Animal Lectins: from Initial Description to Elaborated Structural and Functional Classification

  • Herbert Kaltner
  • Hans-J. Gabius
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 491)


The genetic code connects the two biochemical dimensions of nucleic acids and proteins. Theoretical calculations on coding capacity reveal that oligo saccharides as hardware surpass peptides by more than seven orders of magnitude based on hexamer synthesis. Thus, the sugar code establishes the third dimension of biological information transfer. Using carbohy-drate-binding proteins (lectins, enzymes and antibodies) the information content of such epi-topes is decoded. Currently, five families of animallectins are defined in structural terms, i.e. the C-type, I-type and P-type groups, the galectins and the pentraxins. They are involved in intra-and intercellular glycan routing using oligo saccharides as postal-code equivalents and acting as defense molecules homing in on foreign or aberrant glycosignatures, as crosslinking agent in biosignaling and as coordinator of transient or firm cell-ceIVcell-matrix contacts. By delineating the driving forces toward complex formation, knowledge about the causes for specificity can be turned into design of custom-made high-affinity ligands for clinical applica-tion, e.g. in anti-adhesion therapy, drug targeting or diagnostic histopathology.


Leukocyte Adhesion Deficiency Carbohydrate Ligand Endogenous Lectin Animal Lectin Leukocyte Adhesion Deficiency Type 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Herbert Kaltner
    • 1
  • Hans-J. Gabius
    • 1
  1. 1.Institute of Physiological ChemistryFaculty of Veterinary Medicine, Ludwig-Maximilians- UniversityMünchenGermany

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