Glycoconjugates such as glycoproteins and glycolipids play important roles in cell–cell interaction events including development differentiation m- phogenesis fertilization inflammation and metastasis. A number of reports have documented the association of unique oligosaccharide sequences to p- tein targeting and folding and in mechanisms of infection inflammation and immunity. For glycoproteins these glycan appendages are the result of extensive co- or post-translational modifications of the nascent proteins in the endoplasmic reticulum and in the Golgi apparatus. Although nucleic acids and proteins are copied from a template in a repeated series of identical steps using the same enzymes complex carbohydrates are formed by the sequential actions of cellular glycosyltransferases that specifically recognize unique s- strates. The molecular biology of these transferases and other carbohydra- modifying enzymes is providing important insights on oligosaccharide recognition events. While it is acknowledged that the definition of the protein complement of cells and tissues (the so-called proteome) remains an enormous task in this postgenomic era the characterization of all glycans produced by individual organisms (referred to as the glycome) presents an equally imp- tant challenge. This task is further complicated by the fact that oligosacc- rides cannot presently be cloned. These complex carbohydrates exist in a staggering diversity of structures linkages and branching thus providing an exquisite molecular repertoire for cellular interactions.
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