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The Thomsen-Friedenreich Antigen-Specific Antibody Signatures in Patients with Breast Cancer.

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Alterations in the glycosylation of serum total immunoglobulins show these antibodies to have a diagnostic potential for cancer but the disease-related Abs to the tumor-associated antigens, including glycans, have still poorly been investigated in this respect. We analysed serum samples from

Hypoxia and serum deprivation induces glycan alterations in triple negative breast cancer cells.

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Triple negative breast cancer (TNBC) is a major global public health problem. The lack of targeted therapy and the elevated mortality evidence the need for better knowledge of the tumor biology. Hypoxia and aberrant glycosylation are associated with advanced stages of malignancy, tumor progression

Serum IgA1 shows increased levels of α2,6-linked sialic acid in breast cancer.

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The lectin Helix pomatia agglutinin (HPA) recognizes altered glycosylation in solid cancers and the identification of HPA binding partners in tumour tissue and serum is an important aim. Among the many HPA binding proteins, IgA1 has been reported to be the most abundant in liver metastases.

Sialylation of E-cadherin does not change the spontaneous or ET-18-OMe-mediated aggregation of MCF-7 human breast cancer cells.

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We have investigated the role of sialylation on cell-cell adhesion mediated by E-cadherin. Two MCF-7 human breast cancer cell variants were studied: MCF-7/AZ cells showed a spontaneous cell-cell adhesion in the fast and slow aggregation assay. whereas the adhesion deficient MCF-7/6 cell variant

N-acetylgalactosamine, N-acetylglucosamine and sialic acid expression in primary breast cancers.

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Binding of the lectin from Helix pomatia (HPA), which recognises N-acetylgalactosamine and N-acetylglucosamine glycans, is a predictor of metastasis and poor prognosis in a number of human adenocarcinomas, including breast cancer. The glycoproteins to which it binds in these tumours have been only

Lectin chromatography/mass spectrometry discovery workflow identifies putative biomarkers of aggressive breast cancers.

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We used a lectin chromatography/MS-based approach to screen conditioned medium from a panel of luminal (less aggressive) and triple negative (more aggressive) breast cancer cell lines (n=5/subtype). The samples were fractionated using the lectins Aleuria aurantia (AAL) and Sambucus nigra agglutinin

Effect of alpha 2,6 sialylation on integrin-mediated adhesion of breast cancer cells to fibronectin and collagen IV.

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OBJECTIVE To determine the role of sialylation on α5β1 and α2β1 integrins in the regulation of adhesion between breast cancer cells and extracellular matrix (ECM). METHODS Static cell adhesion assays were performed to quantify avidity of breast cancer cells to ECM. The effects of sialidases on α2,6

[Expression of galectin-3 and Sambucus nigra agglutinin and its clinicopathological significance in benign and malignant lesions of breast].

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OBJECTIVE To detect the expression of galectin-3 (gal-3) and Sambucus nigra agglutinin (SNA) and determine their clinicopathological significance in breast cancers and benign breast lesions. METHODS Envison immunohistochemistry for staining gal-3 expression, and ABC affinity-cytochemistry to detect

Triterpenoid Acids as Important Antiproliferative Constituents of European Elderberry Fruits.

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In Europe, both the fruits and flowers of Sambucus nigra L. have been used against cold, as well as laxative, diaphoretic, and diuretic remedies. There are also a number of commercially available food products that contain elderberry juice, puréed or dried elderberries. Recent comprehensive

A lectin HPLC method to enrich selectively-glycosylated peptides from complex biological samples.

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Glycans are an important class of post-translational modifications. Typically found on secreted and extracellular molecules, glycan structures signal the internal status of the cell. Glycans on tumor cells tend to have abundant sialic acid and fucose moieties. We propose that these cancer-associated

Purification and characterization of cathepsin D from normal human breast tissue.

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The lysosomal aspartyl protease cathepsin D is present in most mammalian cells and is active in the catabolism of intracellular and endocytosed proteins. It appears to be overexpressed and abnormally secreted in breast cancer cells, and may contribute to the process of tumor metastasis. In the

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