Expression of a cell adhesion molecule, neuropilin, in the developing chick nervous system

Dev Biol. 1995 Jul;170(1):207-22. doi: 10.1006/dbio.1995.1208.

Abstract

Neuropilin (previously known as the A5 protein) is a membrane protein identified in Xenopus and is presumed to be involved in the target recognition of the optic nerve fibers. We have isolated cDNAs encoding the chick homologue of neuropilin, using the Xenopus neuropilin cDNA as a hybridization probe. The predicted amino acid sequence of chick neuropilin is 75% identical to that of the Xenopus homologue. A cell aggregation assay showed that fibroblasts transfected with the chick neuropilin cDNA acquired cell adhesiveness. This adhesion is mediated by a heterophilic interaction between neuropilin and protease-sensitive molecules on fibroblasts. The expression of chick neuropilin is restricted to certain neuronal circuits and is dynamically regulated during development, as is the Xenopus homologue. However, their expression patterns differed significantly in the visual systems between the two species: In the chick optic tectum, the localization of neuropilin is confined to layers d and e of SGFS, two of the six layers receiving the retinal input; the chick optic nerve fibers do not express neuropilin; in the chick retina, amacrine cells transiently express neuropilin. Cultured neurons of the dorsal root ganglia express chick neuropilin on their neurites including growth cones. These results suggests that neuropilin functions as a cell adhesion molecule during the formation of certain neuronal circuits in vivo.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Blotting, Northern
  • Cell Adhesion
  • Cell Line
  • Chick Embryo
  • Chickens / genetics*
  • DNA, Complementary / genetics
  • Drosophila melanogaster / cytology
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Ganglia, Spinal / embryology
  • Ganglia, Spinal / metabolism
  • Gene Expression Regulation, Developmental*
  • In Situ Hybridization
  • Mice
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Nerve Tissue Proteins / biosynthesis*
  • Nerve Tissue Proteins / genetics
  • Neuropilin-1
  • Optic Nerve / embryology
  • Optic Nerve / metabolism
  • RNA, Messenger / biosynthesis
  • RNA, Messenger / genetics
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Superior Colliculi / embryology
  • Superior Colliculi / metabolism
  • Transfection
  • Xenopus laevis / embryology
  • Xenopus laevis / genetics
  • Xenopus laevis / metabolism

Substances

  • DNA, Complementary
  • Nerve Tissue Proteins
  • RNA, Messenger
  • Neuropilin-1

Associated data

  • GENBANK/D45416