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J Biol Chem, Vol. 274, Issue 28, 19919-19924, July 9, 1999
B Require the Cytoplasmic
Domain of the Receptor but Different Downstream Signaling Pathways
From the Laboratory of Molecular Neurobiology, Institute of
Biotechnology, and Department of Biosciences, Division of Biochemistry,
University of Helsinki, P. O. Box 56 (Viikinkaari 5), University of
Helsinki, Helsinki FIN-00014, Finland
Receptor for advanced glycation end products
(RAGE) mediates neurite outgrowth in vitro on
amphoterin-coated substrates. Ligation of RAGE by two other ligands,
advanced glycation end products or amyloid 
-peptide, is suggested to
play a role in cell injury mechanisms involving cellular oxidant stress
and activation of the transcription factor NF-
B. However, the RAGE
signaling pathways in neurite outgrowth and cell injury are largely
unknown. Here we show that transfection of RAGE to neuroblastoma cells
induces extension of filopodia and neurites on amphoterin-coated
substrates. Furthermore, ligation of RAGE in transfected cells enhances
NF-B-dependent transcription. Both the RAGE-mediated
neurite outgrowth and activation of NF-B are blocked by deletion of
the cytoplasmic domain of RAGE. Moreover, dominant negative Rac and
Cdc42 but not dominant negative Ras inhibit the extension of neurites
induced by RAGE-amphoterin interaction. In contrast, the
activation of NF-B is inhibited by dominant negative Ras but not Rac
or Cdc42. These data suggest that distinct signaling pathways are used
by RAGE to induce neurite outgrowth and regulate gene expression
through NF-B.
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