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Glycoprotein pattern in human brain tumors studied using lectin binding after sodium dodecyl sulfate-gel electrophoresis and protein blotting.

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The immunoblotting technique was used to study the glycoproteins in human brain tumor samples including astrocytoma, glioblastoma, meningioma and oligodendroglioma, as well as in normal human brain. Glycoproteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis,

Lectin histochemistry of kidney tumours and its pathomorphological relevance.

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Thirty kidney tumours of various histological type were histochemically investigated under the light microscope by means of the ABC-method. We used four biotinylated lectins which are known to bind also to normal renal tubular epithelial cells of different nephron segments. The nuclear grade, the

Glycoconjugates in retinoblastoma. A lectin histochemical study of ten formalin-fixed and paraffin-embedded tumours.

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The binding of eleven biotin- or peroxidase-coupled lectins with different carbohydrate specificities to tumour tissue and remaining morphologically normal retina was studied in ten formalin-fixed and paraffin-embedded human eyes with retinoblastoma. In undetached retinas, outer and inner segments

Lectin expression in carcinoid tumours of the gastrointestinal tract.

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The binding of peroxidase-conjugated Dolichos biflorus (DBA), Triticum vulgaris (WGA), Canavalia ensiformis (Con A), Arachis hypogaea (PNA), Lotus tetragonolobus, and Bandeiraea simplicifolia I (BSAI) to gastrointestinal carcinoid tumours was studied. The results indicate that carcinoid tumour cells

Lectin expression in neoplastic and non-neoplastic lesions of the rectum.

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The expression of six lectins (Arachis hypogaea, B. simplicifolia I, concanavalin A, Dolichus biflorus, Triticum vulgaris, Lotus tetragonolobus) was studied in 24 adenocarcinomas, 24 adenomas, 20 metaplastic polyps, 17 specimens of mucosal prolapse (solitary ulcer syndrome) and 10 of normal mucosa,

Glycosylation of alpha-1-proteinase inhibitor and haptoglobin in ovarian cancer: evidence for two different mechanisms.

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The change in glycosylation of the two acute-phase proteins, alpha-1-proteinase inhibitor (API) and haptoglobin (Hp), in progressive ovarian cancer is different. This has been shown by monosaccharide analysis and lectin-binding studies of proteins purified from serum. In the glycan chains of API,

Lotus tetragonolobus and Maackia amurensis lectins influence phospho-IκBα, IL-8, Lewis b and H type 1 glycoforms levels in H. pylori infected CRL-1739 gastric cancer cells.

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OBJECTIVE Attachment of Helicobacter pylori to the mucous epithelial cells and the mucous layer is said to be a crucial step for infection development. Sugar antigens of gastric mucins (MUC5AC, MUC1) can act as receptors for bacterial adhesins. The aim of the study was to investigate if Lotus

Serum alpha-1-proteinase inhibitor with abnormal properties in ovarian cancer.

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It was previously reported that sera from ovarian cancer patients contained abnormal forms of alpha-1-proteinase inhibitor (API) that predicted unresponsiveness to chemotherapy. These molecules were detected by extracting the sera with the fucose-specific lectin, lotus tetragonolobus, and analysing

Lymph node metastasis-related carbohydrate epitopes of gastric cancer with submucosal invasion.

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This study was conducted to examine the lymph node metastasis-related carbohydrate epitopes of cancer cells in primary lesions of gastric cancer with submucosal invasion (sm gastric cancer). A total of 118 formalin-fixed and paraffin-embedded surgical specimens were studied. Carbohydrate epitopes

Increased fucosylation and other carbohydrate changes in haptoglobin in ovarian cancer.

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Cancer sera have high levels of an abnormal form of haptoglobin (Hp) that can be extracted from blood using the fucose-specific lectin, Lotus tetragonolobus. In order to investigate the carbohydrate abnormality that is responsible for this effect, the monosaccharide composition of Hp has been

Fucose-containing antigens in normal and neoplastic human gastric mucosa: a comparative study using lectin histochemistry and blood group immunohistochemistry.

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The histochemical binding to normal and neoplastic human gastric mucosa of two lectin-peroxidase conjugates which are specific for fucose-containing glycoconjugates is described. The lectins are Ulex europaeus (UEA1) and Lotus tetragonolobus (LTA). Results are compared with ABO and secretor status

Distribution of fucosubstance in kidney and related neoplasms. Absence of lectin-reactive alpha-fucose from the vasculature of bilateral Wilm's tumors.

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Two alpha-fucose-binding lectins, Ulex europaeus agglutinin I (UEA I) and Lotus tetragonolobus agglutinin, were employed to compare and contrast the distribution of fucosubstance in normal human kidneys and a variety of renal tumors. The study employed a total of 31 kidneys surgically removed for

[Glycoproteins associated with metastatic potential of cancer].

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Carbohydrate moieties of glycoproteins have been implicated to be involved in cellular adhesion. Therefore, certain carbohydrate structures in glycoproteins are expected to be associated with metastatic behaviour of cancer cells; such carbohydrate structure can be used as an indicator for the

Decreased branching, increased fucosylation and changed sialylation of alpha-1-proteinase inhibitor in breast and ovarian cancer.

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Proteolytic enzymes could be very important in spread of cancer, but the role of the body's natural inhibitors of these enzymes in this process is unknown. One such inhibitor is the serum glycoprotein, alpha-1-proteinase inhibitor (API). In previous studies we showed that the fucose-specific lectin,

Elevated levels of abnormally-fucosylated haptoglobins in cancer sera.

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Cancer sera have higher levels of serum protein-bound fucose than sera from healthy individuals. In an attempt to identify the cause of this increase, fucoproteins were extracted from the sera of cancer patients and healthy individuals using a fucose-specific lectin (lotus tetragonolobus) coupled to

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