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pyruvate kinase/tumori dojke
Veza se sprema u međuspremnik
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Tumor type M2 pyruvate kinase expression in advanced breast cancer.
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BACKGROUND
Recently, a high validity correlation of the tumor M2 pyruvate kinase (Tu M2-PK) isoenzyme in comparison to standard tumor markers has been demonstrated in solid tumors. We investigated this marker in 67 patients with advanced breast cancer (ABC) in comparison to healthy
Plasma levels of HER-2/neu, tumor type M2 pyruvate kinase and its tyrosine-phosphorylated metabolite in advanced breast cancer.
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BACKGROUND
Tyrosine kinase signal transduction pathways are a focus of interest for therapeutic interventions. The oncoprotein HER-2/neu shows tyrosine kinase activity leading to phosphorylation and activation of numerous second-messenger systems. One target of phosphorylation processes is assumed
Enzyme Kinetic Assay to Measure the Activity of Tumor M2 Pyruvate Kinase in Breast Cancer Patients.
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BACKGROUND
M2 type Pyruvate kinase (PKM2) is the key rate-limiting enzyme of glycolysis, and it mainly exists as a dimer in tumor cells. This study aims to establish an enzyme kinetic assay for serum tumor M2 pyruvate kinase (TuM2-PK), and to evaluate its diagnostic value in breast
Pyruvate kinase M2 interacts with mammalian sterile 20-like kinase 1 and inhibits tamoxifen-induced apoptosis in human breast cancer cells.
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Tamoxifen has been reported to be associated with antagonism of estrogen-mediated cell growth signaling and activation of estrogen receptor-independent apoptosis events. It has been demonstrated that mammalian sterile 20-like kinase 1 is a direct target of Caspases to amplify the apoptotic signaling
Tumor M2 pyruvate kinase--determination in breast cancer patients receiving trastuzumab therapy.
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This study was designed to investigate the value of tumor M2 pyruvate kinase (tumor M2-PK) determination as an early marker for response to trastuzumab therapy in patients with metastasized breast cancer. Plasma samples of 20 trastuzumab patients were collected immediately after standard
Both high expression of pyruvate kinase M2 and vascular endothelial growth factor-C predicts poorer prognosis in human breast cancer.
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Pyruvate kinase M2 (PKM2) and vascular endothelial growth factor-C (VEGF-C) have been known to play an important role in tumorigenesis and tumor progression in breast cancer. However, the association between PKM2 and VEGF-C in breast cancer remains unclear. In the present study, a total of 218
Comparison of pyruvate kinase variants from breast tumor and normal breast.
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BACKGROUND
Pyruvate kinase isozymes in human breast tumor tissue were compared in this study with normal human breast tissue. Two forms of pyruvate kinase present in normal and tumor human breast were purified by ammonium sulfate precipitation, dialysis, gel filtration, ion exchange, and affinity
Heterogeneity of glycolytic enzyme activity and isozyme composition of pyruvate kinase in breast cancer.
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In 6 patients with breast cancer - of whom specimens of the primary tumor as well as one of its metastases were available for examination - we demonstrated intratumoral and intertumoral heterogeneity in expression of activity of the glycolytic enzymes hexokinase, phosphofructokinase, aldolase,
The clinicopathological and prognostic relevance of pyruvate kinase M2 and pAkt expression in breast cancer.
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BACKGROUND
Cancer cell growth has been described to depend on glucose utilization. Activation of Akt and up-regulation of pyruvate kinase M2 (M2-PK) are attributes of tumour glycolysis.
METHODS
In order to evaluate the prognostic relevance of glycolytic markers in breast cancer, the expression of
Metformin Induces Apoptosis and Downregulates Pyruvate Kinase M2 in Breast Cancer Cells Only When Grown in Nutrient-Poor Conditions.
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BACKGROUND
Metformin is proposed as adjuvant therapy in cancer treatment because of its ability to limit cancer incidence by negatively modulating the PI3K/AKT/mTOR pathway. In vitro, in addition to inhibiting cancer cell proliferation, metformin can also induce apoptosis. The molecular mechanism
Effect of pyruvate kinase M2-regulating aerobic glycolysis on chemotherapy resistance of estrogen receptor-positive breast cancer.
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This study aims to explore the effect and mechanism of pyruvate kinase M2 (PKM2) on chemotherapy resistance of estrogen receptor-positive breast cancer (ER BC) by regulating aerobic glycolysis. The expression of PKM2 in ER BC MCF-7 cells, T47D cells and MCF-7/ADR cells (which are subject to
Breaking Glucose Transporter 1/Pyruvate Kinase M2 Glycolytic Loop Is Required for Cantharidin Inhibition of Metastasis in Highly Metastatic Breast Cancer.
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Aerobic glycolysis plays a decisive role in cancer growth. However, its role in cancer metastasis was rarely understood. Cantharidin a natural compound from an arthropod insect cantharis exerts potent anticancer activity. Here we found cantharidin possesses significant anti-metastatic activity on
High Expression of Pyruvate Kinase M2 is Associated with Chemosensitivity to Epirubicin and 5-Fluorouracil in Breast Cancer.
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BACKGROUND
Pyruvate kinase M2 (PKM2) is the key enzyme in the Warburg effect, and it was recently reported to be involved in the metabolic pathways of chemotherapeutic drugs. However, the role of PKM2 in breast cancer and its influence in the sensitivity to front-line anticancer drugs remains
Cyclosporine A inhibits breast cancer cell growth by downregulating the expression of pyruvate kinase subtype M2.
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The high proliferative rate of tumor cells leads to metabolic needs distinct from those of their normal counterparts. An embryonic- and tumor-specific isoform of the enzyme pyruvate kinase M2 (PKM2) is overexpressed in cancer cells to increase the use of glycolytic intermediates for macromolecular
Interaction with Pyruvate Kinase M2 Destabilizes Tristetraprolin by Proteasome Degradation and Regulates Cell Proliferation in Breast Cancer.
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Pyruvate kinase M2 (PKM2), which is predominantly expressed in most cancers, plays a key role in the Warburg effect. However, how PKM2 functions as a tumor supportive protein has not been fully elucidated. Here, we identified tristetraprolin (TTP), an AU-rich, element-binding protein that regulates
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