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( Sung Hoon Choi ),( Mi Sol Lee ),( Shin Won Hwang ),( Jun Yong Park ),( Seung Up Kim ),( Sang Hoon Ahn ),( Weon Sang Ro ),( Kwang Hyub Han ) 대한간학회 2012 춘·추계 학술대회 (KASL) Vol.2012 No.-
Objectives: HIF-1β (ARNT) formed dimerization of HIF-1α, involved in various aspects of cancer biology, including proliferation and survival under hypoxic condition. This is an in vitro study that investigated the mechanism by which small interference HIF-1β (siHIF-1β) inhibits HIF-1α dimerization and thus it lead to suppress tumor cell growth. Method: Three HCC cell lines (HepG2, Huh 7 and Hep3B) were transfected with HIF-1β coding siRNA and cultured under hypoxic conditions (1% O2, 24 hours). Following transfection, the expression levels of HIF-1β , HIF-1α, and growth factors were examined through immuno-blotting. In addition, tumor growth was measured by MTT assay and tumor activity was measured by TUNEL, tumor invasion and migration assay. Results: The inhibition of HIF-1β by small interference RNA (siHIF-1β) led to suppression of tumor cell growth through inhibition of HIF dimerization under hypoxia condition. This effect was increased and maximized at 48 hrs after treatment of HIF-1β coding siRNA. Inhibition of HIF dimerization through treatment of siHIF-1β also regulated the expression of tumor growth related factors (VEGF, EGF and HGF). Inhibition of HIF- dimerization precluded tumor invasion and migration in variable HCC cell lines. Conclusions: Inhibition of HIF dimerization by siHIF-1β may lead to anti-tumor effects in a hypoxic condition of tumor environment.
( Sung Hoon Choi ),( Hye Won Shin ),( Jun Yong Park ),( Ji Young Yoo ),( Do Young Kim ),( Weon Sang Ro ),( Chae Ok Yun ),( Kwang Hyub Han ) 대한간학회 2010 Clinical and Molecular Hepatology(대한간학회지) Vol.16 No.3
Background/Aims: Hypoxia-inducible factor-1α (HIF-1α) is a central transcriptional factor involved in the cellular responses related to various aspects of cancer biology, including proliferation, survival, and angiogenesis, and the metabolism of the extracellular matrix in hypoxia. This study evaluated whether adenovirus-mediated small hairpin RNA (shRNA) against HIF-1α (shHIF-1α) inhibits cell proliferation and angiogenesis in hepatocellular carcinoma (HCC) cell lines. Methods: Knockdown of HIF-1α expression was constructed by adenovirus-mediated RNA interference tools, and HCC cell lines infected with shHIF-1α coding virus were cultured under a hypoxia condition (1% O2) for 24 hours. Following infection, the expression levels of HIF-1α, angiogenesis factors, and matrix metalloproteinase (MMP) were examined using Western blotting. Cell proliferation and angiogenesis were measured by a cell proliferation assay (MTT assay) and an angiogenesis-related assay (invasion and tube-formation assay), respectively. Results: Adenovirus mediated inhibition of HIF-1α induced suppression of tumor growth in HCC cell lines. It also down-regulated the expression of angiogenesis factor and MMP proteins. Angiogenesis as well as mobility of vascular cells to tumor was suppressed by adenovirus-mediated shHIF-1α-infected groups in human umbilical vein endothelial cells (HUVECs). Conclusions: These data suggest that adenovirus-mediated inhibition of HIF-1α inhibits the invasion, tube formation, and cell growth in HUVECs and HCC cells. (Korean J Hepatol 2010;16:280-287)
( Sung Hoon Choi ),( Mi Sol Lee ),( Shin Won Hwang ),( Jun Yong Park ),( Seung Up Kim ),( Sang Hoon Ahn ),( Weon Sang Ro ),( Kwang Hyub Han ) 대한간학회 2012 춘·추계 학술대회 (KASL) Vol.2012 No.1
Objectives: HIF-1β (ARNT) formed dimerization of HIF-1α, involved in various aspects of cancer biology, including proliferation and survival under hypoxic condition. This is an in vitro study that investigated the mechanism by which small interference HIF-1β (siHIF-1β) inhibits HIF-1α dimerization and thus it lead to suppress tumor cell growth. Method: Three HCC cell lines (HepG2, Huh 7 and Hep3B) were transfected with HIF-1β coding siRNA and cultured under hypoxic conditions (1% O2, 24 hours). Following transfection, the expression levels of HIF-1β , HIF-1α, and growth factors were examined through immuno-blotting. In addition, tumor growth was measured by MTT assay and tumor activity was measured by TUNEL, tumor invasion and migration assay. Results: The inhibition of HIF-1β by small interference RNA (siHIF-1β) led to suppression of tumor cell growth through inhibition of HIF dimerization under hypoxia condition. This effect was increased and maximized at 48 hrs after treatment of HIF-1β coding siRNA. Inhibition of HIF dimerization through treatment of siHIF-1β also regulated the expression of tumor growth related factors (VEGF, EGF and HGF). Inhibition of HIF- dimerization precluded tumor invasion and migration in variable HCC cell lines. Conclusions: Inhibition of HIF dimerization by siHIF-1β may lead to anti-tumor effects in a hypoxic condition of tumor environment.
( Do Young Kim ),( Sook In Chung ),( Weon Sang Ro ),( Yong Han Paik ),( Young Nyun Park ),( Sang Hoon Ahn ),( Jung Gyu Park ),( Hee Dong Park ),( Kwan Sik Lee ),( Kwang Hyub Han ) 대한간학회 2012 춘·추계 학술대회 (KASL) Vol.2012 No.1
Background/Aim: To see combined anti-fibrosis effect when lithospermate B (LAB), an anti-oxidant, and Nivocasan, a caspase inhibitor, were simultaneously administered in comparison with either compound. Methods: Hepatic fibrosis was induced in SD rats by thioacetamide (TAA). In fibrosis-preventive experiment, rats were injected with TAA and fed on LAB and Nivocasan at the same time. Grouping was; Normal control (N), Normal+ LAB+ Nivocasan (NLN), TAA control (T), TAA+LAB (TL), TAA+ Nivocasan (TN), TAA+LAB+Nivocasan (TLN). In fibrosisreversal experiment, rats were first treated with TAA, and then LAB and Nivocasan were fed. Grouping was; TAA control (F), TAA+LAB (FL), TAA+Nivocasan (FN), and TAA+LAB+ Nivocasan (FLN). Fibrotic area was evaluated quantitatively by computerized morphometry. Apoptosis was assessed using TUNEL assay, and immunohistochemical staining for malondialdehyde (MDA) and 4-hydroxy-2-nonenal (4HNE) was performed to assess oxidative stress. Real-time quantitative PCR was used to determine expression of fibrosis-related genes. Results: The degree of hepatic fibrosis was significantly reduced in group TLN (4.9%) compared to TL (6.3%) or TN (6.7%) (p < 0.001). These results were similarly observed in fibrosisreversal experiment. Treatment with each compound significantly decreased fibrosis-related gene expression such as type I collagen α1 (col1α1), α-SMA, and TGF-β1 (p < 0.05). Co-treat ment with LAB and Nivocasan further reduced col1α1 expression compared with either compound in both fibrosispreventive and reversal experiment. TUNEL assay revealed that hepatocyte apoptosis significantly decreased in group TN and TLN compared to TL (p < 0.001). Similarly, apoptosis reduced significantly in group FN and FLN compared to FL (p < 0.001). Immunohistochemistry showed decrease of MDA and 4HNE, reflecting amelioration of oxidative stress in both fibrosispreventive and reversal experiment, when LAB or LAB+ Nivocasan was administered compared with Nivocasan alone (p < 0.05). Conclusion: Simultaneous administration of LAB and Nivocasan to suppress oxidative stress and apoptosis resulted in an enhanced effect on inhibition of hepatic fibrosis in rats.
Involvement of heme oxygenase-1 in Korean colon cancer.
Kang, Kyoung Ah,Maeng, Young Hee,Zhang, Rui,Yang, Young Ro,Piao, Mei Jing,Kim, Ki Cheon,Kim, Gi Young,Kim, Young Ree,Koh, Young Sang,Kang, Hee Kyoung,Hyun, Chang Lim,Chang, Weon Young,Hyun, Jin Won Saikon Pub. Co 2012 TUMOR BIOLOGY Vol.33 No.4
<P>Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress. The aim of the present study was to determine the expression level and activity of HO-1 in Korean colon cancer tissues and cell lines. HO-1 protein expression was higher (>1.5-fold) in tumor tissues than in adjacent normal tissues in 14 of 20 colon cancer patients, and HO-1 protein expression was closely correlated with HO-1 enzyme activity in cancer tissues. Immunohistochemical data confirmed that HO-1 protein was expressed at a higher level in colon cancer tissues than in normal mucosa. Furthermore, HO-1 mRNA and protein expression and enzyme activity were higher in the colon cancer cell lines Caco-2, SNU-407, SNU-1033, HT-29, and SW-403 than in the normal fetal human colon cell line FHC. Treatment with the HO-1 inhibitor zinc protoporphyrin decreased the viability of colon cancer cell lines. These data indicate that HO-1 may serve as a clinically useful biomarker of colon cancer and as a target for anticolon cancer drugs.</P>