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Studies of lectin binding to the human cervix uteri. II: Cervical intraepithelial neoplasia and invasive squamous carcinoma

The cell surface carbohydrate profile of formalin-fixed paraffin-embedded tissue sections of neoplastic cervical squamous epithelium was evaluated using lectins of Bauhinia purpurea (BPA), Canavalin ensiformis (Con A), Griffonia simplicifolia I (GS I), Griffonia simplicifolia II (GS II), Maclura pom...

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Bibliographic Details
Published in:The Histochemical journal 1989-06, Vol.21 (6), p.323-336
Main Authors: BYRNE, P, WILLIAMS, A, ROLLASON, T
Format: Article
Language:English
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Summary:The cell surface carbohydrate profile of formalin-fixed paraffin-embedded tissue sections of neoplastic cervical squamous epithelium was evaluated using lectins of Bauhinia purpurea (BPA), Canavalin ensiformis (Con A), Griffonia simplicifolia I (GS I), Griffonia simplicifolia II (GS II), Maclura pomifera (MPA), Archis hypogaea (PNA), Glycine max (SBA), Ulex europaeus I (UEA I) and Triticum vulgaris (WGA). Three lectins (BPA, Con A and PNA) showed a similar pattern of staining in both normal squamous epithelium and in cervical intraepithelial neoplasia (CIN). Variable alterations were seen in lectin-binding patterns in CIN with seven lectins (GS I, GS II, MPA, PNA, SBA, UEA I and WGA). A significant difference was seen between the intensity of staining of normal squamous epithelium and CIN with all lectins except WGA. The alteration in GS II-binding pattern and intensity was significantly related to grade of CIN. No correlation was found between lectin binding and the presence of koilocytes in squamous epithelium. Cases of invasive squamous carcinoma showed a heterogeneous lectin-binding pattern and no significant association was found between lectin binding and tumour differentiation of patient survival. These results indicate that neoplasia in cervical squamous epithelium is associated with alterations in terminal alpha-Man residues, alpha- and beta-GalNAc residues, alpha- and beta-GlcNAc residues, alpha- and beta-Gal residues, and alpha-Fuc-containing residues, present in the outer parts of both N-linked and O-linked glycoconjugates. The implications of these findings are discussed.
ISSN:0018-2214
1573-6865
DOI:10.1007/BF01798495