ovarian neoplasms/phosphatase

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Catalytic and immunologic activities of placental-like alkaline phosphatase in clinical studies. The value of PLAP in follow-up of ovarian cancer.

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Placental-like alkaline phosphatase (PLAP) was measured by its catalytic activity (CA), using an amplified enzyme-linked immunoassay, and by its immunologic activity (IA), using an enzyme-linked immunosorbent assay. In both assays the same monoclonal anti-PLAP antibody was used as the primary

The tumour suppressor OPCML promotes AXL inactivation by the phosphatase PTPRG in ovarian cancer.

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In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI-anchored tumour suppressor OPCML Further, we demonstrate that AXL directly interacts with OPCML,

Ovarian cancer stem-like cells show induced translineage-differentiation capacity and are suppressed by alkaline phosphatase inhibitor.

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Spheroid formation is one property of stem cells-such as embryo-derived or neural stem cells-that has been used for the enrichment of cancer stem-like cells (CSLCs). However, it is unclear whether CSLC-derived spheroids are heterogeneous or whether they share common embryonic stemness properties.

A human monoclonal antibody specific to placental alkaline phosphatase, a marker of ovarian cancer.

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Placental alkaline phosphatase (PLAP) is a promising ovarian cancer biomarker. Here, we describe the isolation, affinity-maturation and characterization of two fully human monoclonal antibodies (termed B10 and D9) able to bind to human PLAP with a dissociation constant (Kd) of 10 and 30 nM,

Cancerous inhibitor of protein phosphatase 2A regulates cisplatin resistance in ovarian cancer.

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Ovarian cancer is the most aggressive type of gynecological cancer. The cause of the poor survival rate is the development of chemotherapy resistance to platinum-based therapies, including cisplatin. The present study aimed to investigate the mechanism of cancerous inhibitor of protein phosphatase

Radionuclide imaging of epithelial ovarian tumours with 123I-labelled monoclonal antibody (H317) specific for placental-type alkaline phosphatase.

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A murine monoclonal antibody, H317, specific for placental-type alkaline phosphatase was labelled with 123I and assessed as an imaging agent using a gamma camera computer system in 18 patients suspected of possible recurrent or metastatic ovarian cancer 1-4 years after removal of the primary tumour.

Phosphatase and Tensin Homolog Is a Potential Target for Ovarian Cancer Sensitization to Cytotoxic Agents.

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OBJECTIVE The phosphatase and tensin homolog (PTEN) tumor suppressor protein has been found to be inactivated or mutated in various human malignancies and to play a role in cisplatin and poly(ADP-ribose) polymerase inhibitor sensitivity. In this study, we assessed the association of PTEN loss with

Metastatic Phosphatase PRL-3 Induces Ovarian Cancer Stem Cell Sub-population through Phosphatase-Independent Deacetylation Modulations.

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Cancer stem cells (CSCs) are responsible for tumor initiation, chemoresistance, metastasis, and relapse, but the underlying molecular origin of CSCs remains elusive. Here we identified that metastatic phosphatase of regenerating liver 3 (PRL-3) transcriptionally upregulates SOX2 in the expansion of

Overexpression of the protein tyrosine phosphatase, nonreceptor type 6 (PTPN6), in human epithelial ovarian cancer.

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Our current understanding of human ovarian tumorigenesis is limited by the lack of a discrete precursor lesion as well as a limited knowledge of the steps in tumor progression. Since the alterations in the regulation of the tyrosyl residues on various cellular proteins appear to be an important

Elevated serum alkaline phosphatase may enable early diagnosis of ovarian cancer.

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A case of endometrioid ovarian carcinoma associated with elevated levels of serum placental-like alkaline phosphatase (PLAP) is presented. Two and a half years before a final diagnosis was made following explorative laparotomy, an incidental blood test revealed elevated alkaline phosphatase in the

Comparison of CA 125 and placental alkaline phosphatase as ovarian tumor markers.

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The serum concentrations of CA 125 and placental alkaline phosphatase were analyzed in 16 patients with ovarian cancer. Increased serum levels of CA 125 and placental alkaline phosphatase were observed in 75% and 50% of the cancer patients, respectively. The serum levels of these tumor markers were

Placental alkaline phosphatase as a tumor marker in ovarian cancer.

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The serum levels of placental alkaline phosphatase were determined with a radioimmunoassay using a polyclonal antibody on 1236 samples from 414 patients with ovarian cancer. The frequencies of elevated enzyme levels for patients with or without evidence of disease were 17.7 and 10.9%, respectively.

A gonadotropin-releasing hormone-responsive phosphatase hydrolyses lysophosphatidic acid within the plasma membrane of ovarian cancer cells.

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Lysophosphatidic acid (LPA) mediates pleomorphic effects on multiple cell lineages, including an increased proliferative response of ovarian cancer cells both in vitro and in vivo, at least in part through the novel expression of LPA receptors. Thus, LPA hydrolysis is necessary to limit the duration

Radioimmunoassay of placental alkaline phosphatase in ovarian cancer sera and tissues.

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A specific radioimmunoassay for human placental alkaline phosphatase has been developed using the 125I-labeled enzyme, highly purified with a fast protein liquid chromatography system and an absorbed rabbit antiserum. The sensitivity of this assay was 0.2 U/L. Serum levels of over 0.2 U/L were found

Translocation of lysophosphatidic acid phosphatase in response to gonadotropin-releasing hormone to the plasma membrane in ovarian cancer cell.

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OBJECTIVE Lysophosphatidic acid mediates proliferative and/or morphologic effects on multiple cell lineages, which include ovarian cancer cells. Lysophosphatidic acid hydrolysis limits the duration of lysophosphatidic acid's action. We examined hormonal translocation of lipid phosphate phosphatase

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