Expression of N-Acetyl Galactosaminylated and Sialylated Glycans by Metastases Arising from Primary Breast Cancer

Brooks, Susan A.; Leathem, Anthony

doi:10.1159/000024504

Cited by 22 publications

(11 citation statements)

References 21 publications

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“…[65][66][67][68]. Lipid-and protein-bound Sia are also elevated in the plasma from cancer patients as compared with healthy individuals [66,[69][70][71][72] and are linked to acute phase condition and chronic disease [e.g.…”

Section: Role Of Neu1 In Regulation Of Receptors and Signalling Pathwaysmentioning

confidence: 99%

Where catabolism meets signalling: neuraminidase 1 as a modulator of cell receptors

Pshezhetsky

Hinek

2011

Glycoconj J

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Terminal sialic acid residues are found in abundance in glycan chains of glycoproteins and glycolipids on the surface of all live cells forming an outer layer of the cell originally known as glycocalyx. Their presence affects the molecular properties and structure of glycoconjugates, modifying their function and interactions with other molecules. Consequently, the sialylation state of glycoproteins and glycolipids has been recognized as a critical factor modulating molecular recognitions inside the cell, between the cells, between the cells and the extracellular matrix, and between the cells and certain exogenous pathogens. Sialyltransferases that attach sialic acid residues to the glycan chains in the process of their initial synthesis were thought to be mainly responsible for the creation and maintenance of a temporal and spatial diversity of sialylated moieties. However, the growing evidence also suggests that in mammalian cells, at least equally important roles belong to sialidases/neuraminidases, which are located on the cell surface and in intracellular compartments, and may either initiate the catabolism of sialoglycoconjugates or just cleave their sialic acid residues, and thereby contribute to temporal changes in their structure and functions. The current review summarizes emerging data demonstrating that neuraminidase 1 (NEU1), well known for its lysosomal catabolic function, can be also targeted to the cell surface and assume the previously unrecognized role as a structural and functional modulator of cellular receptors.

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Section: Role Of Neu1 In Regulation Of Receptors and Signalling Pathwaysmentioning

confidence: 99%

Where catabolism meets signalling: neuraminidase 1 as a modulator of cell receptors

Pshezhetsky

Hinek

2011

Glycoconj J

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“…In addition, the distribution of sialic acid on specific N - or O -linked oligosaccharides has been demonstrated to alter the metastatic potential of cancer cell lines (15). In some cases tumor development has been associated with over expression of β1–6 branching that results in increased number of Galβ1–4GlcNAc structures available for sialylation (16–18). Therefore, exploring cell-surface sialylation changes during tumor development and disease progression likely affords excellent opportunities to identify sensitive and specific cancer biomarkers.…”

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confidence: 99%

Targeted Identification of Metastasis-associated Cell-surface Sialoglycoproteins in Prostate Cancer

Yang

Nyalwidhe

Guo

et al. 2011

Molecular & Cellular Proteomics

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Covalent attachment of carbohydrates to proteins is one of the most common post-translational modifications. At the cell surface, sugar moieties of glycoproteins contribute to molecular recognition events involved in cancer metastasis. We have combined glycan metabolic labeling with mass spectrometry analysis to identify and characterize metastasis-associated cell surface sialoglycoproteins. Our model system used syngeneic prostate cancer cell lines derived from PC3 (N2, nonmetastatic, and ML2, highly metastatic). The metabolic incorporation of AC4ManNAz and subsequent specific labeling of cell surface sialylation was confirmed by flow cytometry and confocal microscopy. Affinity isolation of the modified sialic-acid containing cell surface proteins via click chemistry was followed by SDS-PAGE separation and liquid chromatography-tandem MS analysis. We identified 324 proteins from N2 and 372 proteins of ML2. Using conservative annotation, 64 proteins (26%) from N2 and 72 proteins (29%) from ML2 were classified as extracellular or membrane-associated glycoproteins. A selective enrichment of sialoglycoproteins was confirmed. When compared with global proteomic analysis of the same cells, the proportion of identified glycoprotein and cell-surface proteins were on average threefold higher using the selective capture approach. Functional clustering of differentially expressed proteins by Ingenuity Pathway Analysis revealed that the vast majority of glycoproteins overexpressed in the metastatic ML2 subline were involved in cell motility, migration, and invasion. Our approach effectively targeted surface sialoglycoproteins and efficiently identified proteins that underlie the metastatic potential of the ML2 cells.

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“…Targeting of T and Tn markers by lectins proved to be an efficient tool for both the detection and prognosis of many cancers [94,95,96]. Especially, lectin binding pattern of peanut (PNA) and horse gram (DBA from Dolichos biflorus ) agglutinins, were used as histochemical probes to determine the malignant status of both oral and colonic mucosa [97,98,99,100,101,102]. Moreover, the density of Tn antigen at the cell surface appeared as a good predictor of the aggressiveness in primary breast carcinoma [103].…”

Section: Tn/t-specific Lectins For Cancer Diagnosis/prognosismentioning

confidence: 99%

Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Prognosis and Therapy

Poiroux

Barre

Damme

et al. 2017

IJMS

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Aberrant O-glycans expressed at the surface of cancer cells consist of membrane-tethered glycoproteins (T and Tn antigens) and glycolipids (Lewis a, Lewis x and Forssman antigens). All of these O-glycans have been identified as glyco-markers of interest for the diagnosis and the prognosis of cancer diseases. These epitopes are specifically detected using T/Tn-specific lectins isolated from various plants such as jacalin from Artocarpus integrifola, and fungi such as the Agaricus bisporus lectin. These lectins accommodate T/Tn antigens at the monosaccharide-binding site; residues located in the surrounding extended binding-site of the lectins often participate in the binding of more extended epitopes. Depending on the shape and size of the extended carbohydrate-binding site, their fine sugar-binding specificity towards complex O-glycans readily differs from one lectin to another, resulting in a great diversity in their sugar-recognition capacity. T/Tn-specific lectins have been extensively used for the histochemical detection of cancer cells in biopsies and for the follow up of the cancer progression and evolution. T/Tn-specific lectins also induce a caspase-dependent apoptosis in cancer cells, often associated with a more or less severe inhibition of proliferation. Moreover, they provide another potential source of molecules adapted to the building of photosensitizer-conjugates allowing a specific targeting to cancer cells, for the photodynamic treatment of tumors.

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Expression of N-Acetyl Galactosaminylated and Sialylated Glycans by Metastases Arising from Primary Breast Cancer

Cited by 22 publications

References 21 publications

Where catabolism meets signalling: neuraminidase 1 as a modulator of cell receptors

Where catabolism meets signalling: neuraminidase 1 as a modulator of cell receptors

Targeted Identification of Metastasis-associated Cell-surface Sialoglycoproteins in Prostate Cancer

Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Prognosis and Therapy

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