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adenoma/flädersläktet
Länken sparas på Urklipp
5 resultat
Grading dysplasia in colorectal adenomas by means of the quantitative binding pattern determination of Arachis hypogaea, Dolichos biflorus, Amaranthus caudatus, Maackia amurensis, and Sambucus nigra agglutinins.
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The current study deals with the setting up of a new tool that enables the benign versus the malignant nature of colorectal adenomas to be determined accurately. The 2 objectives are to determine (1) whether adenomas should, or should not, be included in a 2- or a 3-tier grading system, and (2)
Expression of alpha 2,6-linked sialic acid residues in neoplastic but not in normal human colonic mucosa. A lectin-gold cytochemical study with Sambucus nigra and Maackia amurensis lectins.
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Increased sialylation of cell surface glycoconjugates has been demonstrated in malignant tumors and shown to be correlated with the invasive and metastatic growth of colon carcinoma cells. The authors have applied the Maackia amurensis lectin, which interacts with alpha 2,3-linked sialic acid, and
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,
Neoplastic transformation of the thyroid gland is accompanied by changes in cellular sialylation.
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Cancer of the thyroid gland is one of the most common endocrine diseases. Histological evaluation is often complicated by difficulty in distinguishing between benign and malignant lesions. Abnormal glycosylation of cell structures, including changes in sialylation, is a feature of the neoplastic
Sialylation of intracellular proteins of thyroid lesions.
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Enhanced sialylation represents one of the most frequently occurring alterations of the sugar chain structure in various cancers. However, up to now, sialylation of intracellular proteins of thyroid carcinomas has never been investigated. The aim of this study was comparative analysis of cytoplasmic
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