Open AccessAN ALTERED LECTIN BINDING TO MUCUS GLYCOPROTEIN IN GOBLET CELLS OF HUMAN TRACHEOBRONCHIAL EPITHELIUM AMONG FORMER MUSTARD‐GAS WORKERS
Author(s) -
Inai Kouki,
Kou Eihaku,
Nambu Shigeru,
Tokuoka Shoji
Publication year - 1987
Publication title -
acta patholigica japonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
ISSN - 0001-6632
DOI - 10.1111/j.1440-1827.1987.tb00388.x
Subject(s) - mucus , lectin , epithelium , glycoprotein , respiratory epithelium , pathology , mucin , biology , immunology , chemistry , medicine , microbiology and biotechnology , ecology
Lectins, which are well known to have an ability to bind with specific carbohydrate residues of glycoprotein, have been used to examine cellular changes associated with malignant transformation. For the analysis of mucus glycoprotein of goblet cells in the tracheobronchial epithelium, 192 paraffin‐embedded sections from 54 autopsy cases including the cases with a history of mustard‐gas (MG) exposure were stained with seven plant lectins using PAP method. PNA binding with no neuraminidase treatment as well as BSA‐1 binding was observed most frequently in MG‐exposed lung cancer cases. The proportion of cases positive for SBA binding in MG‐exposed and/or lung cancer cases had a statistical difference from non‐MG‐exposed non‐lung cancer cases. These observations may indicate a large heterogeneity in oligosaccharide chains of mucus glycoprotein and suggest its incomplete or abnormal synthesis, which is most likely to be due to previous exposure to carcinogen, such as MG. ACTA PATHOL. JPN. 37:537–548, 1987.