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Stanniocalcin-1 protects bovine intestinal epithelial cells from oxidative stress-induced damage
Li-ming Wu,Rui Guo,Lin Hui,Yong-gang Ye,Jing-mei Xiang,Chun-yun Wan,Miao Zou,Rui Ma,Xiao-zhuan Sun,Shi-jin Yang,Ding-zong Guo 대한수의학회 2014 JOURNAL OF VETERINARY SCIENCE Vol.15 No.4
Chronic enteritis can produce an excess of reactive oxygenspecies resulting in cellular damage. Stanniocalcin-1(STC-1)reportedly possesses anti-oxidative activity, the aim of thisstudy was to define more clearly the direct contribution ofSTC-1 to anti-oxidative stress in cattle. In this study, primaryintestinal epithelial cells (IECs) were exposed to hydrogenperoxide (H2O2) for different time intervals to mimic chronicenteritis-induced cellular damage. Prior to treatment with 200μM H2O2, the cells were transfected with a recombinantplasmid for 48 h to over-express STC-1. Acridine orange/ethidium bromide (AO/EB) double staining and trypan blueexclusion assays were then performed to measure cell viabilityand apoptosis of the cells, respectively. The expression of STC-1and apoptosis-related proteins in the cells was monitored byreal-time PCR and Western blotting. The results indicated thatboth STC-1 mRNA and protein expression levels positivelycorrelated with the duration of H2O2 treatment. H2O2 damagedthe bovine IECs in a time-dependent manner, and this effectwas attenuated by STC-1 over-expression. Furthermore, overexpressionof STC-1 up-regulated Bcl-2 protein expression andslightly down-regulated caspase-3 production in the damagedcells. Findings from this study suggested that STC-1 plays aprotective role in intestinal cells through an antioxidant mechanism.
Zhi, Ai-Min,Feng, Ding-Yuan,Zhou, Xiang-Yan,Zou, Shi-Geng,Huang, Zhi-Yi,Zuo, Jian-Jun,Ye, Hui,Zhang, Chang-Ming,Dong, Ze-Min,Liu, Zhun Asian Australasian Association of Animal Productio 2008 Animal Bioscience Vol.21 No.8
Cationic amino acid transporter $b^{0,+}AT$ (HGMW-approved gene symbol SLC7A9, solute carrier family 7, member 9) plays a crucial role in amino acid nutrition. In the present study, we describe the cloning and sequencing of porcine $b^{0,+}AT$. Based on the sequence of porcine $b^{0,+}AT$ deposited in the NCBI (National Center for Biotechnological Information), we identified a putative porcine homologue. Using rapid amplification of cDNA ends (RACE), the full-length cDNA encoding porcine $b^{0,+}AT$ was isolated. The porcine $b^{0,+}AT$ cDNA was 1,680 bp long, encoding a 487 amino acid trans-membrane protein. The predicted amino acid sequence was found to have 88.9% and 87.1% identity with human and mouse $b^{0,+}AT$, respectively. Real-time RT-PCR indicated porcine $b^{0,+}AT$ transcripts expressed in heart, kidney, muscle and small intestine. The small intestine had the highest $b^{0,+}AT$ mRNA abundance while the muscle had the lowest (p<0.05). Along the longitudinal axis, the ileum had the highest $b^{0,+}AT$ mRNA abundance while the colon had the lowest (p<0.05). The $b^{0,+}AT$ mRNA level was highest on day 7 and 90 in the duodenum (p<0.05). It increased from day 1 to day 26 in the jejunum (p>0.05) and had the highest abundance on day 60 (p<0.05). There was, however, no difference between day 1, 7, 26, 30, 90 and 150 (p>0.05). The strongest $b^{0,+}AT$ expression appeared on day 7 in the ileum before weaning, and then decreased till day 30 but rose gradually again from day 60 to 150 (p<0.05).
( Bo Xu ),( Li Ming Dai ),( Jun Jun Li ),( Meng Deng ),( Hua Biao Miao ),( Jun Pei Zhou ),( Yue Lin Mu ),( Qian Wu ),( Xiang Hua Tang ),( Yun Juan Yang ),( Jun Mei Ding ),( Nan Yu Han ),( Zun Xi Huang 한국미생물 · 생명공학회 2016 Journal of microbiology and biotechnology Vol.26 No.1
Xylanases sourced from different bacteria have significantly different enzymatic properties. Therefore, studying xylanases from different bacteria is important to their applications in different fields. A potential xylanase degradation gene in Massilia was recently discovered through genomic sequencing. However, its xylanase activity remains unexplored. This paper is the first to report a xylanase (XynRBM26) belonging to the glycosyl hydrolase family (GH10) from the genus Massilia. The gene encodes a 383-residue polypeptide (XynRBM26) with the highest identity of 62% with the endoxylanase from uncultured bacterium BLR13. The XynRBM26 expressed in Escherichia coli BL21 is a monomer with a molecular mass of 45.0 kDa. According to enzymatic characteristic analysis, pH 5.5 is the most appropriate for XynRBM26, which could maintain more than 90% activity between pH 5.0 and 8.0. Moreover, XynRBM26 is stable at 37°C and could maintain at least 96% activity after being placed at 37°C for 1 h. This paper is the first to report that GH10 xylanase in an animal gastrointestinal tract (GIT) has salt tolerance, which could maintain 86% activity in 5 M NaCl. Under the optimum conditions, Km, Vmax, and kcat of XynRBM26 to beechwood xylan are 9.49 mg/ml, 65.79 μmol/min/mg, and 47.34 /sec, respectively. Considering that XynRBM26 comes from an animal GIT, this xylanase has potential application in feedstuff. Moreover, XynRBM26 is applicable to high-salt food and seafood processing, as well as other high-salt environmental biotechnological fields, because of its high catalytic activity in high-concentration NaCl.
Feng Chen,Xue-Lin Wang,Ke-Ming Wang,Zhen-Xiang Cheng,Huan-Chu Chen,Ding-Yu Shen 한국진공학회(ASCT) 2002 Journal of Korean Vacuum Science & Technology Vol.6 No.2
NaEr(WO₄)₂ is a new laser material. The planar optical waveguide was formed in NaEr(WO₄)₂ crystal by 2.6 MeV He^+ ion implantation at doses of 1.0-1.5×10^(16) ions/㎤ at room temperature. The effective refractive indices of the dark modes were measured using the prism coupling method. Four TE modes and five TM modes were observed in the waveguide. The refractive index profiles were analyzed using the reflectivity calculation method (RCM). The influence of heat treatment at moderate temperature on the refractive index profiles of the waveguide was also investigated. We used the TRIM’98 (Transport of Ions in Matter) code to simulate the damage profile in the NaEr(WO₄)₂ crystal by 2.6 MeV He^+ ion implantation which is helpful for a better understanding of the waveguide formation.
A Novel Bi-directional Promoter Cloned from Melon and Its Activity in Cucumber and Tobacco
( Cui Yan Wang ),( Dong Feng Ding ),( Rui Xiang Yan ),( Xiao Ju Yu ),( Wei Dong Li ),( Ming Gang Li ) 한국식물학회 2008 Journal of Plant Biology Vol.51 No.2
A bi-directional promoter, DP, was cloned by PCR amplification using the genomic DNA of melon as template. Analysis of its cis-acting elements in both directions revealed a series of inducible regulatory elements and some enhancer elements. To evaluate its transcriptional activity, DP in both directions was then cloned into vector pBI121 to replace the CaMV 35S promoter. DP in both directions also was inserted downstream of CaMV 35S to investigate whether the double promoter might affect expression of the uidA reporter gene at higher levels. Transient expression in cucumber leaves, stems, and fruits as well as in tobacco leaves and stems showed that DP in both directions drove transcription to much higher levels than did the single promoter CaMV 35S. However, activity of the double promoter was lower than the corresponding activity of the single promoter DP in both directions. These results demonstrate that DP is a natural bi-directional promoter, with much more activity than is found with the CaMV 35S promoter. Furthermore, in cucumber and tobacco, it is not suitable to insert DP in either direction downstream of the CaMV 35S promoter to form a double promoter.