scholarly journals Constituents of Aquilaria sinensis Leaves Upregulate the Expression of Matrix Metalloproteases 2 and 9

Molecules ◽  
2021 ◽  
Vol 26 (9) ◽  
pp. 2537
Author(s):  
Sui-Wen Hsiao ◽  
Yu-Chin Wu ◽  
Hui-Ching Mei ◽  
Yu-Hsin Chen ◽  
George Hsiao ◽  
...  
Keyword(s):  
Active Component ◽  
Matrix Metalloproteases ◽  
Matrix Metalloprotease ◽  
Regulatory Activity ◽  
Pheophorbide A ◽  
Aquilaria Sinensis ◽  
Significant Stimulation ◽  
Fibrosarcoma Cells ◽  
Potential Applications ◽  
Human Fibrosarcoma Cells

In this novel study, we isolated 28 compounds from the leaves of Aquilaria sinensis (Lour.) Gilg based on a bioassay-guided procedure and also discovered the possible matrix metalloprotease 2 (MMP-2) and 9 (MMP-9) modulatory effect of pheophorbide A (PA). To evaluate the regulatory activity on MMP-2 and MMP-9, the HT-1080 human fibrosarcoma cells were treated with various concentrations of extracted materials and isolated compounds. PA was extracted by methanol from the leaves of A. sinensis and separated from the fraction of the partitioned ethyl acetate layer. PA is believed to be an active component for MMP expression since it exhibited significant stimulation on MMP-2 and proMMP-9 activity. When treating with 50 μM of PA, the expression of MMP-2 and MMP-9 were increased 1.9-fold and 2.3-fold, respectively. PA also exhibited no cytotoxicity against HT-1080 cells when the cell viability was monitored. Furthermore, no significant MMP activity was observed when five PA analogues were evaluated. This study is the first to demonstrate that C-17 of PA is the deciding factor in determining the bioactivity of the compound. The MMP-2 and proMMP-9 modulatory activity of PA indicate its potential applications for reducing scar formation and comparative medical purposes.

scholarly journals 4-Methylumbelliferone administration enhances radiosensitivity of human fibrosarcoma by intercellular communication

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ryo Saga ◽  
Yusuke Matsuya ◽  
Rei Takahashi ◽  
Kazuki Hasegawa ◽  
Hiroyuki Date ◽  
...  
Keyword(s):  
Intercellular Communication ◽  
Dose Range ◽  
Synthesis Inhibitor ◽  
X Ray ◽  
Tumour Control ◽  
Synergetic Effects ◽  
Fibrosarcoma Cells ◽  
Oxidative Stress Level ◽  
Human Fibrosarcoma Cells

AbstractHyaluronan synthesis inhibitor 4-methylumbelliferone (4-MU) is a candidate of radiosensitizers which enables both anti-tumour and anti-metastasis effects in X-ray therapy. The curative effects under such 4-MU administration have been investigated in vitro; however, the radiosensitizing mechanisms remain unclear. Here, we investigated the radiosensitizing effects under 4-MU treatment from cell experiments and model estimations. We generated experimental surviving fractions of human fibrosarcoma cells (HT1080) after 4-MU treatment combined with X-ray irradiation. Meanwhilst, we also modelled the pharmacological effects of 4-MU treatment and theoretically analyzed the synergetic effects between 4-MU treatment and X-ray irradiation. The results show that the enhancement of cell killing by 4-MU treatment is the greatest in the intermediate dose range of around 4 Gy, which can be reproduced by considering intercellular communication (so called non-targeted effects) through the model analysis. As supposed to be the involvement of intercellular communication in radiosensitization, the oxidative stress level associated with reactive oxygen species (ROS), which leads to DNA damage induction, is significantly higher by the combination of 4-MU treatment and irradiation than only by X-ray irradiation, and the radiosensitization by 4-MU can be suppressed by the ROS inhibitors. These findings suggest that the synergetic effects between 4-MU treatment and irradiation are predominantly attributed to intercellular communication and provide more efficient tumour control than conventional X-ray therapy.

scholarly journals TNP-470 Suppresses the Tumorigenicity of HT1080 Fibrosarcoma Tumor Through the Inhibition of VEGF Secretion From the Tumor Cells

Sarcoma ◽  
2001 ◽  
Vol 5 (4) ◽  
pp. 197-202 ◽  
Author(s):  
Mitsunori Kaya ◽  
Takuro Wada ◽  
Satoshi Nagoya ◽  
Satoshi Kawaguchi ◽  
Toshihiko Yamashita ◽  
...  
Keyword(s):  
Conditioned Medium ◽  
Direct Action ◽  
Angiogenesis Inhibitor ◽  
Angiogenesis Inhibitors ◽  
Fibrosarcoma Cells ◽  
Ht1080 Cells ◽  
Human Fibrosarcoma Cells ◽  
And Migration

Angiogenesis inhibitors are a novel class of promising therapeutic agents for treating cancer. TNP-470, a systemic analogue of fumagillin, is an angiogenesis inhibitor capable of suppressing the tumorigenicity in several animal models even though the mechanisms of action have not been completely clarified. In the current study, we investigated the effects of TNP-470 on human fibrosarcoma cellsin vivoandin vitro. The administration of TNP-470 could suppress the tumorigenicity of HT1080 fibrosarcoma tumor. The conditioned medium from HT1080 fibrosarcoma cells treated with TNP-470 inhibited the proliferation and migration of human endothelial cell line, HUVEC and ECV304. The concentration of VEGF in the conditioned medium from HT1080 cells treated with TNP-470 was lower than that of the cells without TNP-470 treatment, indicating that TNP-470 downregulates the secretion of VEGF from HT1080 cells. These findings strongly suggest that the direct action of TNP-470 on sarcoma cells inhibits angiogenesis through the downregulation of VEGF secretion and this angiogenesis suppression resulted in the inhibition of tumorigenicity of HT1080 fibrosarcoma tumo.

scholarly journals Immunological analysis of a chromosomal antigen specific to human granulocytes

1982 ◽  
Vol 203 (1) ◽  
pp. 235-238 ◽  
Author(s):  
K C Ramage ◽  
J H J Dunn ◽  
A M Campbell
Keyword(s):  
Cell Lines ◽  
Hela Cells ◽  
Human Lymphocytes ◽  
Protein Antigen ◽  
Chromosomal Protein ◽  
Immunological Analysis ◽  
Fibrosarcoma Cells ◽  
Human Granulocytes ◽  
Human Fibrosarcoma Cells

A chromosomal protein antigen specific for human granulocytes is described. The antigen is present in large amounts in granulocytes and in granulocytic leukaemia. It is absent from HeLa cells, human fibrosarcoma cells and human lymphocytes. It is, however, present in small amounts in other human haemopoietic cell lines. The antigen binds tightly to DNA and requires the presence of DNA to react with the antibody.

scholarly journals Evaluation of MMP Inhibitors Isolated from Ligustrum japonicum Fructus

Molecules ◽  
2019 ◽  
Vol 24 (3) ◽  
pp. 604
Author(s):  
Hojun Kim ◽  
Fatih Karadeniz ◽  
Chang-Suk Kong ◽  
Youngwan Seo
Keyword(s):  
Culture Medium ◽  
Mapk Pathway ◽  
Gelatin Zymography ◽  
Inhibitory Effect ◽  
Mmp Inhibitors ◽  
Protein Levels ◽  
Lead Compounds ◽  
Ligustrum Japonicum ◽  
Fibrosarcoma Cells ◽  
Human Fibrosarcoma Cells

The current study investigated the ability of two secoiridoids, GL-3 (1) and oleonuezhenide (2), isolated from the fruits of Ligustrum japonicum to inhibit MMP-2 and -9 activity in phorbol 12-myristate 13-acetate (PMA)-induced HT-1080 human fibrosarcoma cells. Both compounds 1 and 2 were able to exert lowered gelatin digestion activity for MMP-2 and -9 tested by gelatin zymography via suppressing the release of MMPs to culture medium according to ELISA results. Treatment with compounds was also able to suppress the expression of both mRNA and protein levels of MMP-2 and -9. Action mechanism behind the MMP inhibitory effect of the compounds was suggested to be via MAPK pathway indicated by decreased levels of phosphorylated p38, ERK and JNK proteins evaluated employing immunoblotting. Compound 1 was shown to be slightly more active to inhibit MMP-2 and -9, however, compound 2 showed more regular dose-dependency during inhibition. In conclusion, this study suggested that GL-3 and oleonuezhenide were notable natural origin potent MMP inhibitors and could serve as lead compounds for development of anti-invasive MMP inhibitors against tumor metastasis.

scholarly journals Induction of fibronectin matrix assembly in human fibrosarcoma cells by dexamethasone.

1987 ◽  
Vol 104 (3) ◽  
pp. 601-610 ◽  
Author(s):  
P J McKeown-Longo ◽  
C A Etzler
Keyword(s):  
Extracellular Matrix ◽  
Surface Protein ◽  
Order Rate Constant ◽  
Binding Activity ◽  
Matrix Assembly ◽  
Cultured Fibroblasts ◽  
Fibrosarcoma Cells ◽  
The Matrix ◽  
Fibronectin Binding ◽  
Human Fibrosarcoma Cells

Previous studies have suggested that the assembly of fibronectin into the extracellular matrix of cultured fibroblasts is mediated by specific matrix assembly receptors that recognize a binding site in the amino terminus of the fibronectin molecule (McKeown-Longo, P.J., and D.F. Mosher, 1985, J. Cell Biol., 100:364-374). In the presence of dexamethasone, human fibrosarcoma cells (HT-1080) acquired the ability to specifically bind exogenous plasma fibronectin and incorporate it into a detergent-insoluble extracellular matrix. Dexamethasone-induced fibronectin binding to HT-1080 cells was time dependent, dose dependent, and inhibited by cycloheximide. Saturation binding curves indicated that dexamethasone induced the appearance of 7.7 X 10(4) matrix assembly receptors per cell. The induced receptors exhibited a dissociation constant (KD) for soluble fibronectin of 5.0 X 10(-8) M. In parallel experiments, normal fibroblasts exhibited 4.1 X 10(5) receptors (KD = 5.3 X 10(-8) M) per cell. In the presence of cycloheximide, the induced fibronectin-binding activity on HT-1080 cells returned to uninduced levels within 12 h. In contrast, fibronectin-binding activity on normal fibroblasts was stable in the presence of cycloheximide for up to 54 h. The first-order rate constant (Kt = 2.07 X 10(-4) min-1) for the transfer of receptor-bound fibronectin to extracellular matrix was four- to fivefold less than that for normal fibroblasts (Kt = 1.32 X 10(-3) min-1). Lactoperoxidase-catalyzed iodination of HT-1080 monolayers indicated that a 48,000-mol-wt cell surface protein was enhanced with dexamethasone. The results from these experiments suggest that dexamethasone induces functional matrix assembly receptors on the surface of HT-1080 cells; however, the rate of incorporation of fibronectin into the matrix is much slower than that of normal fibroblasts.

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