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Park, Jin-Seu,Lee, Byung-Ryong,Jin, Li Hua,Kim, Choong-Kwon,Choi, Kyung-Soon,Bahn, Jae-Hoon,Lee, Kil-Soo,Kwon, Hyeok-Yil,Chang, Hyun-Woo,Baek, Nam-In,Lee, Hwang-Eunjoo,Kang, Jung-Hoon,Cho, Sung-Woo,Ch Korean Society for Biochemistry and Molecular Biol 2001 Journal of biochemistry and molecular biology Vol.34 No.2
Antioxidant enzymes, scavengers of the reactive oxygen intermediate (ROI), are involved in numerous defense systems in cells. In the present study, we investigated the effects of the hot-water extracts of two medicinally potent mushrooms (Ganoderma lucidum and Phellinus linteus) on the activity and expression of antioxidant enzymes in vitro and in vivo. The mushroom extracts stimulated the catalase activity in a dose-dependent manner in vitro, whereas the other antioxidant enzymes (such as superoxide dismutase (SOD), glutathione peroxidase (GPx)) were unaffected by the extracts. The catalytic activity of catalase in the liver and brain was significantly increased after the oral treatment of the mushroom extracts (2.5 g/kg) to ICR mice for 2 months. Western blot analysis of the liver and brain tissues revealed that the expression level of catalase in the mice, treated with both mushroom extracts, was significantly increased compared to that of the control mice. However, the level of the SOD expression in the mice treated with the natural product extracts was unchanged under the same experimental conditions. Although the mechanisms for the stimulatory effect of the catalase expression by these extracts remains unclear, these results suggest that the ingredients of the Ganoderma lucidum and Phellinus linteus extracts act as an activator of catalase, and regulate the expression of catalase at the translational or transcriptional level.
Park, Lee-Jin,Ju, Sung-Mi,Song, Ha-Yong,Lee, Ji-Ae,Yang, Mi-Young,Kang, Young-Hee,Kwon, Hyung-Joo,Kim, Tae-Yoon,Choi, Soo-Young,Park, Jin-Seu Korean Society for Biochemistry and Molecular Biol 2006 Journal of biochemistry and molecular biology Vol.39 No.5
The infiltration of both monocyte and activated T cells in the skin is one of critical steps in the development of UVB-induced inflammation. Upregulation of adhesion molecules such as intercellular adhesion molecule 1 (ICAM-1) on the surface of keratinocytes plays an important role in this process. In this study, we examined the molecular mechanism responsible for UVB-induced expression of ICAM-1 and subsequent monocyte adhesion by keratinocyte. We observed that (1) UVB induced protein and mRNA expression of ICAM-1 in a dose- and time-dependent manner in human keratinocyte cell HaCaT; (2) UVB induced the translocation of NF-kappaB and inhibition of NF-kappaB by NF-kappaB inhibitors suppressed UVB-induced mRNA and protein expression of ICAM-1; (3) UVB increased the intracellular level of reactive oxygen species (ROS) by HaCaT cells; (4) UVB-induced increase of intracellular ROS level was suppressed by pre-treatment with diphenyl iodonium (DPI) and N-acetyl cysteine (NAC); and (5) inhibition of UVB-induced ROS production by DPI or NAC suppressed UVB-mediated translocation of NF-kappaB, expression of ICAM-1 and subsequent monocyte adhesion in HaCaT cells. These results suggest that UVB-induced ROS is involved in the translocation of NF-kappaB which is responsible for expression of ICAM-1 and subsequent increased monocyte adhesion in human keratinocyte.
Park, Jin-Seu,Lee, Han-Gyu,Lee, Yoon,Kang, Young-Hee,Rhim, Hyang-Shuk,Choi, Soo-Young Korean Society for Biochemistry and Molecular Biol 2000 Journal of biochemistry and molecular biology Vol.33 No.4
The human immunodeficiency virus type 1 (HIV-1), transactivator of transcription (Tat), is one of the viral gene products that is essential for HIV-1 replication. The HIV-l Tat protein regulates transcription from an HIV-1 long terminal repeat (LTR) and affects the gene expression of cellular proteins during infection. In order to develop an expression system to overexpress and simply purify HIV-1 Tat proteins, the HIV-1 Tat coding sequences that contain one or two exons were amplified using PCR and cloned into a pET vector, which contains a consecutive stretch of six histidine residues at the amino-terminus. The reconstituted vectors were overexpressed in the E. coli strain and the soluble recombinant proteins were purified to be homogeneity in a single step by $Ni^{+2}-nitrilotriacetic$ acid Sepharose chromatography under nondenaturing conditions. Recombinant HIV-1 Tat proteins were shown to transactivate the HIV-1 LTR promoter in a dose-dependent manner when introduced into mammalian cells. In addition, treatment of human endothelial cells with purified Tat proteins resulted in a significant increase in the level of vascular cell adhesion molecule-1 (VCAM-1) expression. These results indicate that the recombinant HIV-1 Tat proteins are active in transactivating viral and cellular promoters. The expression and purification system described in this study will facilitate in characterizing the biological functions of the Tat proteins.
Effect of Chlorella vulgaris on Immune-enhancement and Cytokine Production in vivo and in vitro
Hyo-Jin An,Hong-Kun Rim,Jong-Hyun Lee,Min-Jun Seo,Jin-Woo Hong,Na-Hyung Kim,Noh-Yil Myung,Phil-Dong Moon,In-Young Choi,Ho-Jeong Na,Su-Jin Kim,Hyun-Ja Jeong,Hyeung-Suk Park,Jae-Gab Han,Jae-Young Um,Seu 한국식품과학회 2008 Food Science and Biotechnology Vol.17 No.5
The object of this study was to investigate the immune-enhancing effects of Chlorella vulgaris (CV) on a deteriorated immune function by a protein-energy malnutrition (PEM) diet. Unicellular algae, CV were used as a biological response modifier. Male C57BL/6J mice were fed for 15 days with standard diet or a PEM diet, which is associated with decreased host immune defense. After 8 days, mice in the PEM diet group were orally administered by 0.05, 0.1, and 0.15 g/kg body weight of CV or distilled water. Nutritional parameters, and interferon (IFN)-γ levels were significantly increased in the blood serum of the CV (0.15 g/kg)-treated group (29.6±2.8 pg/mL) compared to the non-treated PEM group (4.1±0.4 pg/mL, p<0.05). In addition, cell proliferation and production of cytokines were investigated via a CV (0.01, 0.1, and 1 mg/mL) treatment using a human T cell line MOLT-4 cell. The CV treatment (1 mg/mL) significantly increased the production of both IFN-γ and interleukin (IL)-2 (51.3±3.4 and 285.9±18.8 pg/mL, respectively) compared to the control (51.3±3.4 and 442.6±14.3 pg/mL, respectively), but did not affect the production of IL-4. These results suggest that CV may be useful in improving the immune function.
Transduced PEP-1-Grb7 Fusion Protein Suppressed LPS-induced COX-2 Expression
An, Jae-Jin,Kim, So-Young,Lee, Sun-Hwa,Kim, Dae-Won,Ryu, Hea-Jin,Yeo, Seung-Il,Jang, Sang-Ho,Kwon, Hyung-Joo,Kim, Tae-Yoon,Lee, Sang-Chul,Poo, Ha-Ryoung,Cho, Sung-Woo,Lee, Kil-Soo,Park, Jin-Seu,Eum, W Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.2
Although the incidence and severity of atopic dermatitis (AD) is steadily increasing at an alarming rate, its pathogenic mechanisms remain poorly understood yet. Recently, we found that the expression of Grb7 protein was markedly decreased in AD patients using proteomic analysis. In the present study, human Grb7 gene was fused with PEP-1 peptide in a bacterial expression vector to produce a genetic in-frame PEP-1-Grb7 fusion protein. The expressed and purified PEP-1-Grb7 fusion proteins transduced efficiently into skin cells in a time- and dose-dependent manner when added exogenously in culture media. Once inside the cells, the transduced PEP-1-Grb7 protein was stable for 48 h. In addition, transduced PEP-1-Grb7 fusion protein markedly increased cell viability in macrophage RAW 264.7 cells treated with LPS by inhibition of the COX-2 expression level. These results suggest that the PEP-1-Grb7 fusion protein can be used in protein therapy for inflammatory skin disorders, including AD.