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13 results on '"Kim, Im Gyu"'

3. Cyclosporine A inhibits TGF-β2-induced myofibroblasts of primary cultured human pterygium fibroblasts

Author

Gum, Sang Il, Kim, Yeoun-Hee, Jung, Jae-Chang, Kim, Im Gyu, Lee, Jun Seok, Lee, Kyoo Won, and Park, Young Jeung

Subjects
Male, 0301 basic medicine, Oligonucleotides, Biophysics, Inflammation, Pterygium, Biochemistry, Transforming Growth Factor beta2, 03 medical and health sciences, 0302 clinical medicine, Downregulation and upregulation, Laminin, Humans, Medicine, Myofibroblasts, Molecular Biology, Cells, Cultured, Messenger RNA, biology, business.industry, Cell Differentiation, Muscle, Smooth, Cell Biology, Fibroblasts, Actins, eye diseases, Fibronectins, Fibronectin, 030104 developmental biology, Microscopy, Fluorescence, Immunology, Cyclosporine, 030221 ophthalmology & optometry, Cancer research, biology.protein, Female, sense organs, medicine.symptom, business, Myofibroblast, Immunosuppressive Agents, Software, Intracellular, Signal Transduction, Transforming growth factor
Abstract

Cyclosporine A (CsA), an immunomodulatory drug, and is increasingly used to treat moderate dry eye syndrome and ocular surface inflammation. However, any inhibitory effect on differentiation of fibroblasts to myofibroblasts remains unclear. Here, we show that the inhibitory effect of CsA on transforming growth factor-beta2 (TGF-β2)-induced myofibroblasts in primary cultured human pterygium fibroblasts. CsA significantly decreased mRNA and protein expression of myofibroblast-related markers including α-SMA, laminin, and fibronectin. These findings were supported by the results from immunofluorescence staining. Taken together, these results indicate the therapeutic potential of CsA against pterygium progression. Further studies are necessary to elucidate the precise intracellular signal mechanism responsible for CsA-induced downregulation of myofibroblast markers in pterygium fibroblasts.

Published
2017

13. Engineered Escherichia coli with periplasmic carbonic anhydrase as a biocatalyst for CO2 sequestration.

Author

Jo BH, Kim IG, Seo JH, Kang DG, and Cha HJ

Subjects
Base Sequence, Biocatalysis, Blotting, Western, Carbon Sequestration genetics, Carbonic Anhydrases metabolism, Cell Fractionation, DNA Primers genetics, Escherichia coli metabolism, Molecular Sequence Data, Periplasm enzymology, Polymerase Chain Reaction, Sequence Analysis, DNA, Carbon Dioxide metabolism, Carbon Sequestration physiology, Carbonic Anhydrases genetics, Escherichia coli genetics, Genetic Engineering, Neisseria gonorrhoeae enzymology
Abstract

Carbonic anhydrase is an enzyme that reversibly catalyzes the hydration of carbon dioxide (CO2). It has been suggested recently that this remarkably fast enzyme can be used for sequestration of CO2, a major greenhouse gas, making this a promising alternative for chemical CO2 mitigation. To promote the economical use of enzymes, we engineered the carbonic anhydrase from Neisseria gonorrhoeae (ngCA) in the periplasm of Escherichia coli, thereby creating a bacterial whole-cell catalyst. We then investigated the application of this system to CO2 sequestration by mineral carbonation, a process with the potential to store large quantities of CO2. ngCA was highly expressed in the periplasm of E. coli in a soluble form, and the recombinant bacterial cell displayed the distinct ability to hydrate CO2 compared with its cytoplasmic ngCA counterpart and previously reported whole-cell CA systems. The expression of ngCA in the periplasm of E. coli greatly accelerated the rate of calcium carbonate (CaCO3) formation and exerted a striking impact on the maximal amount of CaCO3 produced under conditions of relatively low pH. It was also shown that the thermal stability of the periplasmic enzyme was significantly improved. These results demonstrate that the engineered bacterial cell with periplasmic ngCA can successfully serve as an efficient biocatalyst for CO2 sequestration.

Published
2013
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