Pin1 acts as a modulator of cell proliferation through alteration in NF-κB but not β-catenin/TCF4 signalling in a subset of endometrial carcinoma cells

2010 ◽  
Vol 222 (4) ◽  
pp. 410-420 ◽  
Author(s):  
Makoto Saegusa ◽  
Miki Hashimura ◽  
Takeshi Kuwata
Keyword(s):  
Cell Proliferation ◽  
Endometrial Carcinoma ◽  
Carcinoma Cells

scholarly journals P-LAP/IRAP-induced cell proliferation and glucose uptake in endometrial carcinoma cells via insulin receptor signaling

BMC Cancer ◽  
2007 ◽  
Vol 7 (1) ◽  
Author(s):  
Kiyosumi Shibata ◽  
Hiroaki Kajiyama ◽  
Kazuhiko Ino ◽  
Akihiro Nawa ◽  
Seiji Nomura ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Insulin Receptor ◽  
Endometrial Carcinoma ◽  
Glucose Uptake ◽  
Carcinoma Cells ◽  
Receptor Signaling ◽  
Insulin Receptor Signaling

miR-486-3p Controls the Apoptosis of Endometrial Carcinoma Cells

2022 ◽  
Vol 12 (5) ◽  
pp. 1002-1007
Author(s):  
Donghua Wang ◽  
Xiaoli Liu ◽  
Lirong Cao ◽  
Shixiong Gong ◽  
Yi He ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cell Migration ◽  
Endometrial Carcinoma ◽  
Real Time ◽  
Spectrophotometric Method ◽  
Real Time Pcr ◽  
Carcinoma Cells ◽  
Migration And Invasion ◽  
Invasive Capacity ◽  
Ec Cells

Our study aimed to discuss the mechanism of miR-486-3p in controlling the apoptosis of endometrial carcinoma (EC) cells. EC cells were divided into NC group, miR-486-3p mimic and miR-486-3p inhibitor group followed by analysis of miR-486-3p level by Real-time PCR, cell proliferation by spectrophotometric method, apoptosis by FCM, cell migration and invasion by Transwell analysis. EC cells showed reduced miR-486-3p level. The EC malignant biological behaviors could be prompted through retraining miR-486-3p level with increased EC cell invasive capacity. DDR1 was a target of miR-486-3p. The variation of tumor activity could be regulated through controlling DDR1 expression. In conclusion, the apoptotic and invasive characteristic of EC cells are restrained after overexpression of miR-486-3p in EC cells through targeting DDR1, indicating that miR-486-3p could be considered to be one kind of brand-new target for the treatment of EC.

scholarly journals 1α,25(OH)2D3 Induces Actin Depolymerization in Endometrial Carcinoma Cells by Targeting RAC1 and PAK1

2016 ◽  
Vol 40 (6) ◽  
pp. 1455-1464 ◽  
Author(s):  
Ni Zeng ◽  
Madhuri S. Salker ◽  
Shaqiu Zhang ◽  
Yogesh Singh ◽  
Bing Shi ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Actin Cytoskeleton ◽  
Endometrial Carcinoma ◽  
Actin Polymerization ◽  
Carcinoma Cells ◽  
Filamentous Actin ◽  
Transcript Levels ◽  
Actin Depolymerization ◽  
Protein Levels ◽  
Ishikawa Cells

Background: Cell proliferation and motility require actin reorganization, which is under control of various signalling pathways including ras-related C3 botulinum toxin substrate 1 (RAC1), p21 protein-activated kinase 1 (PAK1) and actin related protein 2 (ARP2). Tumour cell proliferation is modified by 1α,25-Dihydroxy-Vitamin D3 (1α,25(OH)2D3), a steroid hormone predominantly known for its role in calcium and phosphorus metabolism. The present study explored whether 1α,25(OH)2D3 modifies actin cytoskeleton in Ishikawa cells, a well differentiated endometrial carcinoma cell line. Methods: To this end, actin cytoskeleton was visualized by confocal microscopy. Globular over filamentous actin ratio was determined utilizing Western blotting and flow cytometry, transcript levels by qRT-PCR and protein abundance by immunoblotting. Results: A 24 hour treatment with 1α,25(OH)2D3 (100 nM) significantly decreased RAC1 and PAK1 transcript levels and activity, decreased ARP2 protein levels and depolymerized actin. The effect of 1α,25(OH)2D3 on actin polymerization was mimicked by pharmacological inhibition of RAC1 and PAK1. Conclusions: 1α,25(OH)2D3 leads to disruption of RAC1 and PAK1 activity with subsequent actin depolymerization of endometrial carcinoma cells.

scholarly journals Autocrine stimulation of IGF1 in estrogen-induced growth of endometrial carcinoma cells: involvement of the mitogen-activated protein kinase pathway followed by up-regulation of cyclin D1 and cyclin E

2009 ◽  
Vol 16 (1) ◽  
pp. 113-122 ◽  
Author(s):  
Hiroyasu Kashima ◽  
Tanri Shiozawa ◽  
Tsutomu Miyamoto ◽  
Akihisa Suzuki ◽  
Junko Uchikawa ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Protein Kinase ◽  
Cyclin D1 ◽  
Endometrial Carcinoma ◽  
Carcinoma Cells ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Ishikawa Cells ◽  
Autocrine Stimulation ◽  
Stimulation Of

To examine estrogen-induced growth mechanisms of endometrial carcinoma, we investigated the estrogen-induced activation of the mitogen-activated protein kinase (MAPK) pathway and cell cycle regulators. Estradiol (E2) treatment at concentrations of 10−8 M and 10−6 M to estrogen receptor (ER)-positive endometrial carcinoma Ishikawa cells for 24 h resulted in increased cell proliferation by 20% and 28% respectively. The E2-induced proliferation was associated with the activation of extracellular signal-regulated kinase (MAPK)3/1 and up-regulation of cyclin D1 and E, which were suppressed by the addition of an MAP2K inhibitor (U0126) or an ER antagonist (ICI 182 780). Then, our screening for estrogen-inducible growth factors identified that IGF1 was up-regulated remarkably by E2. Immunoprecipitation using conditioned medium of Ishikawa cells after E2 treatment confirmed the E2-induced secretion of IGF1 protein. Treatment with recombinant IGF1 stimulated cell proliferation in a dose-dependent fashion, in association with MAPK3/1 phosphorylation and up-regulation of cyclin D1 and E. These IGF1-induced responses were suppressed by treatment with MAP2K inhibitor or anti-IGF1 receptor antibody. Immunohistochemical staining confirmed the expression of activated MAPK3/1 in normal proliferative phase endometria and endometrial carcinomas, indicating the involvement of this pathway in actively proliferating endometrial tissues in vivo. These findings suggest that E2-induced proliferation of endometrial carcinoma cells is mediated by the MAPK3/1 pathway via autocrine stimulation of IGF1.

scholarly journals lncRNA-ZFAS1 promotes the progression of endometrial carcinoma by targeting miR-34b to regulate VEGFA expression

Open Medicine ◽  
2021 ◽  
Vol 16 (1) ◽  
pp. 1472-1481
Author(s):  
Hongli Zhu ◽  
Qihui Cheng ◽  
Hong Cai
Keyword(s):  
Cell Proliferation ◽  
Endometrial Carcinoma ◽  
Noncoding Rna ◽  
Carcinoma Cell ◽  
Underlying Mechanism ◽  
Carcinoma Cells ◽  
Factor X ◽  
Endometrial Carcinoma Cell ◽  
Proliferation And Metastasis ◽  
Cell Proliferation And Metastasis

Abstract Zinc finger nuclear transcription factor, X-box binding 1-type containing 1 antisense RNA 1 (ZFAS1) functions as an oncogenic long noncoding RNA (lncRNA) to promote proliferation and metastasis of endometrial carcinoma cell; however, the underlying mechanism has not been fully understood. First, RT-qPCR analysis of endometrial carcinoma tissues and cells showed that ZFAS1 was enriched in endometrial carcinoma tissues and cells. miR-34b was reduced in endometrial carcinoma and suggested negative correlation with ZFAS1 in endometrial carcinoma. Second, functional assays demonstrated that siRNA-mediated silence of ZFAS1 suppressed endometrial carcinoma cell proliferation and metastasis. Third, ZFAS1 bind to miR-34b and negatively regulate expression of miR-34b in endometrial carcinoma cells. miR-34b also bind to and negatively regulate expression of vascular endothelial growth factor A (VEGFA) in endometrial carcinoma cells. Lastly, knockdown of miR-34b counteracted with the suppressive effects of ZFAS1 silence on endometrial carcinoma cell proliferation and metastasis. In conclusion, lncRNA ZFAS1 functioned as an oncogene to promote endometrial carcinoma cell proliferation and metastasis through miR-34b/VEGFA axis.

Immunocytochemical localization of β1-4 galactosyltransferase in endometrial carcinoma cells

1990 ◽  
Vol 48 (3) ◽  
pp. 944-945
Author(s):  
Ichiro Yamamoto ◽  
Toshiaki Tachibana ◽  
Hiroko Maruyama ◽  
Noriyuki Komatsu ◽  
Hiroyuki Kuramoto ◽  
...  
Keyword(s):  
Endometrial Carcinoma ◽  
Cell Lines ◽  
Endometrial Adenocarcinoma ◽  
Protein A ◽  
Rabbit Antiserum ◽  
Carcinoma Cells ◽  
Affinity Column ◽  
Antibody Technique ◽  
Galactosyl Transferase ◽  
C Terminus

We have paid attention to the alteration of glycosyltransferase in carcinoma cells, because it might be related to the malignancy of the cells. In this connection, localization of β1-4 galactosyl transferase (β1-4 Gal T) in human endometrial carcinoma cells was examined immunocytochemically using two kinds of cell lines, each of which showed different degree of differentiation.An antibody was purified from the rabbit antiserum against the synthetic peptide, IFNRLVFRGMSC (W89) of human β1-4 Gal T coupled with KLH (keyhole limpet hemocyanine) by protein A column and peptide-affinity column chromatography. The anti-W89 serum reacts to the C-terminus of human β 1-4 Gal T and to both membrane-bound and soluble forms of the enzyme. Cell line of well differentiated endometrial adenocarcinoma (I) and that of poorly differentiated endometrial adenocarcinoma (50B) were cultivated respectively in MEM medium containing 15% FCS and 2 mM glutamine for 4 d at 37°C under 5% CO2. The cells were fixed in a mixture of 4% paraformaldehyde and 0.1% glutaraldehyde in 0.1 M Soerensen’s phosphate buffer (pH 7.4) at 4°C for 30 min, washed with PBS, then freezed and thawed. The indirect method of the peroxidase- labeled antibody technique was used for immunocytochemistry of both LM and TEM on the cell lines. The cells were dehydrated in ethanol and embedded in TAAB 812. Ultrathin sections were observed under a TEM, JEM-100S.

scholarly journals Overexpression of Indoleamine 2,3-Dioxygenase in Human Endometrial Carcinoma Cells Induces Rapid Tumor Growth in a Mouse Xenograft Model

2008 ◽  
Vol 14 (22) ◽  
pp. 7251-7259 ◽  
Author(s):  
Norio Yoshida ◽  
Kazuhiko Ino ◽  
Yoshiyuki Ishida ◽  
Hiroaki Kajiyama ◽  
Eiko Yamamoto ◽  
...  
Keyword(s):  
Tumor Growth ◽  
Endometrial Carcinoma ◽  
Xenograft Model ◽  
Carcinoma Cells ◽  
Mouse Xenograft ◽  
Indoleamine 2,3 Dioxygenase ◽  
Mouse Xenograft Model
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