Analysis of N-glycan of Growth Factor Receptors

  • Motoko Takahashi


Changes in oligosaccharide structure are associated with many physiological and pathological events. A number of membrane bound receptors for growth factors and cytokines are glycosylated, and oligosaccharide moieties are crucial for the regulation of some of those receptors. Strategies for examining the function of oligosaccharides in glycoproteins in culture cells are somewhat limited. One involves eliminating the oligosaccharide moiety from the target proteins by introducing a mutation in the oligosaccharide binding sites of the protein. The other is, in order to determine the role of each structure, manipulation of the oligosaccharides via the introduction of glycosyltransferases or by using RNAi. The drawback of the latter strategy is that it is difficult to identify the key target protein as the change in glycosyltransferase levels can alter the oligosaccharides in a variety of proteins.


Epidermal Growth Factor Receptor Human Epidermal Growth Factor Receptor Sodium Orthovanadate Epidermal Growth Factor Receptor Tyrosine Kinase Inhibit Epidermal Growth Factor Receptor Tyrosine Kinase 
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 2008

Authors and Affiliations

  • Motoko Takahashi
    • 1
  1. 1.Department of BiochemistrySapporo Medical University School of MedicineSapporoJapan

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