Lectin binding in endometrial adenocarcinoma.
The relative increase in endometrial adenocarcinoma in women has increased the need for more objective criteria in the distinction of hyperplastic and neoplastic endometrium. The authors have used the ability of lectins to detect changes in surface glycoproteins to probe the differences among proliferative endometrium, endometrial adenomatous hyperplasia and adenocarcinomas. Paraffin-embedded sections of tissue obtained by Vakutage endometrial sampling technics were stained with each of 7 FITC lectin conjugates. Thirty-four specimens were examined (7 proliferative, 12 hyperplastic, and 15 adenocarcinomatous). Wheat germ agglutinin binding was detectable in all specimens with a distribution at the cell luminal border of glandular formations irrespective of diagnosis. However, adenocarcinoma cases showed distribution along the lumenal border and the cell periphery with loss of orientation of the lectin binding. Similar alterations and increased binding were noted for Concanavalin A. The WGA binding to sections was specifically inhibitable by oligosaccharides of N-acetyl-glucosamine. The results provide an objective criterion for detection of loss of cell orientation useful in the diagnosis of endometrial adenocarcinoma in tissue fragments.
D000230:Adenocarcinoma / Q000175:diagnosis* / Q000276:immunology; D000918:Antibody Specificity; D001667:Binding, Competitive; D003937:Diagnosis, Differential; D004714:Endometrial Hyperplasia / Q000175:diagnosis*; D005260:Female; D006801:Humans; D037102:Lectins / Q000276:immunology / Q000378:metabolism*; D011485:Protein Binding; D014594:Uterine Neoplasms / Q000175:diagnosis* / Q000276:immunology
D037102:Lectins