Peanut lectin-binding sites in polyps of the colon and rectum. Adenomas, hyperplastic polyps, and adenomas with in situ carcinoma Academic Article uri icon

Overview

MeSH Major

  • Colonic Neoplasms
  • Intestinal Polyps
  • Lectins
  • Rectal Neoplasms

abstract

  • Peanut lectin (PNA) has a specificity for the disaccharide beta-D-Gal-(1 leads to 3)-D-GalNac which is the purported antigenic determinant for the T blood group antigen (TAg). This TAg is considered the immediate precursor of the MN blood group substance. In normal colonic epithelium, PNA binds to the supranuclear (stalk) portion of epithelial cells. This corresponds to the detection of beta-DGal-(1 leads to 3)-D-GalNac in nascent oligosaccharide chains in the Golgi cisternae prior to addition of terminal sialic acid. Colonic carcinomas bind PNA in the "region" of the glycocalyx or in the apical portion of the cell, which represents incomplete glycoprotein synthesis. Eighty-two percent of tubular adenomas, 80% of villous adenomas, and 91% of adenomas with in situ cancer expressed PNA in a supranuclear distribution, reminiscent of normal colonic epithelium. This stalk distribution was seen in goblet cells. Twenty-five percent of tubular adenomas, 43% of villous adenomas and 60% of adenomas with in situ cancer (adenoma portion) expressed PNA in an apical cytoplasmic and/or glycocalyx pattern among nonmucinous columnar cells. In 80% of the cases, the in situ cancer itself expressed PNA in an apical cytoplasmic and/or glycocalyx pattern. Fetal and most colon cancer cells fail to produce mucin goblets and make incomplete glycoproteins. The cytologic localization of TAg by PNA corresponds to the cells' ability to produce mucin goblets. Most adenomas consist of goblet cells, localize TAg to the stalk, and probably make complete MN glycoprotein as does normal colonic epithelium. However, in adenomas, nonmucinous columnar cells localize TAg to the apical cytoplasm and/or glycocalyx region and represent incomplete blood group glycoprotein synthesis.

publication date

  • December 1983

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 6656197

Additional Document Info

start page

  • 655

end page

  • 61

volume

  • 49

number

  • 6