Beyond plant lectin histochemistry: preparation and application of markers to visualize the cellular capacity for protein-carbohydrate recognition.

Oligosaccharides can store biological information. In this respect, their capacity even outmatches that of oligo- and polymeric structures of nucleotides and amino acids. Protein-carbohydrate interactions are thus considered to be involved in the regulation of diverse cellular activities. Over decades, plant lectins have proven valuable for assessing structural aspects of the enormous variety of carbohydrate epitopes and for monitoring spatially and/or temporally restricted patterns of expression. If the presence of these epitopes and the alterations in their occurrence bear physiological relevance, one reasonable possibility is that the visualized saccharides serve as ligands in an operative protein-carbohydrate recognition system. To support the validity of this hypothesis, receptor sites for a sugar compound must be localized. Carrier-immobilized carbohydrates (neoglycoconjugates) are adequate for this purpose. Chemical synthesis gains access to such probes. In the first stage, the presence of binding sites such as lectins in the tissue is ascertained. The next step toward proving the outlined hypothesis is the application of the first localized then purified endogenous receptors as glycohistochemical markers. It is essential to point out that the fine specificities of plant and animal lectins can differ, although they share an identical monosaccharide specificity. Thus, neoglycoconjugates for localizing sugar ligand-binding proteins and endogenous lectins to detect suitable binding partners are promising probes to enhance our knowledge about the capacities of cells to be engaged in protein-carbohydrate recognition in situ.