Browsing by Author "Chang, Hui-Fang"

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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-Hsien
;
Yang, Yi-Chun
High 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.
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-Hua
;
Chang, Chia-Chu
Gold 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.
In Vitro and In Vivo Experimental Studies of PM2.5 on Disease Progression
(2018-07-01)
Cho, Ching-Chang
;
Hsieh, Wen-Yeh
;
Tsai, Chin-Hung
;
Chen, Cheng-Yi
;
Chang, Hui-Fang
Air pollution is a very critical issue worldwide, particularly in developing countries. Particulate matter (PM) is a type of air pollution that comprises a heterogeneous mixture of different particle sizes and chemical compositions. There are various sources of fine PM (PM2.5), and the components may also have different effects on people. The pathogenesis of PM2.5 in several diseases remains to be clarified. There is a long history of epidemiological research on PM2.5 in several diseases. Numerous studies show that PM2.5 can induce a variety of chronic diseases, such as respiratory system damage, cardiovascular dysfunction, and diabetes mellitus. However, the epidemiological evidence associated with potential mechanisms in the progression of diseases need to be proved precisely through in vitro and in vivo investigations. Suggested mechanisms of PM2.5 that lead to adverse effects and chronic diseases include increasing oxidative stress, inflammatory responses, and genotoxicity. The aim of this review is to provide a brief overview of in vitro and in vivo experimental studies of PM2.5 in the progression of various diseases from the last decade. The summarized research results could provide clear information about the mechanisms and progression of PM2.5-induced disease.
Renal chymase-dependent pathway for angiotensin II formation mediated acute kidney injury in a mouse model of aristolochic acid I-induced acute nephropathy
(2019-01-11)
Hsieh, Wen-Yeh
;
Chang, Teng-Hsiang
;
Chang, Hui-Fang
;
Chuang, Wan-Hsuan
;
Lu, Li-Che
Angiotensin-converting enzyme (ACE) is the primary enzyme that converts angiotensin I (Ang I) to angiotensin II (Ang II) in the renin-angiotensin system (RAS). However, chymase hydrates Ang I to Ang II independently of ACE in some kidney diseases, and it may play an important role. The present study investigated whether chymase played a crucial role in aristolochic acid I (AAI)-induced nephropathy. C57BL/6 mice were treated with AAI via intraperitoneal injection for an accumulated AAI dosage of 45 mg/kg body weight (BW) (15 mg/kg BW per day for 3 days). The animals were sacrificed after acute kidney injury development, and blood, urine and kidneys were harvested for biochemical and molecular assays. Mice exhibited increased serum creatinine, BUN and urinary protein after the AAI challenge. Significant infiltrating inflammatory cells and tubular atrophy were observed in the kidneys, and high immunocytokine levels were detected. Renal RAS-related enzyme activities were measured, and a significantly increased chymase activity and slightly decreased ACE activity were observed in the AAI-treated mice. The renal Ang II level reflected the altered profile of RAS enzymes and was significantly increased in AAI-treated mice. Treatment of AAI-induced nephropathic mice with an ACE inhibitor (ACEI) or chymase inhibitor (CI; chymostatin) reduced renal Ang II levels. The combination of ACEI and CI (ACEI+CI) treatment significantly reversed the AAI-induced changes of Ang II levels and kidney inflammation and injuries. AAI treatment significantly increased renal p-MEK without increasing p-STAT3 and p-Smad3 levels, and p-MEK/p-ERK1/2 signalling pathway was significantly activated. CI and ACEI+CI treatments reduced this AAI-activated signaling pathway. AAI-induced nephropathy progression was significantly mitigated with CI and ACEI+CI treatment. This study elucidates the role of RAS in the pathogenesis of AAI-induced nephropathy.