• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.86-86
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• 1995

No Abstract, See Full Text

• Molecules and Cells
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• v.28 no.1
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• pp.49-55
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• 2009

Hepatitis delta virus (HDV) infection causes fulminant hepatitis and liver cirrhosis. To elucidate the molecular mechanism of HDV pathogenesis, we examined the effects of HDV viral proteins, the small hepatitis delta antigen (SHDAg) and the large hepatitis delta antigen (LHDAg), on $NF-{\kappa}B$ signaling pathway. In this study, we demonstrated that $TNF-{\alpha}-induced$ $NF-{\kappa}B$ transcriptional activation was increased by LHDAg but not by SHDAg in both HEK293 and Huh7 cells. Furthermore, LHDAg promoted TRAF2-induced $NF-{\kappa}B$ activation. Using coimmunoprecipitation assays, we demonstrated that both SHDAg and LHDAg interacted with TRAF2 protein. We showed that isoprenylation of LHDAg was not required for the increase of $NF-{\kappa}B$ activity. We further showed that only LHDAg but not SHDAg increased the $TNF-{\alpha}-mediated$ nuclear translocation of p65. This was accomplished by activation of $I{\kappa}B_{\alpha}$ degradation by LHDAg. Finally, we demonstrated that LHDAg augmented the COX-2 expression level in Huh7 cells. These data suggest that LHDAg modulates $NF-{\kappa}B$ signaling pathway and may contribute to HDV pathogenesis.

• Asian Pacific Journal of Cancer Prevention
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• v.17 no.10
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• pp.4643-4646
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• 2016

The CC chemokine receptor 5 (CCR5) delta 32 allele results in a nonfunctional form of the chemokine receptor and has been implicated in a variety of immune-mediated diseases. $CCR5{\Delta}32$ may also predispose one to chronic liver disease or be linked with resistance to HBV infection. This study was undertaken to investigate any association between CCR5 polymorphism with resistance to hepatitis B or susceptibility to HBV infection. A total of 812 Iranian individuals were enrolled into two groups: HBV infected cases (n=357), who were HBsAg-positive, and healthy controls (n=455). We assessed polymorphisms in the CCR5 gene using specific CCR5 oligonucleotide primers surrounding the breakpoint deletion. Genotype distributions of the HBV infected cases and healthy controls were determined and compared. The CCR5/CCR5 (WW) and $CCR5/CCR5{\Delta}32$ (W/D) genotypes were found in (98%) and (2%) of HBV infected cases, respectively. The $CCR5{\Delta}32/{\Delta}32$genotype was not found in HBV infected cases. Genotype distributions of CCR5 in healthy controls were W/W genotype in (87.3%), W/D genotype in (11.2%) and D/D genotype in (1.5%). Heterozygosity for $CCR5/CCR5{\Delta}32$ (W/D) in healthy controls was greater than in HBV infected cases (11.2% vs 2%, p < 0.001). W/D and D/D genotypes were more prominent in healthy controls than in HBV infected cases. This study provides evidence that the $CCR5{\Delta}32$ polymorphism may have a protective effect in resistance to HBV infection at least in the Iranian population.

• Molecules and Cells
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• v.25 no.4
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• pp.545-552
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• 2008

A hepadnaviruses replicates its DNA genome via reverse transcription of an RNA template (pregenomic RNA or pgRNA), which has a cap structure at the 5' end and a poly(A) tail at the 3' end. We have previously shown that the 5' cap is indispensable for encapsidation of the pgRNA. A speculative extension of the above finding is that the cap contributes to encapsidation via its interaction with the poly(A) tail, possibly involving eIF4E-eIF4G-PABP interaction. To test this hypothesis, poly(A)-less pgRNAs were generated via cleavage by a cis-acting hepatitis delta virus ribozyme sequence. We found that accumulation of the poly(A)-less pgRNA was markedly diminished, mostly likely due to its reduced stability. Importantly, however, the remaining poly(A)-less pgRNAs were nonetheless encapsidated and reverse transcribed normally when the reduced stability was taken account. Our finding clearly contradicts the notion that the poly(A) tail has any function in encapsidation and viral reverse transcription.

• BMB Reports
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• v.37 no.6
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• pp.741-748
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• 2004

The hepatitis C virus is associated with the development of liver cirrhosis and hepatocellular carcinomas. Among the 10 polyproteins produced by the virus, no function has been clearly assigned to the non-structural 5A (NS5A) protein. This study was designed to identify the hepatocellular proteins that interact with NS5A of the HCV. Yeast two-hybrid experiments were performed with a human liver cDNA prey-library, using five different NS5A derivatives as baits, the full-length NS5A (NS5A-F, amino acid (aa) 1~447) and its four different derivatives, denoted as NS5A-A (aa 1~150), -B (aa 1~300), -C (aa 300~447) and D (aa 150~447). NS5A-F, NS5A-B and NS5A-C gave two, two and 10 candidate clones, respectively, including an AHNAK-related protein, the secreted frizzled-related protein 4 (SFRP4), the N-myc downstream regulated gene 1 (NDRG1), the cellular retinoic acid binding protein 1 (CRABP-1), ferritin heavy chain (FTH1), translokin, tumor-associated calcium signal transducer 2 (TACSTD2), phosphatidylinositol 4-kinase (PI4K) and $centaurin{\delta}$ 2 ($CENT{\delta}2$). However, NS5A-A produced no candidates and NS5A-D was not suitable as bait due to transcriptional activity. Based on an in vitro binding assay, CRABP-1, PI4K, $CENT{\delta}2$ and two unknown fusion proteins with maltose binding protein (MBP), were confirmed to interact with the glutathione S-transferase (GST)/NS5A fusion protein. Furthermore, the interactions of CRABP-1, PI4K and $CENT{\delta}2$ were not related to the PXXP motif (class II), as judged by a domain analysis. While their biological relevance is under investigation, the results contribute to a better understanding of the possible role of NS5A in hepatocellular signaling pathways.

• Journal of Yeungnam Medical Science
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• v.2 no.1
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• pp.211-220
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• 1985

Serum HBsAg, AntiHBs, HBeAg, AntiHBe and AntiHBc were detected by radioimmunoassay in 39 patients with acute viral hepatitis, 79 patients with chronic hepatitis, 30 patients with liver cirrhosis, 16 patients with primary hepatocellular carcinoma, 14 patients of HBsAg carriers and 129 cases of controls:78 cases of normal level of SGOT, SGPT, and 51 cases of elevated level of SGOT, SGPT. Following results were obtained: 1. HBsAg was detected in 66.7% of acute viral hepatitis, 63.3% of chronic hepatitis, 36.7% of liver cirrhosis, 81.3% of primary hepatocellular carcinoma and 27.1% of controls. 2. AntiHBs was positive in 0% of acute viral hepatitis, 21.5% of chronic hepatitis, 36.7% of liver cirrhosis, 31.3% of primary hepatocellular carcinoma, 0% of carrier and 44.2% of controls. 3. HBeAg was detected in 45.6% of chronic hepatitis, 23.3% of liver cirrhosis and 31.3% of primary hepatocellular carcinoma. 4. Among chronic liver diseases, antiHBe was positive in 56.3% of primary hepatocellular carcinoma, 23.3% of liver cirrhosis and 20.3% of chronic hepatitis. 5. AntiHBc was detected in most of all examines and the significance of presence of AntiHBc does not seem to represent liver disease itself but the evidence of infection of HBV. 6. Among 14 HBV carriers, 6 cases presented with abnormal SGOT, SGPT. 7. All HBV markers were negative in 5.1% of acute viral hepatitis, 5.1% of chronic hepatitis and 14.7% of controls: 17.6% of subjects with abnormal SGOT, SGPT and 12.8% of subjects with normal SGOT, SGPT. 8. Beside of HBV, other causes, such as non A, non B virus, Delta-agent, other viruses or related factors should be excluded among the patients with evidence of HBV infection associated with elevation of SGOT & SGPT.

• Journal of Life Science
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• v.13 no.5
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• pp.551-558
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• 2003

Hepatitis C Virus (HCV) is associated with a severe liver disease and increased frequency in the development of hepatocellular carcinoma. Overexpression of HCV core protein is known to transform fibroblast cells. Phospholipase D (PLD) activity is commonly elevated in response to mitogenic signals, and PLD has been also reported to be overexpressed and hyperactivated in some human cancer. The aim of this study was to understand how PLD can be regulated in HCV core protein-transformed NIH3T3 mouse fibroblast cells. We observed that in unstimulated state, basal PLD activity was higher in NIH3T3 cells overexpressing HCV core protein than in vector-transfected cells. Although expression of PLD and protein kinase C (PKC) in core protein-transformed cells was similar with that of control cells, phorbol 12-myristate 13-acetate (PMA), which is known to activate PKC, stimulated significantly PLD activity in core protein-transformed cells, compared with that of the control cells. PLD activity assay using PKC isozyme-specific inhibitor, and PKC translocation experiment showed that PKC-$\delta$ was mainly involved in the PMA-induced PLD activation in the core-transformed cells. Taken together, these results suggest that PLD might be implicated in core protein-induced transformation.

• Korean Journal of Poultry Science
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• v.46 no.1
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• pp.31-37
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• 2019

A chicken clathrin-associated adaptor protein $3-{\delta}$ subunit 2 (AP3S2) is a subunit of AP3, which is involved in cargo protein trafficking to target membrane with clathrin-coated vesicles. AP3S2 may play a role in virus entry into host cells through clathrin-dependent endocytosis. AP3S2 is also known to participate in metabolic disease developments of progressions, such as liver fibrosis with hepatitis C virus infection and type 2 diabetes mellitus. Chicken AP3S2 (chAP3S2) gene was originally identified as one of the differentially expressed genes (DEGs) in chicken kidney which was fed with different calcium doses. This study aims to characterize the molecular characteristics, gene expression patterns, and transcriptional regulation of chAP3S2 in response to the stimulation of Toll-like receptor 3 (TLR3) to understand the involvement of chAP3S2 in metabolic disease in chicken. As a result, the structure prediction of chAP3S2 gene revealed that the gene is highly conserved among AP3S2 orthologs from other species. Evolutionarily, it was suggested that chAP3S2 is relatively closely related to zebrafish, and fairly far from mammal AP3S2. The transcriptional profile revealed that chAP3S2 gene was highly expressed in chicken lung and spleen tissues, and under the stimulation of poly (I:C), the chAP3S2 expression was down-regulated in DF-1 cells (P<0.05). However, the presence of the transcriptional inhibitors, BAY 11-7085 (Bay) as an inhibitor for nuclear factor ${\kappa}B$ ($NF{\kappa}B$) or Tanshinone IIA (Tan-II) as an inhibitor for activated protein 1 (AP-1), did not affect the expressional level of chAP3S2, suggesting that these transcription factors might be dispensable for TLR3 mediated repression. These results suggest that chAP3S2 gene may play a significant role against viral infection and be involved in TLR3 signaling pathway. Further study about the transcriptional regulation of chAP3S2 in TLR3 pathways and the mechanism of chAP3S2 upon virus entry shall be needed.