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Search Results: 1 - 10 of 3409 matches for " Seon-Ah Ha "
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p-Glycoprotein ABCB5 and YB-1 expression plays a role in increased heterogeneity of breast cancer cells: correlations with cell fusion and doxorubicin resistance
Ji Yang, Seon-Ah Ha, Yun-Sik Yang, Jin Kim
BMC Cancer , 2010, DOI: 10.1186/1471-2407-10-388
Abstract: Doxorubicin resistant human breast MCF-7 clones were generated. The doxorubicin-induced cell fusion events were examined. Heterokaryons were identified and sorted by FACS. In the development of doxorubicin resistance, cell-fusion associated genes, from the previous results of microarray, were verified using dot blot array and quantitative RT-PCR. The doxorubicin-induced expression patterns of pro-survival and pro-apoptotic genes were validated.YB-1 and ABCB5 were up regulated in the doxorubicin treated MCF-7 cells that resulted in certain degree of genomic instability that accompanied by the drug resistance phenotype. Cell fusion increased diversity within the cell population and doxorubicin resistant MCF-7 cells emerged probably through clonal selection. Most of the drug resistant hybrid cells were anchorage independent. But some of the anchorage dependent MCF-7 cells exhibited several unique morphological appearances suggesting minor population of the fused cells maybe de-differentiated and have progenitor cell like characteristics.Our work provides valuable insight into the drug induced cell fusion event and outcome, and suggests YB-1, GST, ABCB5 and ERK3 could be potential targets for the anti-cancer drug development against drug resistant breast cancer cells. Especially, the ERK-3 serine/threonine kinase is specifically up-regulated in the resistant cells and known to be susceptible to synthetic antagonists.The prognosis of breast cancer patients is closely associated with the response of the tumor cells to chemotherapy. Doxorubicin is one of the primary chemotherapeutic agents used for the treatment of breast cancer [1,2]. Various tumors initially respond to administered drugs, however, once the cancer cells could gain resistance during anticancer drug treatment, there are only a few treatment options [3,4]. Resistance to chemotherapy is believed to cause treatment failure in over 90% of the patients with metastatic cancer [5,6]. Multidrug resistant cancer cel
The bone morphogenetic protein antagonist gremlin 1 is overexpressed in human cancers and interacts with YWHAH protein
Hong Namkoong, Seung Shin, Hyun Kim, Seon-Ah Ha, Goang Cho, Soo Hur, Tae Kim, Jin Kim
BMC Cancer , 2006, DOI: 10.1186/1471-2407-6-74
Abstract: We used the differential display (DD) RT-PCR method using normal cervical, cervical cancer, metastatic cervical tissues, and cervical cancer cell lines to identify genes overexpressed in cervical cancers and identified gremlin 1 which was overexpressed in cervical cancers. We determined expression levels of gremlin 1 using Northern blot analysis and immunohistochemical study in various types of human normal and cancer tissues. To understand the tumorigenesis pathway of identified gremlin 1 protein, we performed a yeast two-hybrid screen, GST pull down assay, and immunoprecipitation to identify gremlin 1 interacting proteins.DDRT-PCR analysis revealed that gremlin 1 was overexpressed in uterine cervical cancer. We also identified a human gremlin 1 that was overexpressed in various human tumors including carcinomas of the lung, ovary, kidney, breast, colon, pancreas, and sarcoma. PIG-2-transfected HEK 293 cells exhibited growth stimulation and increased telomerase activity. Gremlin 1 interacted with homo sapiens tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, eta polypeptide (14-3-3 eta; YWHAH). YWHAH protein binding site for gremlin 1 was located between residues 61–80 and gremlin 1 binding site for YWHAH was found to be located between residues 1 to 67.Gremlin 1 may play an oncogenic role especially in carcinomas of the uterine cervix, lung, ovary, kidney, breast, colon, pancreas, and sarcoma. Over-expressed gremlin 1 functions by interaction with YWHAH. Therefore, Gremlin 1 and its binding protein YWHAH could be good targets for developing diagnostic and therapeutic strategies against human cancers.The identification of molecular alterations in cancerous and pre-cancerous cells has provided insight into the role of oncogenes and tumor suppressor genes in tumor initiation and progression [1]. Oncogenes are derived from highly conserved proto-oncogenes that are altered by chromosomal point mutations, gene amplifications, or gene rearrangements
Oncoprotein HCCR-1 expression in breast cancer is well correlated with known breast cancer prognostic factors including the HER2 overexpression, p53 mutation, and ER/PR status
Seon-Ah Ha, Youn Lee, Seung Shin, Hyun Kim, Sanghee Kim, Hong Namkoong, Hae Kim, Sang Jung, Yu Lee, Yeun Chung, Sang Jung, Jin Kim
BMC Cancer , 2009, DOI: 10.1186/1471-2407-9-51
Abstract: Oncogene HCCR-1 expression levels were determined in normal breast tissues, breast cancer tissues and cancer cell lines. We examined whether HCCR-1 protein expression in breast cancer is related to different biological characteristics, including ER, PR, p53 genotype, and HER2 status in 104 primary breast cancer tissues using immunohistochemical analyses.HCCR-1 was upregulated in breast cancer cells and tissues compared with normal breast tissues. In this study, overexpression of HCCR-1 was well correlated with known breast cancer prognostic markers including the presence of steroid receptors (ER and PR), p53 mutation and high HER2 overexpression. HCCR-1 was not detected in the ER-negative, PR-negative, p53 negative and low HER2 breast cancer tissues. These data indicate that the level of HCCR-1 in breast cancer tissues is relatively well correlated with known breast cancer factors, including the HER2 overexpression, p53 mutation, and ER/PR status.Determination of HCCR-1 levels as options for HER2 testing is promising although it needs further evaluation.Cells expressing HCCR-1 are tumorigenic in nude mice [1]. The functional role of this oncogene in tumorigenesis is manifested as a negative regulator of the p53 tumor suppressor [1]. In the previous study, we investigated HCCR-1 protein expression in breast cancer and the possibility of using HCCR-1 as a useful biomarker for human breast cancer [2]. We also examined whether HCCR-1 protein expression in breast cancer is related to different biological characteristics including ER, PR, p53 genotype, and the HER2 status. Northern and Western blot analyses and immunohistochemical studies indicate that the HCCR-1 mRNA and protein are overexpressed in breast cancer tissues compared to the normal breast tissues [1,2]. Serological studies revealed an 86.8% sensitivity for HCCR-1 in breast cancer, which was higher than 21.0% for CA15-3 [2,3]. The HCCR-1 assay has an advantage over CA15-3 in diagnosing breast cancer. These res
HCCR-1, a novel oncogene, encodes a mitochondrial outer membrane protein and suppresses the UVC-induced apoptosis
Goang-Won Cho, Seung Shin, Hyun Kim, Seon-Ah Ha, Sanghee Kim, Joo-Hee Yoon, Soo Hur, Tae Kim, Jin Kim
BMC Cell Biology , 2007, DOI: 10.1186/1471-2121-8-50
Abstract: To investigate the biological function of HCCR-1 in the cell, we predicted biological features using bioinformatic tools, and have identified a LETM1 homologous domain at position 75 to 346 of HCCR-1. This domain contains proteins identified from diverse species predicted to be mitochondrial proteins. Fluorescence microscopy and fractionation experiments showed that HCCR-1 is located in mitochondria in the COS-7, MCF-7 and HEK/293 cell lines, and subcompartamentally at the outer membrane in the HEK/293 cell line. The topological structure was revealed as the NH2-terminus of HCCR-1 oriented toward the cytoplasm. We also observed that the D1-2 region, at position 1 to 110 of HCCR-1, was required and sufficient for posttranslational mitochondrial import. The function of HCCR-1 on mitochondrial membrane is to retard the intrinsic apoptosis induced by UVC and staurosporine, respectively.Our experiments show the biological features of HCCR-1 in the cell, and suggest that uncontrolled expression of HCCR-1 may cause mitochondrial dysfunction that can result in resisting the UVC or staurosporine-induced apoptosis and progressing in the tumor formation.Mitochondria are responsible for a number of metabolic tasks in eukaryotic cells. Their primary function is to generate energy through oxidative phosphorylation in organelles. Mitochondria also play an important role in other biological activities such as programmed cell death [1], calcium signaling and generation of detoxification of reactive oxygen species [2].Mitochondria consist of four subcompartments – an outer membrane, an inner membrane, an inter-membrane space and matrix. The chaperone proteins, and the translocase components, help mitochondrial transport into the subcompartments through their membranes [3]. During the cytoplasmic translation of mitochondrial proteins, they are recognized by chaperone proteins which interfere with the folding of the protein. A positively charged signal sequence, on the mitochondrial pr
Fibrinogen gamma-A chain precursor in CSF: a candidate biomarker for Alzheimer's disease
Joung Lee, Hong Namkoong, Hyun Kim, Sanghee Kim, Dong Hwang, Hae Na, Seon-Ah Ha, Jae-Ryong Kim, Jin Kim
BMC Neurology , 2007, DOI: 10.1186/1471-2377-7-14
Abstract: We applied proteomics approaches to analyze CSF samples derived from 27 patients with AD, 3 subjects with MCI and 30 controls. The AD group was subdivided into three groups by clinical severity according to clinical dementia rating (CDR), a well known clinical scale for dementia.We demonstrated an elevated level of fibrinogen gamma-A chain precursor protein in CSF from patients with mild cognitive impairment and AD compared to the age-matched normal subjects. Moreover, its expression was more prominent in the AD group than in the MCI and correlated with disease severity and progression. In contrast, fibrinogen gamma-A chain precursor protein was detected very low in the age-matched normal group.These findings suggest that the CSF level of fibrinogen gamma-A chain precursor may be a candidate biomarker for AD.Neurodegenerative diseases are characterized by chronic, progressive, irreversible deterioration of neurological function affecting cognition and motor-sensory functions. Diagnosis of neurodegenerative disease largely depends on clinical manifestations; patients usually present to clinicians when their symptoms interfere with activities of daily living (ADL). By the time patients present with these complaints, nerve cells have already been damaged irreversibly and progression of disease may be inevitable. For this reason, there is a need for a molecular-based diagnostic marker in biologic fluids that can identify neurodegenerative disease at an early or preclinical phase; this diagnostic marker could be a disease-modifying compound targeted to drug development [1].Biochemical changes in the brain are well reflected in the CSF which is in direct contact with the brain extracellular space. Biomarkers have been discussed as possible diagnostic tools but have not been frequently used in research on the elderly because of the general paucity of supportive scientific data. However, there is an obvious need for greater diagnostic specificity and sensitivity across many
TCF/β-catenin plays an important role in HCCR-1 oncogene expression
Goang-Won Cho, Mi-Hwa Kim, Seung Kim, Seon-Ah Ha, Hyun Kim, Sanghee Kim, Jin W Kim
BMC Molecular Biology , 2009, DOI: 10.1186/1471-2199-10-42
Abstract: In this study, we showed how the expression of HCCR-1 is modulated. The luciferase activity assay indicated that the HCCR-1 5'-flanking region at positions -166 to +30 plays an important role in HCCR-1 promoter activity. Computational analysis of this region identified two consensus sequences for the T-cell factor (TCF) located at -26 to -4 (Tcf1) and -136 to -114 (Tcf2). Mutation at the Tcf1 site led to a dramatic decrease in promoter activity. Mobility shift assays (EMSA) revealed that nuclear proteins bind to the Tcf1 site, but not to the Tcf2 site. LiCl, Wnt signal activator by GSK-3β inhibition, significantly increased reporter activities in wild-type Tcf1-containing constructs, but were without effect in mutant Tcf1-containing constructs in HEK/293 cells. In addition, endogenous HCCR-1 expression was also increased by treatment with GSK-3β inhibitor, LiCl or AR-A014418 in HEK/293 and K562 cells. Finally, we also observed that the transcription factor, TCF, and its cofactor, β-catenin, bound to the Tcf1 site.These findings suggest that the Tcf1 site on the HCCR-1 promoter is a major element regulating HCCR-1 expression and abnormal stimulation of this site may induce various human cancers.Proto-oncogenes normally help regulate cell growth and differentiation under well-controlled conditions, including mitogenic signal transductions in cells [1,2]. Uncontrolled expression of proto-oncogenes due to mutations or activation of signaling can give rise to a tumor-inducing agent, which is known as an oncogene [2,3]. For more than a decade, there has been a focus on the transcriptional regulation of oncogenes or proto-oncogenes in search of therapeutic clues against cancers which are induced by over-transcription of their oncogenes.Wnt is known as a proto-oncogene and its signaling pathway is a complex network of proteins with roles in embryogenesis [4-6] and cancer [7]. Wnt and its signaling pathway is also involved in normal physiologic processes, including cell pola
Transdifferentiation-inducing HCCR-1 oncogene
Seon-Ah Ha, Hyun K Kim, JinAh Yoo, SangHee Kim, Seung M Shin, Youn S Lee, Soo Y Hur, Yong W Kim, Tae E Kim, Yeun J Chung, Shin S Jeun, Dong W Kim, Yong G Park, Jin Kim, Soon Y Shin, Young H Lee, Jin W Kim
BMC Cell Biology , 2010, DOI: 10.1186/1471-2121-11-49
Abstract: We report here that HCCR-1, previously shown to play an oncogenic role in human cancers, induces epithelial-to-mesenchymal transition (EMT) and mesenchymal-to-epithelial transition (MET) in human and mouse, respectively. The stem cell factor receptor CD117/c-Kit was induced in this transdifferentiated (EMT) sarcoma tissues. This MET occurring in HCCR-1 transfected cells is reminiscent of the transdifferentiation process during nephrogenesis. Indeed, expression of HCCR-1 was observed during the embryonic development of the kidney. This suggests that HCCR-1 might be involved in the transdifferentiation process of cancer stem cell.Therefore, we propose that HCCR-1 may be a regulatory factor that stimulates morphogenesis of epithelia or mesenchyme during neoplastic transformation.The concept that genetic events cooperate to achieve malignant transformation was proposed over a decade ago. Primary rodent cells are efficiently converted into tumorigenic cells by the co-expression of cooperating oncogenes. However, similar experiments with human cells have consistently failed [1]. In 1999, after more than 15 years of trying, researchers have managed to convert normal human cells into tumor cells by delivering telomerase catalytic subunit in combination with two oncogenes [2]. Although malignant transformation of human cells by a single oncogene may not occur or may require specialized factors, we demonstrated that HCCR-1, associated with various types of human cancers, alone induced tumorigenic conversion of mouse cells [3].We have identified a novel oncogene, human cervical cancer oncogene (HCCR), that was classified into 2 types: HCCR-1 (GenBank accession number AF 195651) and HCCR-2 (GenBank accession number AF 315598) [3]. The HCCR-1 and HCCR-2 overexpressed cells were tumorigenic in nude mice and HCCR transgenic mice developed breast cancers and metastasis [3,4]. Also, HCCR-1 was overexpressed in various types of human malignancies and was found to regulate the p53 tum
Early Structural and Functional Defects in Synapses and Myelinated Axons in Stratum Lacunosum Moleculare in Two Preclinical Models for Tauopathy
Hervé Maurin, Seon-Ah Chong, Igor Kraev, Heather Davies, Anna Kremer, Claire Marie Seymour, Benoit Lechat, Tomasz Jaworski, Peter Borghgraef, Herman Devijver, Geert Callewaert, Michael G. Stewart, Fred Van Leuven
PLOS ONE , 2014, DOI: 10.1371/journal.pone.0087605
Abstract: The stratum lacunosum moleculare (SLM) is the connection hub between entorhinal cortex and hippocampus, two brain regions that are most vulnerable in Alzheimer’s disease. We recently identified a specific synaptic deficit of Nectin-3 in transgenic models for tauopathy. Here we defined cognitive impairment and electrophysiological problems in the SLM of Tau.P301L mice, which corroborated the structural defects in synapses and dendritic spines. Reduced diffusion of DiI from the ERC to the hippocampus indicated defective myelinated axonal pathways. Ultrastructurally, myelinated axons in the temporoammonic pathway (TA) that connects ERC to CA1 were damaged in Tau.P301L mice at young age. Unexpectedly, the myelin defects were even more severe in bigenic biGT mice that co-express GSK3β with Tau.P301L in neurons. Combined, our data demonstrate that neuronal expression of protein Tau profoundly affected the functional and structural organization of the entorhinal-hippocampal complex, in particular synapses and myelinated axons in the SLM. White matter pathology deserves further attention in patients suffering from tauopathy and Alzheimer’s disease.
Gremlin-1 Induces BMP-Independent Tumor Cell Proliferation, Migration, and Invasion
Minsoo Kim, Soomin Yoon, Sukmook Lee, Seon Ah Ha, Hyun Kee Kim, Jin Woo Kim, Junho Chung
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0035100
Abstract: Gremlin-1, a bone morphogenetic protein (BMP) antagonist, is overexpressed in various cancerous tissues but its role in carcinogenesis has not been established. Here, we report that gremlin-1 binds various cancer cell lines and this interaction is inhibited by our newly developed gremlin-1 antibody, GRE1. Gremlin-1 binding to cancer cells was unaffected by the presence of BMP-2, BMP-4, and BMP-7. In addition, the binding was independent of vascular endothelial growth factor receptor-2 (VEGFR2) expression on the cell surface. Addition of gremlin-1 to A549 cells induced a fibroblast-like morphology and decreased E-cadherin expression. In a scratch wound healing assay, A549 cells incubated with gremlin-1 or transfected with gremlin-1 showed increased migration, which was inhibited in the presence of the GRE1 antibody. Gremlin-1 transfected A549 cells also exhibited increased invasiveness as well as an increased growth rate. These effects were also inhibited by the addition of the GRE1 antibody. In conclusion, this study demonstrates that gremlin-1 directly interacts with cancer cells in a BMP- and VEGFR2-independent manner and can induce cell migration, invasion, and proliferation.
An Alternative Path for the Preparation of Triacetylcellulose from Unrefined Biomass  [PDF]
Hee Kyung Lim, Ha Young Song, Dal Rye Kim, Jeong Ho Ko, Sun Ah Lee, Kee-In Lee, In Taek Hwang
Advances in Chemical Engineering and Science (ACES) , 2015, DOI: 10.4236/aces.2015.51004
Abstract: An alternative path for the preparation of triacetylcellulose (TAC) from unrefined biomass Palm Empty Fruit Bunch (EFB) has been found with environmental benefits. The method comprises separation and regeneration of cellulose from lignocellulosic biomass dissolved in ionic liquid BMIMCl, and also modification of cellulose to TAC. The triacetylcellulose with a degree of substitution of 2.93 was obtained by the reaction of acetic anhydride at 55C with drastically reducing number of steps currently required to produce this derivative from raw materials itself. TAC was characterized using NMR analysis. The triacetate cellulose is typically used for the creation of fibers and film base.
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