Molecular Mechanisms of Complex Carbohydrate Recognition at the Cell Surface

  1. W.I. Weis,
  2. M.S. Quesenberry*,,
  3. M.E. Taylor*,§,
  4. K. Bezouška*,††,
  5. W.A. Hendrickson, and
  6. K. Drickamer*
  1. *Department of Biochemistry and Molecular Biophysics and Howard Hughes Medical Institute, Columbia University, New York, New York 10032

This extract was created in the absence of an abstract.

Excerpt

Complex carbohydrates conjugated to lipids and proteins at cell surfaces, in the extracellular matrix, and in extracellular fluids can function in two fundamentally different ways. They can influence the intrinsic properties of the lipid or protein to which they are attached, or they can serve as recognition markers. In the latter case, lectins, or carbohydrate-recognition proteins, are generally required to mediate the biological activity of the saccharide. Endogenous animal lectins have been identified with increasing frequency. More than 50 of these have been characterized at the level of primary structure. These sequences fall into a remarkably small number of groups (Drickamer 1992). The largest and most diverse of these groups consists of Ca++-dependent, or C-type, lectins (Drickamer 1988).

C-type animal lectins mediate several different types of interactions at the cell surface. Many of these proteins interact with endogenous saccharides. The asialoglycoprotein receptor is a prototype cell-surface C-type lectin that binds...

  • Present address: Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 20212

  • §

    § Present address: Institute of Glycobiology, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3UK, United Kingdom

  • ††

    †† Present address: Institute of Biotechnology, Charles University, Hlavova 8/2030, CS-128 40 Praha 2, Czechcslovakia.

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