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Anushka Vidurangi Samaraweera,D.S. Liyanage,W.K.M. Omeka,Hyerim Yang,Thanthrige Thiunuwan Priyathilaka,Jehee Lee 제주대학교 해양과학연구소 2020 해양과환경연구소 연구논문집 Vol.44 No.-
Peroxiredoxins (Prxs) are cysteine-dependent antioxidant proteins that play a leading part in oxidative stress response. Peroxiredoxin 4 (Prx4) is located in the endoplasmic reticulum, where it is primarily involved in regulating the concentration of H2O2, generated during protein folding. Prx4 is also located in the extracellular space, where it activates the JAK/STAT-mediated stress response. Here, we focus on the identification and characterization of the sequence and function of Prx4 from the big-belly seahorse (Hippocampus abdominalis) (HaPrx4). The size of the HaPrx4 coding sequence was 777 bp, which encoded a 258 amino acid protein of 28.8 kDa molecular weight. The amino acid sequence comprises a signal peptide, two active sites with peroxidatic cysteine and resolving cysteine, catalytic triad, and peroxiredoxin superfamily domain. According to the tissue distribution results, ovaries exhibited the highest HaPrx4 expression level within fourteen examined tissues. The HaPrx4 transcriptional responses to four immune stimulants (lipopolysaccharides, polyinosinic: polycytidylic acid, Edwardsiella tarda, and Streptococcus iniae) were evaluated in the blood and liver tissues. Additionally, the functions of recombinant HaPrx4 protein were evaluated by metal ion-catalyzed oxidation assay, peroxidase activity assay, insulin reduction assay, cell viability assay, and Hoechst staining. The assay results confirmed that the functions of HaPrx4 involved DNA protection, hydrogen peroxide (H2O2) elimination, oxidoreductase activity, enhancing cell survival, and cell protection. The results of the current study propose that HaPrx4 is effectively involved in H2O2 scavenging activity during stress conditions and in innate immune responses of the big-belly seahorse.
효소제 기반 면역증강제가 육계의 성장, 항산화 지수, 면역 활성 및 장 건강에 미치는 영향
Anushka Lokhande,Santosh Ingale,문준영,김진수 강원대학교 동물생명과학연구소 2022 동물자원연구 Vol.33 No.4
This study was conducted to evaluate the effects of ImmunoSEB as an immune-booster additive on the performance of broiler chicks. A total of 1150 broiler chickens were randomly allotted to three treatments on the basis of body weight (10 pens per treatment with 40 broilers in each pen): the control (CON), CON + ImmunoSEB 0.025% in feed (SEB25), and CON + ImmunoSEB 0.050% in feed (SEB50). The experiment was conducted for d 42 in three phases (phase 1, d 0–14; phase 2, d 15–28; and phase 3, d 29–42). There were significant differences in the average daily gain (ADG) and feed intake. The ADG at d 14 in the SEB50 treatment was greater than that in the CON treatment. The overall ADG in the SEB50 treatment was greater than that in the CON treatment. During d 0–14, the feed intake of chickens in the SEB50 treatment increased compared to that in the CON treatment. The crude protein and lysine digestibility improved in the SEB25 and SEB50 treatments compared to those in the CON treatment at d 28. Superoxide dismutase concentration significantly increased in the SEB50 treatment compared to that in the CON treatment. The interleukin-1β and tumor necrosis factor-α concentrations were higher in the cecum of chickens in the CON treatment than in the SEB25 and SEB50 treatments. A lower population of E. coli was detected in the ileum and cecum of broilers fed the SEB50 diet compared to those of broilers fed the CON diet. The overall result showed the beneficial effects of using ImmunoSEB at a dose of 0.050% in broiler chickens.
Anushka Vidurangi Samaraweera,M.D. Neranjan Tharuka,Thanthrige Thiunuwan Priyathilaka,Hyerim Yang,Sukkyoung Lee,Jehee Lee 제주대학교 해양과학연구소 2021 해양과환경연구소 연구논문집 Vol.45 No.-
Peroxiredoxins (Prxs) are ubiquitously expressed antioxidant proteins that can protect aerobic organisms from oxidative stress. Here, we characterized the HaPrx3 homolog at the molecular level from big-belly seahorse (Hippocampus abdominalis) and analyzed its functional activities. The coding sequence of HaPrx3 consists of 726 bp, which encodes 241 amino acids. The predicted molecular weight and theoretical isoelectric point (pI) of HaPrx3 was 26.20 kDa and 7.04, respectively. Multiple sequence alignments revealed that the arrangements of domains, catalytic triads, dimers, and decamer interfaces of HaPrx3 were conserved among Prx sequences of other organisms. According to the phylogenetic analysis, HaPrx3 is clustered with the teleost Prx3 subclade. The highest transcript level of HaPrx3 was detected in the ovary tissue among fourteen healthy fish tissues. The mRNA levels of HaPrx3 in blood and liver tissues were significantly (P < 0.05) upregulated in response to lipopolysaccharide (LPS), polyinosinic-polycytidylic (poly I:C), Edwardsiella tarda, and Streptococcus iniae, suggesting its involvement in immune responses. Under functional properties, insulin disulfide reduction assay confirmed the oxidoreductase activity of recombinant HaPrx3. A cell viability assay and Hoechst staining indicated cell survival ability and reduction of apoptotic activity, respectively. Moreover, a peroxidase activity assay verified peroxidase activity, while a metal-catalyzed oxidation (MCO) assay indicated the DNA protection ability of HaPrx3. Collectively, it is concluded that HaPrx3 may play a significant role in oxidative stress and immune responses against pathogenic infections in big-belly seahorses.