Journal of Microbiology

Journal Article

Hepatitis C virus infection stimulates transforming growth factor-β1 expression through up-regulating miR-192: Ji Hyun Kim , Chang Ho Lee , Seong-Wook Lee; J. Microbiol. 2016;54(7):520-526. Published online June 28, 2016; DOI: https://doi.org/10.1007/s12275-016-6240-3

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The objective of this study was to determine the molecular mechanisms underlying chronic liver injury and fibrosis caused by hepatitis C virus (HCV). This study revealed that miR-192 expression was induced by HCV infection without affecting viral replication. However, viral-induced miR-192 up-regulated transforming growth factor-β1 (TGF-β1) expression in liver cells at transcriptional level. TGF-β1 stimulation by HCV-induced miR-192 was caused through ZEB1 down-regulation and TGF-β1 increased miR-192 level via positive feedback pathway. Increase in miR-192 expression by HCV infection was due to HCV core protein released and/or expressed by viral infection. TGF-β1 promoter activity was also increased by HCV core protein in liver cells. Taken together, HCV infection resulted in increased TGF-β1 transcription in hepatocytes through ZEB1 down-regulation by HCV core-mediated miR-192 stimulation. Importantly, miR-192 inhibition with anti-miR-192 rescued ZEB1 expression down-regulated by HCV infection, thus reducing the level of TGF-β1 expression increased by HCV infection in hepatocytes. These results suggest a novel mechanism of HCV-mediated liver fibrogenesis with miR-192 being a potential molecular target to ameliorate viral pathogenesis.

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Expression of immunologically active porcine recombinant TGF-β1 precursor protein in baculovirus system: Lim, Hyun , Kim, Pyeung Hyeun , Chun, Gie Taek , Choi, Eui Yul , Yie, Se Won; J. Microbiol. 1997;35(4):341-346.

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Abstract: In order to express recombinant porcine TGF-β1 protein in a baculovirus expression system the entire TGF-β1 gene containing extra amino acids at the N terminus was cloned into pFBa and pFBb of the Bac-To-Bac^TM baculovirus expression system. One of the clones contained 106 extra amino acids and was designated pFBa-106 TGF-β1, and the other had 28 extra amino acids and was designated pFBb-28 TGF-β1. The orientation of the gene was identified with restriction enzyme mapping and PCR with internal TGF-β1 primers. Sf-9 cells were infected at a m.o.i. of 10 by the recombinant viruses generated from the two expected sizes of 55 kD and 46.4kD. these precursor forms of TGF-β1 with a polyclonal antibody against human TGF-β1. No mature form of TGF-β1 protein was detected on SDS gels and an immunoblot indicated that TGF-β1 precursor is not properlu processed in insect cells.

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