Characterisation of complex carbohydrates in cervical glandular intraepithelial neoplasia and invasive adenocarcinoma.
Using a panel of 11 biotinylated lectins and an avidin-peroxidase detection system on paraffin sections of formalin-fixed material, the range of expression of N-linked glycoprotein backbone structures and glycoprotein terminal structures was established in normal cervical glands. A characteristic pattern of luminal lectin reactivity was noted in areas of glandular tubal metaplasia. A consistent change in the topographic distribution of carbohydrate structures in cervical glandular neoplasia was found. In contrast to cytoplasmic expression in normal glands, 90% of adenocarcinomas, 92% of cases of high-grade cervical glandular intraepithelial neoplasia, and 63% of cases of low-grade cervical glandular intraepithelial neoplasia showed novel linear expression along the lumina of glands. The results indicate molecular as well as morphological similarities between invasive adenocarcinomas and putative preinvasive glandular lesions.
Griffin
N R
NR
Department of Histopathology, University Hospital, Nottingham, England.
Wells
M
M
D000230:Adenocarcinoma / Q000737:chemistry*; D002240:Carbohydrate Sequence; D005260:Female; D006023:Glycoproteins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007124:Immunoenzyme Techniques; D037102:Lectins / Q000378:metabolism; D008679:Metaplasia / Q000378:metabolism; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry*; D002583:Uterine Cervical Neoplasms / Q000737:chemistry*; D002578:Uterine Cervical Dysplasia / Q000737:chemistry*
D006023:Glycoproteins; D037102:Lectins; D009363:Neoplasm Proteins