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nucleotidase/سرطان الثدي

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مقالاتالتجارب السريريةبراءات الاختراع
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Overexpression of Ecto-5'-nucleotidase (CD73) promotes T-47D human breast cancer cells invasion and adhesion to extracellular matrix.

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الدخول التسجيل فى الموقع
Ecto-5'-nucleotidase (CD73) was overexpressed in malignancies of epithelial origin and was involved in a variety of cellular processes such as cytoprotection and anti-inflammation. In the present study, human mammary T-47D cells were transfected with pcDNA-NT5E to establish a CD73 overexpressed cell

Alterations in serum glycosyltransferases and 5'-nucleotidase in breast cancer patients.

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We have measured sialyltransferase, galactosyltransferase, and fucosyltransferase as sell as 5'-nucleotidase in the serum of breast cancer patients. Serum sialyltransferase values in 65 normal healthy females ranged from 2.6 to 8.5 units, with a mean of 5.4. In 25 women with operable primary breast

Role of estrogen receptor in the regulation of ecto-5'-nucleotidase and adenosine in breast cancer.

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OBJECTIVE The purpose is to understand the expression of ecto-5'-nucleotidase (eN), an adenosine producing enzyme with potential roles in angiogenesis, growth, and immunosuppression, in estrogen receptor (ER)-negative and -positive breast cancer. METHODS We investigated the regulation of eN

A preliminary study of the role of extracellular -5'- nucleotidase in breast cancer stem cells and epithelial-mesenchymal transition.

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Tumor stem cell theory may well explain a variety of malignant behaviors of tumors. Cells undergoing epithelial-mesenchymal transition (EMT) share many characteristics with tumor stem cells. Our previous studies showed that extracellular -5'- nucleotidase (CD73), one of the important surface markers

Serum 5'-nucleotidase: automation of a manual assay and brief observations on values in patients with breast cancer.

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We have modified a manual assay method for the determination of serum 5'-nucleotidase so that the reaction product, phosphate, is assayed colorimetrically using a continuous flow system. The contribution of non-specific phosphatase enzymes is assessed in the presence of nickel ions which

Ecto-5'-nucleotidase promotes invasion, migration and adhesion of human breast cancer cells.

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OBJECTIVE Associated with many molecules, metastasis includes cell adhesion to extracellular matrix, migration towards specific direction and invasion into local vessel of distant organs. The purpose of the present study was to evaluate the role of ecto-5'-nucleotidase (eN, ecto-5-NT, CD73)

Serum 5'-nucleotidase of a breast cancer patient.

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Serum derived from the breast cancer patient included in this study was found to be a rich source of 5'-nucleotidase. In addition, it also contains nonspecific alkaline phosphatase. The properties of 5'-nucleotidase were studied by eliminating the interference of serum non-specific alkaline

Serum sialyltransferase and 5'-nucleotidase as reliable biomarkers in women with breast cancer.

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Sialyltransferase and 5'-nucleotidase were measured in the sera of 135 women with breast cancer: 53 undergoing mastectomy for primary cancer and 83 receiving different modalities of palliative therapy for metastatic disease. The objective of this study was to determine whether these enzyme levels

The cytosolic 5'-nucleotidase cN-II lowers the adaptability to glucose deprivation in human breast cancer cells.

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The cytosolic 5'-nucleotidase cN-II is a highly conserved enzyme implicated in nucleotide metabolism. Based on recent observations suggesting additional roles not directly associated to its enzymatic activity, we studied human cancer cell models with basal or decreased cN-II expression. We developed

RNA interference of ecto-5'-nucleotidase (CD73) inhibits human breast cancer cell growth and invasion.

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الدخول التسجيل فى الموقع
Metastasis is a leading cause of mortality and morbidity in breast cancer. Recently, dramatic overexpression of ecto-5'-nucleotidase (CD73), a glycosylphosphatidylinositol-anchored cell surface protein has been found in estrogen receptor-negative [ER (-)] breast cancer cell lines and in clinical

Effects of ecto-5'-nucleotidase on human breast cancer cell growth in vitro and in vivo.

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Ecto-5'-nucleotidase (CD73) is an essential enzyme that generates adenosine, an essential molecule for cell growth. CD73 increases significantly in many breast cancers. In this study, alpha,beta-methylene adenosine-5'-diphosphate (APCP), a specific CD73 inhibitor was used to block the hydrolase's

Extracellular 5'-nucleotidase (CD73) promotes human breast cancer cells growth through AKT/GSK-3β/β-catenin/cyclinD1 signaling pathway.

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To identify the role and to explore the mechanism of extracellular 5'-nucleotidase (CD73) in human breast cancer growth, CD73 expression was measured firstly in breast cancer tissues and cell lines, and then interfered with or over-expressed by recombinant lentivirus in cell lines. Impacts of CD73

Serum adenosine deaminase, 5'-nucleotidase & alkaline phosphatase in breast cancer patients.

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Serum levels of adenosine deaminase (ADA), 5-nucleotidase (5'-NT) and alkaline phosphatase (ALP) were studied in 25 patients of carcinoma breast and 25 normal subjects. Adenosine deaminase was found to be the better probable parameter for the detection of cancer and to assess the development of

Enzymes that hydrolyze adenine nucleotides in platelets from breast cancer patients.

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The activities of NTPDase (EC 3.6.1.5, apyrase, CD39) and 5'-nucleotidase (EC 3.1.3.5, CD73) enzymes were analyzed in platelets from breast cancer patients. Initially, patients were compared in terms of length (years) of tamoxifen use. The following groups were studied: breast cancer patients who

Lipid rafts remodeling in estrogen receptor-negative breast cancer is reversed by histone deacetylase inhibitor.

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الدخول التسجيل فى الموقع
Recently, we have found dramatic overexpression of ecto-5'-nucleotidase (or CD73), a glycosylphosphatidylinositol-anchored component of lipid rafts, in estrogen receptor-negative [ER-] breast cancer cell lines and in clinical samples. To find out whether there is a more general shift in expression
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