Browsing by Author "Sun, Yu-Ling"
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Item type:Item, An efficient Photobioreactors/Raceway circulating system combined with alkaline-CO2 capturing medium for microalgal cultivation(2018-10-01) ;Kuo, Chiu-Mei ;Jian, Jhong-Fu ;Sun, Yu-Ling ;Lin, Tsung-HsienYang, Yi-ChunHigh efficiency of microalgal growth and CO2 fixation in a Photobioreactors (PBRs)/Raceway circulating (PsRC) system combined with alkaline-CO2 capturing medium and operation was established and investigated. Compared with a pH 6 medium, the average biomass productivity of Chlorella sp. AT1 cultured in a pH 11 medium at 2L min(-1) circulation rate for 7 days increased by about 2-fold to 0.346g L-1 d(-1). The maximum amount of CO2 fixation and CO2 utilization efficiency of Chlorella sp. AT1 could be obtained at a PBRs to Raceway ratio of 1:10 in an indoor-simulated PsRC system. A similar result was also shown in an outdoor PsRC system with a 10-ton scale for microalgal cultivation. Under the appropriate circulation rate, the stable growth performance of Chlorella sp. AT1 cultured by long-term semi-continuous operation in the 10-ton outdoor PsRC system was observed, and the total amount of CO2 fixation was approximately 1.2kg d(-1) with 50% CO2 utilization efficiency.Item type:Item, Detection of chymase activity using a specific peptide probe conjugated onto gold nanoparticles(2018-01-01) ;Chang, Hui-Fang ;Sun, Yu-Ling ;Yeh, Fang-Yuan ;Tseng, I-HuaChang, Chia-ChuGold nanoparticles (AuNPs) can be applied in biosensors using fluorescence resonance energy transfer (FRET) technique. Based on this technique, we have established a sensitive and efficient biosensing method by modifying a peptide-probe onto AuNPs to detect proteinase enzyme activity in this study. This biosensing method was designed for chymase activity detection and applied in kidney disease diagnosis. In this study, 16 nm-AuNPs were used to construct the AuNPs-based fluorescence peptide probe (named AuNPs-peptide probe) for chymase activity determination. The peptide sequence is FITC-Acp-DRVYIHPFHLDDDDDC, which comprises a fluorophore at the N-terminal end, an enzyme (chymase) substrate (DRVYIHPFHL), a spacer (DDDDD) and cysteine (C) to conjugate to AuNPs surface. When the enzyme catalyzes the substrate sequence, the fluorophore drifts away from AuNPs and the fluorescence emitting signal can be excited at 495 nm and detected at 515 nm. The results indicate that the time required for the AuNPs-peptide probe for activity detection of chymase was only 15 min, and a linear correlation from 10 to 100 ng mL(-1) of chymase was acquired. The chymase reaction would be significantly inhibited by addition of specific chymase inhibitor chymostatin. The AuNPs-peptide probe was tested for the detection of high concentrations of trypsin and chymotrypsin, but only minor emitted fluorescence intensity was detected. According to these results, sensitivity and specificity of the AuNPs-peptide probe for chymase detection have been confirmed. AuNPs-peptide probe was successfully used for the detection of renal chymase activity; and the results indicate the pathogenically increased chymase activity in kidney tissue of nephropathic mice from aristolochic acid I treatment.Item type:Item, Effects of Diosgenin on Myometrial Matrix Metalloproteinase-2 and-9 Activity and Expression in Ovariectomized Rats(2011) ;Chang, Chi-Chen ;Kuan, Tang-Ching ;Hsieh, Yao-Yuan ;Ho, Ying-JuiSun, Yu-LingDiosgenin, a traditional Yam extraction, has been used in hormone replacement for menopausal women. We aimed to investigate the influences of diosgenin administration upon the MMP-2 and -9 activity and expression and reproductive hormones of ovariectomized (OVX) rats, a model of menopausal status. Seven-week old female Wistar rats with bilateral OVX or sham operation (controls) were divided and administered different dosages of diosgenin (0, 10, 50, or 100 mg/kg/day) for 8 weeks. Serum was then sampled for progesterone (P4) and estradiol (E2) assay and uterine horns harvested. Myometrial MMP-2 and -9 activity and expression were surveyed and myometrial collagen expression was also assayed. The results show higher body weight in OVX rats across the 8 weeks post surgery and no significant differences were noted among OVX or Sham rats with diosgenin supplements. There were lower P4 and E2 concentrations in OVX rats compared to Sham rats, and higher P4 concentration of Sham rats post diosgenin supplement. MMP-2 and -9 mRNA expression and activity was lower in OVX rats, although higher MMP-2 and lower MMP-9 activity/mRNA expression was observed in OVX rats post diosgenin supplementation. Collagen mRNA expression was higher in OVX rats compared to Sham controls, and diosgenin administration decreased collagen mRNA expression in OVX rats. In conclusion, diosgenin is associated with gelatinase expression and collagen metabolism in OVX rats. Diosgenin administration can partially reverse the effects of OVX upon MMP functions and hormone status. Adequate diosgenin supplement might modulate myometrial gelatinase expression and collagen metabolism in menopausal subjects.Item type:Item, Increased expression of extracellular matrix proteins in rapid atrial pacing-induced atrial fibrillation(2007-07-01) ;Lin, Chih-Sheng ;Lai, Ling-Ping ;Lin, Jiunn-Lee ;Sun, Yu-LingHsu, Chih-WeiBACKGROUND: Atria[ fibrillation (AF) is characterized by structural remodeling of the extracellular matrix (ECM) in cardiac atrium. OBJECTIVE: The purpose of this study was to gain further insight into atrial ECM remodeling at the molecular Level and to test whether altered expression of ECM proteins was associated with the disease. METHODS: Sustained AF was induced in nine adult pigs after 3-4 weeks of continuous rapid atrial pacing at a rate of 600 bpm. Histologic studies and immunohistochemical stain were performed to identify the potential pathologic substrate underlying abnormalities in atrial tissues with sustained AF. RESULTS: In the pathologic findings, the fraction of myocardial ECM (ECM%) was measured, with a significantly greater ECM% found in the AF group compared with the sham operated group (n = 6; i.e., pigs with normal sinus rhythm [SR]). A set of 9,182 genes was screened with cDNA microarray analysis. In AF animals, expression of 121 genes increased and 24 genes decreased by >= 1.75-fold compared with SR animals. Significant up-regulation of fibronectin-1 (4.9-fold), fibrillin-1 (3.1-fold), and fibromodulin (1.9-fold) in the fibrillating atria was confirmed by quantitative real-time reverse transcriptase-polymerase chain reaction. Western blot analysis revealed significantly increased atrial fibronectin-1, fibrillin-1, and fibromodulin in the AF group compared with the SR group (1.5-, 2.7-, and 2.1-fold, respectively). Immunohistochemical staining of AF tissue displayed increased accumulation of fibronectin-1 and fibrillin-1 in the atrial interstitial space. CONCLUSION: Increased expression of ECM proteins in fibrillating atria supports the hypothesis that ECM metabolism contributes to the development of AF.Item type:Item, Instillation of particulate matter 2.5 induced acute lung injury and attenuated the injury recovery in ACE2 knockout mice(2018-01-01) ;Lin, Chung-I ;Tsai, Chin-Hung ;Sun, Yu-Ling ;Hsieh, Wen-YehLin, ChangInhaled particulate matter 2.5 (PM2.5) can cause lung injury by inducing serious inflammation in lung tissue. Renin-angiotensin system (RAS) is involved in the pathogenesis of inflammatory lung diseases and regulates inflammatory response. Angiotensin-converting enzyme II (ACE2), which is produced through the angiotensin-converting enzyme (ACE)/angiotensin II (Ang II) axis, protects against lung disease. However, few studies have focused on the relationships between PM2.5 and ACE2. Therefore, we aimed to explore the role of ACE2 in PM2.5-induced acute lung injury (ALI). An animal model of PM(2.)5-induced ALI was established with wild type (C57BL/6, WT) and ACE2 gene knockout (ACE2 KO) mice. The mice were exposed to PM2.5 through intratracheal instillation once a day for 3 days (6.25 mg/kg/day) and then sacrificed at 2 days and 5 days after PM2.5 instillation. The results show that resting respiratory rate (RRR), levels of inflammatory cytokines, ACE and MMPs in the lungs of WT and ACE2 KO mice were significantly increased at 2 days postinstillation. At 5 days postinstillation, the PM2.5-induced ALI significantly recovered in the WT mice, but only partially recovered in the ACE2 KO mice. The results hint that PM(2.)5 could induce severe ALI through pulmonary inflammation, and the repair after acute PM2.5 postinstillation could be attenuated in the absence of ACE2. Additionally, our results show that PM2.5-induced ALI is associated with signaling p-ERK1/2 and p-STAT3 pathways and ACE2 knockdown could increase pulmonary p-STAT3 and p-ERK1/2 levels in the PM(2.)5-induced ALI.Item type:Item, Soluble Fusion Expression and Production of Rabbit Neutrophil Peptide-1 in Escherichia coli(2011-09-01) ;Sun, Yu-Ling ;Lin, Yi-Juain ;Lin, Chih-Sheng ;生物科技學系Department of Biological Science and TechnologyRabbit neutrophil peptide-1 (NP1) is a prototypic a-defensin with a broad antimicrobial spectrum. The Escherichia coli-preferential coding sequence of rabbit mature NP-1 (maNP1) was designed, amplified and cloned into plasmid pET32b(+) to construct an expression vector. pET32-maNP1. This expression vector was transformed into E. coli Rosetta-gami(DE3)pLysS for expressing the fusion protein, Trx-(His)(6)-maNP1, i.e., expressed maNP1 is sequentially downstream of a thioredoxin (Trx) and a (His)(6)-tag. The quantitative data showed that there were 52% and 4.5% of the fused Trx-(His)(6)-maNP1 expressed in the soluble and insoluble form in the E. cola carrying pET32-maNP1 with IPTG induction, respectively. The produced fusion protein was collected and purified by Ni-NTA resin, and then cleaved by enterokinsase to release maNP1 peptide. The purified recombinant maNP1 showed significantly antimicrobial activities against clinical bacteria, E. coli and Pseudomonas aeruginosa (Gram-negative) and Staphylococcus aureus and Bacillus subtilis (Gram-positive). The application of this expression approach represents a potential method to produce functional maNP1 by fusion protein expressed in E. coli.