endometrial neoplasms/phosphatase

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Gefitinib enhances sensitivity of endometrial cancer cells to progestin therapy via dual-specificity phosphatase 1.

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In this study, we investigated if Gefitinib, an epidermal growth factor receptor (EGFR) inhibitor, augments endometrial cancer (EC) therapy with medroxyprogesterone acetate (MPA). Combined treatment with Gefitinib plus MPA decreased the proliferation and invasiveness of the Ishikawa and RL952 EC

Membrane-associated serine/threonine protein phosphatase in endometrial cancer.

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OBJECTIVE Reversible serine/threonine protein phosphorylation catalyzed by kinases and phosphatases plays a crucial role in cellular growth and differentiation. We attempted to determine the subcellular location of serine/threonine phosphatase (protein phosphatase type 2A [PP2A]) in endometrial

Infrequent methylation of the DUSP6 phosphatase in endometrial cancer.

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OBJECTIVE Dual-specificity phosphatase six (DUSP6, MKP3, or PYST1) dephosphorylates phosphotyrosine and phosphothreonine residues on ERK-2 (MAPK1) to inactivate the ERK-2 kinase. DUSP6 is a critical regulator of the ERK signaling cascade and has been implicated as a tumor suppressor. DNA methylation

Relationship between polycomb-group protein BMI-1 and phosphatases regulating AKT phosphorylation level in endometrial cancer.

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The PI3K/AKT pathway is frequently activated in endometrial carcinoma. BMI-1 (B-lymphoma Mo-MLV insertion region 1) protein affects expression of PTEN (phosphatase and tensin homolog) in some cancers, but its significance for endometrial tumorigenesis is not known. The objective of this study was to

Effects of oestradiol and progesterone on the alkaline phosphatase activity of a human endometrial cancer cell-line.

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The alkaline phosphatase (ALPase) activity of a human endometrial cancer cell-line, established and designated as HEC-50-B in our laboratory, was investigated biochemically and histochemically in relation to its cell growth pattern and to the effects of the sex steroid hormones, oestradiol and

Precision Therapy for Aggressive Endometrial Cancer by Reactivation of Protein Phosphatase 2A.

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Critically important to reducing uterine cancer mortality is the development of more effective therapy for aggressive endometrial cancers, including uterine serous cancer and uterine carcinosarcoma, which together account for over half of deaths due to endometrial cancer. About one-third of these

Dual specificity phosphatase 6 plays a critical role in the maintenance of a cancer stem-like cell phenotype in human endometrial cancer.

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The prognosis of patients with high-grade or advanced-stage endometrial cancer remains poor. As cancer stem-like cells (CSCs) are thought to be associated with endometrial cancers, it is essential to investigate the molecular mechanisms that regulate endometrial CSCs. Dual specificity phosphatase 6

PME-1 modulates protein phosphatase 2A activity to promote the malignant phenotype of endometrial cancer cells.

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Protein phosphatase 2A (PP2A) negatively regulates tumorigenic signaling pathways, in part, by supporting the function of tumor suppressors like p53. The PP2A methylesterase PME-1 limits the activity of PP2A by demethylating its catalytic subunit. Here, we report the finding that PME-1

Effects of steroid hormones and antisteroids on alkaline phosphatase activity in human endometrial cancer cells (Ishikawa line).

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Alkaline phosphatase activity in human endometrial cancer cells of the estrogen-responsive Ishikawa line was markedly stimulated (3-20-fold in 4 days) by estrogens, 5 alpha-dihydrotestosterone, and dehydroepiandrosterone but not by testosterone, medroxyprogesterone acetate, glucocorticoids, several

Antitumor effects of metformin via indirect inhibition of protein phosphatase 2A in patients with endometrial cancer.

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Metformin, an antidiabetic drug, inhibits the endometrial cancer cell growth in vivo by improving the insulin resistance; however, its mechanism of action is not completely understood. Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase associated with insulin resistance and type 2

MiR-205 inhibits cell apoptosis by targeting phosphatase and tensin homolog deleted on chromosome ten in endometrial cancer Ishikawa cells.

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BACKGROUND MicroRNAs (miRNAs) are frequently dysregulated in human cancers and can act as either potent oncogenes or tumor suppressor genes. In the present study, we intend to prove that the gene PTEN (phosphatase and tensin homolog deleted on chromosome ten) is a target gene of miR-205 and to

[MicroRNA-145-5p over-expression suppresses proliferation, migration and invasion and promotes apoptosis of human endometrial cancer cells by targeting dual specific phosphatase 6].

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To investigate the role of microRNA-145-5p (miR-145-5p) in regulating the proliferation, migration, invasion and apoptosis of human endometrial carcinoma cells.Human endometrial carcinoma Ishikawa cells were transfected with miR-145-5p mimic, miR-145-5p

[Biochemical studies on alkaline phosphatase isoenzyme profile in endometrial cancer].

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Heat-stable ALP has been attracting attention as one of the oncodevelopmental proteins. ALP are now subdivided by biochemical methods into three major groups e.g. tissue-unspecific, intestinal and term placental isoenzymes. Furthermore, term placental ALP in cancer is classified into L-leucine

Phosphatase and tensin homolog (PTEN) pseudogene expression in endometrial cancer: a conserved regulatory mechanism important in tumorigenesis?

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OBJECTIVE The PTEN pseudogene, PTENP1, was recently shown to play a role in cell proliferation in a prostate cancer model. In the present study, we sought to determine whether PTENP1 is expressed in endometrial cancer (EMCA) cell lines and primary tumors along with the microRNAs (miRNAs) that are

Biochemical properties of alkaline phosphatase from endometrial cancer cells.

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The occurrence of alkaline phosphatase (AP) activity was examined in several human endometrial adenocarcinomas. Catalytic activities were detectable only in 10 out of 15 tumors, with no apparent correlation between elevated AP and histological type. The apparent molecular weight of the enzyme after

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