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glucosamine/рак дојке

Веза се чува у привремену меморију
Страна 1 од 57 резултати

Synthesis of 6'-O-lissamine-rhodamine B-glucosamine as a novel probe for fluorescence imaging of lysosomes in breast tumors.

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Lysosomes contain multiple proteases, which play a crucial role in breast cancer invasion and metastasis. Noninvasive labeling of lysosomes in breast cancer cells and solid breast tumor models is therefore useful to study lysosomal trafficking and its role in invasion. We have synthesized a novel

Inhibition of PKC-Induced COX-2 and IL-8 Expression in Human Breast Cancer Cells by Glucosamine.

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Breast cancer is a common cancer leading to many deaths among females. Cyclooxygenase-2 (COX-2) and interleukin-8 (IL-8) are two highly expressed inflammatory mediators to be induced by the protein kinase C (PKC) signaling via various inflammatory stimuli and both contribute significantly to cancer

Phase II study of glucosamine with chondroitin on aromatase inhibitor-associated joint symptoms in women with breast cancer.

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OBJECTIVE Many women with hormone receptor-positive breast cancer discontinue effective aromatase inhibitor (AI) treatment due to joint symptoms. METHODS We conducted a single-arm, open-label, phase II study evaluating glucosamine-sulfate (1,500 mg/day) + chondroitin-sulfate (1,200 mg/day) for 24

Glucosamine-bound near-infrared fluorescent probes with lysosomal specificity for breast tumor imaging.

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Noninvasive imaging of lysosomes will be useful 1) to elucidate the role of lysosomal parameters in cancer, 2) to diagnose malignant lesions, and 3) to evaluate future lysosome-targeted anticancer therapies. Lysosome-specific labeling of glucosamine-bound near-infrared (NIR) fluorescent probes, IR-1

Folate/N-acetyl glucosamine conjugated mesoporous silica nanoparticles for targeting breast cancer cells: A comparative study.

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Folate receptors (FR) have been well recognized as a marker to target nano-sized carriers for cancer diagnosis and therapy. In contrast, influx transport systems (e.g. GLUT transporters) that transport essential amino acids and nutrients to cancer cells have not been exploited much for targeted

Autoradiographic localization of glycoprotein in human breast cancer cells maintained in organ culture after incubation with (3H)fucose or (3H)glucosamine.

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Explants of nine infiltrating duct carcinomas of the human female breast, maintained in organ culture, were exposed to the glycoprotein precursors, L-[3H]furcose and [3H]glucosamine, in order to determine the cellular distribution of newly synthesized glycoprotein as revealed by autoradiography with

Glucosamine decreases the stemness of human ALDH+ breast cancer stem cells by inactivating STAT3.

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Cancer stem cells (CSCs) are a subpopulation of cancer cells responsible for tumor maintenance and relapse due to their ability to resist various anticancer effects. Owing to the resistance of CSCs to the effects of targeted therapy, an alternative strategy that targets post-translational

Monoclonal antibody identification and characterization of a Mr 43,000 membrane glycoprotein associated with human breast cancer.

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A monoclonal antibody (323/A3) with a high degree of selectivity for binding to breast cancer cells was produced by immunization of mice with MCF-7 human breast cancer cells. The antigen recognized by 323/A3 on MCF-7 appears to be surface localized, and by enzyme-linked immunosorbent assay, the

The calcitonin receptor on T 47D breast cancer cells. Evidence for glycosylation.

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The glycosyl nature of the receptor for the peptide hormone calcitonin has been investigated in a human breast cancer cell line, T 47D. Studies have been carried out to assess the ability of various lectins and of the antibiotic tunicamycin to inhibit specific binding of calcitonin to the cells, to

Cell cycle-specific growth inhibition of human breast cancer cells induced by metabolic inhibitors.

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Proliferation of exponentially growing breast cancer cells (line Hs578T) was blocked specifically in G1 by 3-hydroxy-3-methylglutaryl Coenzyme A (HMG CoA) reductase inhibition, as well as by inhibition of N-linked glycosylation. As a consequence of these inhibitory conditions, the cells were

Glucosamine is an effective chemo-sensitizer via transglutaminase 2 inhibition.

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Aberrant increases of transglutaminase 2 (TGase 2) in tumors contribute to drug resistance. The role of TGase 2 in cancer pathogenesis was unknown until we showed that TGase 2 activates NF-kappaB in the absence of kinase-dependent phosphorylation. It appears that increased expression of TGase 2 is

MUC1 expression in human breast cancer cells is altered by the factors affecting cell proliferation.

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Increased expression of the epithelial mucin MUC1 has been linked to tumor aggressiveness in human breast carcinoma. In the present study, we have investigated if the factors affecting cells proliferation could influence MUC1 mucin biosynthesis and shedding from cell surface into the culture medium

Requirement for isoprenoid-dependent posttranslational modifications in the cell-cycle progression of human breast-cancer cells.

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Treatment with HMG CoA reductase inhibitors, i.e. 25-hydroxycholesterol and mevinolin, inhibited cell growth of the human breast cancer cell line MDA231 in a cell cycle-specific manner by blocking progression through G1. Since 25-hydroxycholesterol, as distinguished from mevinolin, also inhibits

A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans.

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The alpha2,3 sialyltransferase, alpha2,3 SAT (O), catalyzes the transfer of sialic acid to Galbeta1,3 N-acetyl-D-galactosamine (GalNAc) (core-1) in mucin type O-glycosylation, and thus terminates chain extension. A Core-2 branch can also be formed from core-1 by the core-2 beta1,6

Targeting breast cancer with sugar-coated carbon nanotubes.

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OBJECTIVE To evaluate the use of glucosamine functionalized multiwalled carbon nanotubes (glyco-MWCNTs) for breast cancer targeting. METHODS Two types of glucosamine functionalized MWCNTs were developed (covalently linked glucosamine and non-covalently phospholipid-glucosamine coated) and evaluated
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