Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 6 de 6
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
Comput Commun ; 206: 172-177, 2023 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-37197297

RESUMO

In recent years, coronavirus disease 2019 (COVID-19) has been a severe issue the world faces. Emergency rescue networks concerning the distribution of relief materials have gained extensive attention to tackle COVID-19 and related emergency issues. However, it is challenging to establish reliable and efficient emergency rescue networks due to information asymmetry and lack of trust among different rescue stations. In this work, we propose blockchain-based emergency rescue networks to track every transaction of the relief materials reliably and make decisions to deliver relief materials efficiently. More specifically, we propose a hybrid blockchain architecture that employs on-chain data verification to authenticate data records and off-chain data storage to reduce storage overhead. Furthermore, we propose a fireworks algorithm to efficiently calculate the optimal allocation strategies for relief materials. The algorithm provides chaotic random screening and node request guarantee techniques with good convergence. The simulation results show that integrating blockchain technology and the fireworks algorithm can significantly improve relief materials' operation efficiency and distribution quality.

2.
Front Endocrinol (Lausanne) ; 13: 1072176, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-36778601

RESUMO

Objective: The purpose of this study was to evaluate the influence of abnormal semen parameters on embryo aneuploidy based on single nucleotide polymorphism microarray (SNP array). Methods: A total of 464 blastocysts from 103 PGT-A cycles were analyzed. The embryo quality and embryo aneuploidy rates were compared between different groups which divided by male semen parameters (sperm concentration, motility, morphology, and DFI) according the WHO criteria (2021). Results: The total blastocysts chromosome aneuploidy rate was 42.3% (191/452). In the teratozoospermia group, the good-quality embryo and blastocyst formation rate were lower than the normal group(44.4% vs 60.7%, P <0.01; 33.3% vs 43.5%, P <0.05), The good-quality embryo rate in normal DFI group was significantly higher than high-DFI group (59.0% vs 48.4%, P < 0.05). The blastocyst aneuploidy rate in low sperm concentration group, and high DFI group was no differences between with that in normal sperm concentration and DFI group (47.7% vs 37.8% and 44.7% vs 37.8%, P>0.05). The aneuploid rate of blastocyst in teratozoospermic and asthenozoospermia group was significantly higher than that of normal morphology and motility group (50.0% vs 34.0% and 46.7% vs 33.7%, P<0.05). Conclusion: Our study revealed that sperm DFI were positively correlated with blastocyst aneuploidy rate, while sperm motility and sperm morphology rate were negatively correlated with blastocyst aneuploidy rate. Abnormal semen parameters may affect embryo quality and increase the aneuploidy rate of blastocyst chromosomes, suggesting that in clinical practice of assisted reproduction patients with abnormal semen parameters can be treated in advance to improve sperm quality, so as to reduce the impact on embryo quality and achieve a better pregnancy outcome.


Assuntos
Fertilização in vitro , Teratozoospermia , Feminino , Gravidez , Masculino , Humanos , Injeções de Esperma Intracitoplásmicas , Sêmen , Correlação de Dados , Motilidade dos Espermatozoides , Testes Genéticos , Aneuploidia
3.
Fish Shellfish Immunol ; 95: 635-643, 2019 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-31678183

RESUMO

Small heat shock proteins (sHSPs) are ATP-independent chaperones and involved into various physiological and stress processes. In the present study, a 28.6-kD sHSP coding gene, MnHSP28.6, was cloned and characterized from the oriental river prawn Macrobrachium nipponense. Tissue distribution analysis via qPCR and western blot revealed that MnHSP28.6 predominantly expressed in muscle. The temporal transcription of MnHSP28.6 in muscle after bacterial challenge, heavy metal exposure and doxorubicin (DOX) injection was investigated by qPCR. The results showed that the expression of MnHSP28.6 were strongly enhanced by both Cd2+ and Cu2+ exposure, as well as DOX injection, but not by bacterial infection. Aggregation assays showed that recombinant MnHSP28.6 could effectively prevent temperature-induced aggregation of citrate synthase, and reduction-induced aggregation of insulin in vitro. MnHSP28.6 also could protect muscle extracts from heat-induced protein denaturation and superoxide dismutase (SOD) inactivation. Expressing MnHSP28.6 in E. coli conferred host cell impressive protection against H2O2 compared to control. These results suggest a protective role of MnHSP28.6 in maintaining protein homeostasis, preventing aggregation, promoting resistance to heavy metal and keeping redox balance.


Assuntos
Proteínas de Artrópodes/metabolismo , Proteínas de Choque Térmico Pequenas/metabolismo , Intoxicação por Metais Pesados/veterinária , Estresse Oxidativo , Palaemonidae/genética , Animais , Proteínas de Artrópodes/genética , Proteínas de Choque Térmico Pequenas/genética , Intoxicação por Metais Pesados/prevenção & controle , Temperatura Alta , Chaperonas Moleculares/genética , Músculos/metabolismo , Oxirredução , Substâncias Protetoras , Proteostase
4.
Fish Shellfish Immunol ; 89: 701-709, 2019 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-31004801

RESUMO

Based on the transcriptome database, we screened out four ferritin subunit genes (MnFer2-5) from the oriental river prawn Macrobrachium nipponense, which encode two non-secretory and two secretory peptides. MnFer2 and 4 possess a strictly conserved ferroxidase site, and MnFer3 has a non-typical ferroxidase site. MnFer5 seems to be a number of ferritin families, which has a distinct dinuclear metal binding motif, but lacks an iron ion channel, a ferroxidase site and a nucleation site. Diverse tissue-specific transcriptions of the four genes indicate their functional diversity in the prawn. Among them, MnFer2 is mainly expressed in hepatopancreas and intestines, MnFer3 and 4 are predominantly expressed in gills, and MnFer5 is widely expressed in various tissues with high presence in intestines, hepatopancreas and haemocytes. The transcription of all the four MnFer genes can be strongly induced by doxorubicin, indicating the involvement of these ferritin subunits in protection from oxidative stress. Upon Aeromonas hydrophila infection, only MnFer5 is persistently up-regulated, while other subunits including MnFer2-4 are down-regulated during the early stage, followed by recovery and even a slight increase at 48 h post bacterial challenge. Moreover, the iron binding capacity of recombinant MnFer2 is also demonstrated in vitro. The E. coli expressing MnFer2 displays increased resistance to hydrogen peroxidase cytotoxicity. These results suggest a protective role of ferritins from M. nipponense in iron homeostasis, redox biology and antibacterial immunity and shed light on the molecule evolution of crustacean ferritin subunits.


Assuntos
Ferritinas/genética , Ferritinas/imunologia , Regulação da Expressão Gênica/imunologia , Imunidade Inata/genética , Estresse Oxidativo/imunologia , Penaeidae/genética , Penaeidae/imunologia , Sequência de Aminoácidos , Animais , Proteínas de Artrópodes/química , Proteínas de Artrópodes/genética , Proteínas de Artrópodes/imunologia , Sequência de Bases , Relação Dose-Resposta a Droga , Doxorrubicina/farmacologia , Ferritinas/química , Perfilação da Expressão Gênica , Homeostase/imunologia , Oxirredução , Palaemonidae , Filogenia , Isoformas de Proteínas/química , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Distribuição Aleatória , Alinhamento de Sequência
5.
Chem Commun (Camb) ; 55(9): 1342-1344, 2019 Jan 24.
Artigo em Inglês | MEDLINE | ID: mdl-30640326

RESUMO

Patterned nanotriangle arrays with composition graded and multilayered Ag-Cu were fabricated by a co-deposition and nanosphere lithography process. With the increase of the number of layers or constructing a continuum graded layer, the index sensitivity of the resulting nanotriangles kept on increasing, indicating that the graded boundaries can improve plasmon resonance sensing.

6.
Fish Shellfish Immunol ; 70: 327-334, 2017 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-28882803

RESUMO

In Macrobrachium nipponense, the rhodanese homologue 2 (MnRDH2) gene codes for a single rhodanese domain protein. Considering the lack of information on the biological role of the ubiquitous rhodaneses in invertebrate, we examined the functions of MnRDH2 using both in silico and in vitro approaches. Quantitative PCR analysis of different tissues indicated that expression of MnRDH2 was enriched in hepatopancreas, in which bacterial challenge by Aeromonas hydrophila induced MnRDH2 expression. Knocking down MnRDH2 by RNA interference caused significant accumulations of reactive oxygen species and malondialdehyde (MDA). Using Escherichia coli (DE3), we expressed MnRDH2 and the mutant MnRDH2C78A, in which the predicted catalytic cysteine was mutated to alanine, and found significant rodanese activity of the recombinant MnRDH2 in vitro, but not for the mutant rMnRDH2C78A. We observed that rMnRDH2 was able to significantly increase tolerance of the host bacteria to oxidative stressor phenazine methosulfate. These results suggest that MnRDH2 might have the potential to buffer general levels of oxidants via regulation of redox reactions. In conclusion, our study begins to hint a possible biological functionality of MnRDH2 as a redox switch to activate defensive activities against oxidative damage, which helps host in maintaining the cellular redox balance. These characteristics will facilitate future investigations into the physiological functions for invertebrate rhodanese family genes.


Assuntos
Antioxidantes/metabolismo , Imunidade Inata , Palaemonidae/genética , Palaemonidae/imunologia , Tiossulfato Sulfurtransferase/genética , Tiossulfato Sulfurtransferase/imunologia , Sequência de Aminoácidos , Animais , Proteínas de Artrópodes/genética , Proteínas de Artrópodes/imunologia , Sequência de Bases , Escherichia coli/fisiologia , Especificidade de Órgãos , Alinhamento de Sequência
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA