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A dominant negative receptor for specific secreted semaphorins is generated by deleting an extracellular domain from neuropilin-1.

Abstract
Neuropilins have recently been characterized as receptors for secreted semaphorins. Here, we report the generation of a dominant negative form of neuropilin-1 by the deletion of one of its extracellular domains. Expression of this variant in cultured primary sympathetic neurons blocks the paralysis of growth cone motility normally induced by SEMA-3A (collapsin-1, semaphorin III, semaphorin D) and SEMA-3C (collapsin-3, semaphorin E) but not that induced by SEMA-3F (semaphorin IV). A truncated form of neuropilin-1 that is missing its cytoplasmic domain fails to act as a dominant negative receptor component. These results suggest that neuropilin-1 is a necessary component of receptor complexes for some, but not all, secreted semaphorin family members. Overexpression of dominant negative neuropilins should provide a powerful new method of blocking the functions of secreted semaphorins.
AuthorsM J Renzi, L Feiner, A M Koppel, J A Raper
JournalThe Journal of neuroscience : the official journal of the Society for Neuroscience (J Neurosci) Vol. 19 Issue 18 Pg. 7870-80 (Sep 15 1999) ISSN: 1529-2401 [Electronic] United States
PMID10479689 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Carrier Proteins
  • Glycoproteins
  • Nerve Growth Factors
  • Nerve Tissue Proteins
  • Receptors, Cell Surface
  • Recombinant Proteins
  • SEMA3A protein, human
  • Semaphorin-3A
  • semaphorin IV
  • Neuropilin-1
Topics
  • Animals
  • COS Cells
  • Carrier Proteins (metabolism)
  • Cells, Cultured
  • Chick Embryo
  • Chickens
  • Ganglia, Sympathetic (physiology)
  • Glycoproteins (metabolism)
  • Humans
  • Models, Molecular
  • Nerve Growth Factors (metabolism)
  • Nerve Tissue Proteins (chemistry, genetics, metabolism, physiology)
  • Neurons (physiology)
  • Neuropilin-1
  • Polymerase Chain Reaction
  • Protein Conformation
  • Receptors, Cell Surface (genetics, physiology)
  • Recombinant Proteins (chemistry, metabolism)
  • Semaphorin-3A
  • Sequence Deletion
  • Transfection

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