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In silico analysis of molecular mechanisms of Galanthus nivalis agglutinin-related lectin-induced cancer cell death from carbohydrate-binding motif evolution hypothesis.

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Galanthus nivalis agglutinin-related lectins, a superfamily of strictly mannose-binding-specific lectins widespread amongst monotyledonous plants, have drawn a rising attention for their remarkable anti-proliferative and apoptosis-inducing activities toward various types of cancer cells; however,

Determination of hyperglycosylated human chorionic gonadotropin produced by malignant gestational trophoblastic neoplasias and male germ cell tumors using a lectin-based immunoassay and surface plasmon resonance.

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The ability to reliably detect aberrant glycosylation of human chorionic gonadotropin (hCG) may have profound implications for the diagnosis and monitoring of malignant gestational trophoblastic neoplasia, germ cell tumors, other malignancies, and pregnancy complications. To become a clinically

Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties.

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To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize

Anti-tumor and anti-viral activities of Galanthus nivalis agglutinin (GNA)-related lectins.

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Galanthus nivalis agglutinin (GNA)-related lectin family, a superfamily of strictly mannose-binding specific lectins widespread among monocotyledonous plants, is well-known to possess a broad range of biological functions such as anti-tumor, anti-viral and anti-fungal activities. Herein, we mainly

Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines.

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BACKGROUND The aim of the present study was to determine whether stage of invasiveness of bladder cancer cell lines contributes to alterations in glycan pattern of their cadherins. RESULTS Human non-malignant epithelial cell of ureter HCV29, v-raf transfected HCV29 line (BC3726) and transitional

Lectin Histochemistry Shows WGA, PHA-L and HPA Binding Increases During Progression of Human Colorectal Cancer.

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OBJECTIVE Most colorectal carcinomas develop from an adenoma-carcinoma sequence to metastatic disease. The aim of the present study was to use lectins, carbohydrate-binding proteins, to detect changes in glycosylation during this malignant progression. METHODS Sections from normal colorectal mucosa,

Induction of apoptosis by Polygonatum odoratum lectin and its molecular mechanisms in murine fibrosarcoma L929 cells.

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BACKGROUND The Galanthus nivalis agglutinin (GNA)-related lectins have been reported to bear antiproliferative and apoptosis-inducing activities in cancer cells; however, the precise mechanisms by which GNA-related lectins induce cell death are still only rudimentarily understood. METHODS In the

Carbohydrate moieties of N-cadherin from human melanoma cell lines.

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Expression of N-cadherin an adhesion molecule of the cadherin family, in tumor cells is associated with their increased invasive potential. Many studies suggested the role of N-linked oligosaccharides as important factors that contribute to metastasis by influencing tumor cell invasion and adhesion.

Lectin-binding sites in epithelial cells of the mouse prostate gland.

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The prostate is an exocrine gland in the male reproductive tract that secretes seminal fluids. To gain insight into the cytochemical properties of prostatic epithelial cells, the characteristics of glycoconjugates in mouse prostate sections were examined by lectin histochemistry and

Polygonatum cyrtonema lectin induces murine fibrosarcoma L929 cell apoptosis via a caspase-dependent pathway as compared to Ophiopogon japonicus lectin.

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Galanthus nivalis agglutinin (GNA)-related lectin family, a superfamily of strictly mannose-binding specific lectins, has been well-known to possess several biological functions including apoptosis-inducing activities. However, the precise mechanisms of GNA-related lectins to induce apoptosis

Comparison of the lectin-binding pattern in different human melanoma cell lines.

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Glycosylation is generally altered in tumour cells in comparison with their normal counterparts. These alterations are thought to be important because they contribute to the abnormal behaviour of cancer cells. Therefore, we have comparatively analysed the glycoproteins in cell extracts from human

Altered glycosylation associated with dedifferentiation of hepatocellular carcinoma: a lectin microarray-based study.

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Altered glycosylation associated with hepatocellular carcinoma (HCC) is well documented. However, few reports have investigated the association between dedifferentiation and glycosylation. Therefore, the aim of this study was to analyze glycosylation associated with dedifferentiation

Polygonatum odoratum lectin induces apoptosis and autophagy by regulation of microRNA-1290 and microRNA-15a-3p in human lung adenocarcinoma A549 cells.

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Polygonatum odoratum lectin (POL), a mannose-binding specific Galanthus nivalis agglutinin (GNA)-related lectin has been reported with remarkable anti-proliferative and apoptosis-inducing effects against several tumor cells. Our previous research revealed that POL can induce apoptosis and autophagy

Structural analysis and binding properties of isoforms of tarin, the GNA-related lectin from Colocasia esculenta.

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The lectins, a class of proteins that occur widely in animals, plants, fungi, lichens and microorganisms, are known for their ability to specifically bind to carbohydrates. Plant lectins can be classified into 12 families including the Galanthus nivalis agglutinin (GNA)-related lectin superfamily,

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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