• Title/Summary/Keyword: Fibrosarcoma

Search Result 156, Processing Time 0.031 seconds

Suppression of Human Fibrosarcoma Cell Metastasis by Phyllanthus emblica Extract in Vitro

  • Yahayo, Waraporn;Supabphol, Athikom;Supabphol, Roongtawan
    • Asian Pacific Journal of Cancer Prevention
    • /
    • v.14 no.11
    • /
    • pp.6863-6867
    • /
    • 2013
  • Phyllanthus emblica (PE) is known to exhibit various pharmacological properties. This study aimed to evaluate the antimetastatic potential of a PE aqueous extract. Cytotoxicity to human fibrosarcoma cells, HT1080, was determined by viability assay using the 3-(4,5-dimethylthiazol,2-yl)-2,5-diphenyltetrazolium bromide (MTT) reagent. Cell migration and invasion were investigated using chemotaxis chambers containing membranes precoated with collagen IV and Matrigel, respectively. Cell attachment onto normal surfaces of cell culture plates was tested to determine the cell-adhesion capability. The molecular mechanism of antimetastatic activity was assessed by measuring the gene expression of matrix metalloproteinases, MMP2, and MMP9, using reverse transcription-polymerase chain reaction (RT-PCR) assay. The mRNA levels of both genes were significantly down-regulated after pretreatment with PE extract for 5 days. Our findings show the antimetastatic function of PE extract in reducing cell proliferation, migration, invasion, and adhesion in both dose- and time-dependent manners, especially growth arrest with low $IC_{50}$ value. A decrease in the expression of both MMP2 and MMP9 seems to be the cellular mechanism for antimetastasis in this case. There is a high potential to use PE extracts clinically as an optional adjuvant therapeutic drug for therapeutic intervention strategies in cancer therapy or chemoprevention.

Inhibition of the expression on MMP-2, 9 and morphological changes via human fibrosarcoma cell line by 6,6'-bieckol from marine alga Ecklonia cava

  • Zhang, Chen;Li, Yong;Shi, Xiujuan;Kim, Se-Kwon
    • BMB Reports
    • /
    • v.43 no.1
    • /
    • pp.62-68
    • /
    • 2010
  • Matrix Metalloproteinases (MMPs) are a family of zinc-endopeptidases which can degrade extracellular matrix (ECM) components and play important roles in a variety of biological and pathological processes. 6,6'-bieckol isolated and characterized from an edible marine brown alga Ecklonia cava (EC), according to the comprehensive spectral analysis of MS and NMR data. Here the influence of 6,6'-bieckol on expressions of MMPs was examined by zymography and western blot analysis via human fibrosarcoma cell line (HT1080). It is shown that 6,6'-bieckol significantly down regulated the expressions of MMP-2 and -9 in dose-dependent manner. The influence of 6,6'-bieckol on the cell viability and cell behavior of HT1080 cells were also investigated, our dates shown that it suppressed the migration and 3D culture in HT1080 cells. Meanwhile, we explored several signal pathways which may contribute to this process, and found the suppressing of MMPs expressions in HT1080 cells might be due to the suppression of NF-${\kappa}B$ signal pathway.

Seahorse-derived peptide suppresses invasive migration of HT1080 fibrosarcoma cells by competing with intracellular α-enolase for plasminogen binding and inhibiting uPA-mediated activation of plasminogen

  • Kim, Yong-Tae;Kim, Se-Kwon;Jeon, You-Jin;Park, Sun Joo
    • BMB Reports
    • /
    • v.47 no.12
    • /
    • pp.691-696
    • /
    • 2014
  • ${\alpha}$-Enolase is a glycolytic enzyme and a surface receptor for plasminogen. ${\alpha}$-Enolase-bound plasminogen promotes tumor cell invasion and cancer metastasis by activating plasmin and consequently degrading the extracellular matrix degradation. Therefore, ${\alpha}$-enolase and plasminogen are novel targets for cancer therapy. We found that the amino acid sequence of a peptide purified from enzymatic hydrolysates of seahorse has striking similarities to that of ${\alpha}$-enolase. In this study, we report that this peptide competes with cellular ${\alpha}$-enolase for plasminogen binding and suppresses urokinase plasminogen activator (uPA)-mediated activation of plasminogen, which results in decreased invasive migration of HT1080 fibrosarcoma cells. In addition, the peptide treatment decreased the expression levels of uPA compared to that of untreated controls. These results provide new insight into the mechanism by which the seahorse-derived peptide suppresses invasive properties of human cancer cells. Our findings suggest that this peptide could emerge as a potential therapeutic agent for cancer.

Cytotoxic Effect of Chalcone Derivatives in MCF-7 Human Breast Cancer and HT-1080 Human Fibrosarcoma Cells (Chalcone 유도체들의 사람 유방암세포주 및 사람 섬유육종 세포에 대한 세포독성효과)

  • Kang, You-Ra;Park, Min-A;Cho, Mi-Yeon;Lee, Kyung-Hee;Kim, Jung-Ae
    • YAKHAK HOEJI
    • /
    • v.54 no.1
    • /
    • pp.27-31
    • /
    • 2010
  • Xanthohumol, a prenylated chalcone of the Hop plant (Humulus lupulus L.), has been reported to suppress tumor growth. 4-hydroxychalcone and isobavachalcone are chalcone derivatives and they have similar structure with xanthohumol. In the present study, we investigated the cytotoxic activities of chalcone and its derivatives, 4-hydroxychalcone, xanthohumol, and isobavachalcone, in MCF-7 and adriamycin resistant MCF-7 (MCF-7/ADR) breast cancer cells and HT-1080 fibrosarcoma cells. In a cell viability assay using 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide (MTT) reagent, chalcone and 4-hydroxychalcone decreased cell viability in HT-1080 cells, but not in MCF-7 and MCF-7/ADR cells. Isobavachalcone showed similar cytotoxicity in HT-1080 cells, and only limited cytotoxicity in MCF-7 and MCF-7/ADR cells at very high concentration (50 ${\mu}M$). In contrast, xanthohumol showed concentration-dependent cytotoxicity in MCF-7, MCF-7/ADR, and HT-1080 cancer cells. Taken together, the structure-activity relationship of chalcone and its derivatives indicate that chalcones may be valuable cytotoxic compounds against selective cancer types.

Galangin and Kaempferol Suppress Phorbol-12-Myristate-13-Acetate-Induced Matrix Metalloproteinase-9 Expression in Human Fibrosarcoma HT-1080 Cells

  • Choi, Yu Jung;Lee, Young Hun;Lee, Seung-Taek
    • Molecules and Cells
    • /
    • v.38 no.2
    • /
    • pp.151-155
    • /
    • 2015
  • Matrix metalloproteinase (MMP)-9 degrades type IV collagen in the basement membrane and plays crucial roles in several pathological implications, including tumorigenesis and inflammation. In this study, we analyzed the effect of flavonols on MMP-9 expression in phorbol-12-myristate-13-acetate (PMA)-induced human fibrosarcoma HT-1080 cells. Galangin and kaempferol efficiently decreased MMP-9 secretion, whereas fisetin only weakly decreased its secretion. Galangin and kaempferol did not affect cell viability at concentrations up to $30{\mu}M$. Luciferase reporter assays showed that galangin and kaempferol decrease transcription of MMP-9 mRNA. Moreover, galangin and kaempferol strongly reduce $I{\kappa}B{\alpha}$ phosphorylation and significantly decrease JNK phosphorylation. These results indicate that galangin and kaempferol suppress PMA-induced MMP-9 expression by blocking activation of NF-${\kappa}B$ and AP-1. Therefore, these flavonols could be used as chemopreventive agents to lower the risk of diseases involving MMP-9.

Primary Pericardial Fibrosarcoma Presenting as Cardiac Tamponade - A case report - (심낭압전으로 발견된 원발성 심낭 섬유육종 - 1예 보고 -)

  • Lim, Ju-Yong;Sung, Kyu-Wan;Kang, Gil-Hyun;Yoo, Dong-Gon;Kim, Chong-Wook;Park, Chong-Bin
    • Journal of Chest Surgery
    • /
    • v.40 no.8
    • /
    • pp.574-577
    • /
    • 2007
  • Primary malignant neoplasm of the pericardium is very rare, Neoplastic involvement of the pericardium may result in rapidly developing hemorrhagic effusion. A 30-year-old male who occasionally suffered from chest tightness was referred to our hospital under the diagnosis of unstable angina. He presented with acute chest pain and severe dyspnea that had developed one day previously. The diagnostic investigations such as echocardiography, chest CT and magnetic resonance image suggested cardiac tamponade that was caused by rupture of the pericardial teratoma. An operation to remove the tumor and effusion was performed. The pericardial mass was completely excised, and the result of the frozen biopsy favored malignancy. The final pathologic report was malignant fibrosarcoma of the pericardium and no malignant cells were found on the cytology of the pericardial effusion. The patient had a smooth postoperative course and was referred to another hospital for additional radiation therapy. We report here on this case of cardiac tamponade that was caused by primary pericardial fibrosarcoma, and this required urgent diagnosis and surgical management.

Effects of Seaweeds on Matrix Metalloproteinases Derived from Normal Human Dermal Fibroblasts and Human Fibrosarcoma Cells (사람피부섬유아세포 및 섬유아육종세포로부터 유래된 기질금속단백질효소에 대한 해조류의 효능)

  • Park, In-Hwan;Lee, Sang-Hoon;Kim, Se-Kwon;Ngo, Dai-Nghiep;Jeon, You-Jin;Kim, Moon-Moo
    • Journal of Life Science
    • /
    • v.21 no.11
    • /
    • pp.1501-1510
    • /
    • 2011
  • In recent years novel potential pharmocological candidates have been looked for in animal, seaweed, sponge, fungi and marine bacteria resources. In this study, matrix metalloproteinases (MMPs) that play an important role in metastasis, arthritis, chronic inflammation and wrinkle formation were used as target enzymes to screen therapeutic agents. The inhibitory effects of several marine algae including green algae (5 species), red algae (18 species) and brown algae (4 species) methanolic extracts on MMPs were investigated in human dermal fibroblasts and human fibrosarcoma cell line (HT1080 cells) using gelatin zymography. In human dermal fibroblasts, the inhibition of MMP-2 was observed in Laurencia okamurae, Polysiphonia japonica, Grateloupia lanceolate and Sinkoraena lancifolia of red algae. In contrast, MMP-2 activation was enhanced in Enteromorpha compressa and E. linza of green algae, and Peltaronia bighamiae and Sargassum thunbergii of brown algae. In human fibrosarcoma cells, MMP-9 activation was decreased in the presence of S. thunbergii of brown algae, Polysiphonia japonica in red algae and E. compressa and E. linza of green algae. The interesting finding is that E. compressa and E. linza of green algae, and S. thunbergii of brown algae exhibited a positive effect on MMP-2 in normal cells, but a negative effect on MMP-9 in cancer cell lines. These results suggest that E. compressa and E. linza of green algae, and S. thunbergii of brown algae contain potential therapeutic ingredients for cancer treatment.

Central odontogenic fibroma: a case report

  • Nah, Kyung-Soo
    • Imaging Science in Dentistry
    • /
    • v.41 no.2
    • /
    • pp.85-88
    • /
    • 2011
  • Central odontogenic fibroma is a rare odontogenic neoplasm that originates from odontogenic ectomesenchyme. Here, a case of central odontogenic fibroma in a 17-year-old male is reported. Since the present case showed a multilocular radiolucency with partially ill-defined border between the right mandibular condyle and the distal root of the right mandibular third molar, differential diagnosis involved a wide range of pathosis from benign lesions like ameoloblastic fibroma and odontogenic myxoma to more aggressive lesions such as desmoplastic fibroma, juvenile aggressive fibromatosis, or fibrosarcoma.

Inhibitory effects of dihydrohinokiflavone on tumor cell growth and invasion

  • Yun, Chang-Hyun;Yoon, Sang-Oh;Chung, An-Sik
    • Proceedings of the Korean Society of Toxicology Conference
    • /
    • 2003.05a
    • /
    • pp.41-42
    • /
    • 2003
  • Matrix metalloproteinases (MMPs) inhibitors were screened from Metasequoia glyptostroboides and one potent inhibitor, dihydrohinokiflavone (DHHF), a biflavonoid, was selected. DHHF inhibited proliferation of HT1080, human fibrosarcoma cells in a dose-dependent manner. Noncytotoxic levels of DHHF dramatically decreased MMP-9 and MMP-2 production in unistimulated cells, but did not change the level of tissue inhibited of metalloproteinase (TIMP)-1, an inhibitor of MMP-9.(omitted)

  • PDF