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© The Rockefeller University Press, 0021-9525/2000//1283 $5.00
The Journal of Cell Biology, Volume 148, Number 6, , 2000 1283-1294

Original Article

Determination of Cell Adhesion Sites of Neuropilin-1



Masayuki Shimizua,b, Yasunori Murakamia,b, Fumikazu Sutoa, and Hajime Fujisawaa,b

a Group of Developmental Neurobiology, Division of Biological Science, Nagoya University Graduate School of Science, Chikusa-ku, Nagoya 464-8602
b "Research Area" CREST, Japan Science and Technology Corporation, Minato-ku, Tokyo 105-001, Japan
Group of Developmental Neurobiology, Division of Biological Science, Nagoya University Graduate School of Science, Chikusa-ku, Nagoya 464-8602, Japan.+81-52-789-2979+81-52-789-2978

fujisawa{at}bio.nagoya-u.ac.jp

Neuropilin-1 is a type 1 membrane protein with three distinct functions. First, it can mediate cell adhesion via a heterophilic molecular interaction. Second, in neuronal cells, neuropilin-1 binds the class 3 semaphorins, which are neuronal chemorepellents, and plays a role in the directional guidance of axons. Neuropilin-1 is expected to form complexes with the plexinA subfamily members and mediate the semaphorin-elicited inhibitory signals into neurons. Third, in endothelial cells, neuropilin-1 binds a potent endothelial cell mitogen, vascular endothelial growth factor (VEGF)165, and regulates vessel formation. Though the binding sites in neuropilin-1 for the class 3 semaphorins and VEGF165 have been analyzed, the sites involved in cell adhesion activity of the molecule have not been identified. In this study, we produced a variety of mutant neuropilin-1s and tested their cell adhesion activity. We showed that the b1 and b2 domains within the extracellular segment of neuropilin-1 were required for the cell adhesion activity, and peptides with an 18–amino acid stretch in the b1 and b2 domains were sufficient to induce the cell adhesion activity. In addition, we demonstrated that the cell adhesion ligands for neuropilin-1 were proteins and distributed in embryonic mesenchymal cells but distinct from the class 3 semaphorins, VEGF, or plexins.

Key Words: neuropilin-1 • cell adhesion • cell aggregation • semaphorins • mutant protein

© 2000 The Rockefeller University Press

Abbreviations used in this paper: aa, amino acids; GST, glutathione-S-transferase; VEGF, vascular endothelial growth factor.


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