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1.
Yi Chuan ; 45(5): 447-458, 2023 May 20.
Artigo em Inglês | MEDLINE | ID: mdl-37194591

RESUMO

Neuregulin 4 (NRG4) is an important adipocytokine, which plays crucial roles in maintaining energy balance, regulating glucose and lipid metabolism, and preventing non-alcoholic fatty liver disease in mammals. At present, the genomic organization, transcript and protein isoforms of human NRG4 gene have been fully explored. Previous studies in our laboratory have shown that the NRG4 gene is expressed in chicken adipose tissue, but the chicken NRG4 (cNRG4) genomic structure, transcript and protein isoforms are still unknown. To this end, in this study, the genomic and transcriptional structure of the cNRG4 gene were systematically investigated using rapid amplification of cDNA ends (RACE) and reverse transcription-polymerase chain reaction (RT-PCR). The results showed that the coding region (CDS) of the cNRG4 gene was small, but it had a very complex transcriptional structure characterized by multiple transcription start sites, alternative splicing, intron retention, cryptic exons, and alternative polyadenylation, thus leading to production of four 5?UTR isoforms (cNRG4 A, cNRG4 B, cNRG4 C, and cNRG4 D) and six 3?UTR isoforms (cNRG4 a, cNRG4 b, cNRG4 c, cNRG4 d, cNRG4 e, and cNRG4 f) of the cNRG4 gene. The cNRG4 gene spanned 21,969 bp of genomic DNA (Chr.10:3,490,314~3,512,282) and consisted of 11 exons and 10 introns. Compared with the cNRG4 gene mRNA sequence (NM_001030544.4), two novel exons and one cryptic exon of the cNRG4 gene were identified in this study. Bioinformatics analysis, RT-PCR, cloning and sequencing analysis showed that the cNRG4 gene could encode three protein isoforms (cNRG4-1, cNRG4-2 and cNRG4-3). This study lays a foundation for further research on the function and regulation of the cNRG4 gene.


Assuntos
Processamento Alternativo , Galinhas , Animais , Processamento Alternativo/genética , Sequência de Bases , Galinhas/genética , DNA Complementar/genética , Genômica , Íntrons/genética , Neurregulinas/genética , Isoformas de Proteínas/genética
2.
Huan Jing Ke Xue ; 42(10): 4798-4806, 2021 Oct 08.
Artigo em Chinês | MEDLINE | ID: mdl-34581122

RESUMO

Polybrominated diphenyl ethers(PBDEs) are potentially harmful to human health and the ecological environment. It is, therefore, of great significance to develop efficient, economic, and environmentally-friendly advanced oxidation systems for their effective degradation. Here, a magnetic biochar supported manganese dioxide composite(α-MnO2/MWB) synthesized by hydrothermal methods was used as a catalyst to activate peroxymonosulfate(PMS) in the degradation of 2, 2', 4, 4'-tetrabrominated diphenyl ether(BDE-47). The prepared materials were characterized by SEM, XRD, FT-IR, and BET. The results showed that α-MnO2/MWB had the best catalytic performance, and the highest degradation efficiency reached 94% under optimal conditions(α-MnO2/MWB mass ratio=1:2, catalyst dosage=0.05 g·L-1, PMS concentration=5 mmol·L-1, BDE-47 concentration=1 mg·L-1). The effect of initial pH on the system was not distinct, while chloride ions(Cl-) and humic acid(HA) inhibited the degradation of BDE-47. In comparison, nitrate ions(NO3-) and bicarbonate ions(HCO3-) had no notable effect on the degradation. SO4-· and·OH were the key free radicals in the degradation of BDE-47 in this system, with SO4-· being dominant. As showed by the XPS characterization of the materials before and after the reaction, a change in the valence states of Mn and Fe was the main reason for the activation of PMS. It was also revealed that α-MnO2/MWB composites maintained high catalytic performance after being reused up to four times.


Assuntos
Compostos de Manganês , Óxidos , Carvão Vegetal , Éter , Éteres Difenil Halogenados , Humanos , Fenômenos Magnéticos , Peróxidos , Espectroscopia de Infravermelho com Transformada de Fourier
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