Neoglycoprotein binding to colorectal tumour cells: comparison between primary and secondary lesions

Virchows Arch A Pathol Anat Histopathol. 1991;419(3):217-22. doi: 10.1007/BF01626351.

Abstract

Biotinylated neoglycoproteins are useful to determine the expression of sugar receptors (lectins) histochemically in routinely processed tissue sections. Assessment of the presence of distinct receptor classes with specificity to beta-galactosides and to alpha- or beta-N-acetylgalactosamine, selected on the basis of their potential relevance for recognition processes within the metastatic cascade in murine model systems, was performed for a common human tumour type, colorectal cancer. The four different types of neoglycoproteins, derived from covalent attachment of commercially available derivatives of beta-N-acetylgalactosamine, differed only quantitatively in their capacity to detect specific binding on cultured cells and tissue sections, thus posing no major restriction on the choice of synthetic process for histochemical efficiency of the product. Glycocytological application revealed specific probe binding and a regulation of level of receptor expression for a human colon carcinoma cell line primarily for N-acetylgalactosamine-specific receptors upon retinoic acid-induced differentiation. Monitoring of sections of the 12 cases of primary and secondary colorectal lesions invariably disclosed the presence of the respective receptors, the extent of cell labelling in primary tumours and metastases being similar. Establishment of metastases, even in different target organs, is apparently not followed by a major phenotypic variation in this feature.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylgalactosamine / metabolism
  • Adenocarcinoma / metabolism*
  • Biotin
  • Cell Differentiation / drug effects
  • Colonic Neoplasms / metabolism*
  • Glycoproteins / chemical synthesis
  • Glycoproteins / metabolism*
  • Histocytochemistry
  • Humans
  • Neoplasm Metastasis*
  • Platelet Glycoprotein GPIb-IX Complex*
  • Platelet Membrane Glycoproteins*
  • Receptors, Immunologic / metabolism
  • Tretinoin / pharmacology
  • Tumor Cells, Cultured

Substances

  • Glycoproteins
  • Platelet Glycoprotein GPIb-IX Complex
  • Platelet Membrane Glycoproteins
  • Receptors, Immunologic
  • glycoprotein receptor GPIb-IX
  • Tretinoin
  • Biotin
  • Acetylgalactosamine