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.
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Authors | M J Renzi, L Feiner, A M Koppel, J A Raper |
Journal | The 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 |
PMID | 10479689
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
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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
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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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