utilization of scallop mantle by-products with low concentrations of NaCl.


Assuntos
Pectinidae , Cloreto de Sódio , Animais , Humanos , Cloreto de Sódio/metabolismo , Proteínas/química , Pectinidae/química , Cloreto de Sódio na Dieta
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA