Receptor tyrosine phosphatase-delta is a homophilic, neurite-promoting cell adhesion molecular for CNS neurons

Mol Cell Neurosci. 1999 Oct-Nov;14(4-5):370-84. doi: 10.1006/mcne.1999.0789.

Abstract

Appropriate regulation of tyrosine phosphorylation is essential for axon growth and guidance; evidence from invertebrates indicates that receptor-type tyrosine phosphatases (RPTPs) are required for correct axon growth during CNS development. One vertebrate RPTP, PTP-delta, is highly expressed in brain and has a cell adhesion molecule-like extracellular domain (ECD) comprising three immunoglobulin repeats and eight fibronectin type III repeats. Using fluorescent beads (Covaspheres) coated with the PTP-delta ECD, as well as insect cells expressing PTP-delta on their surfaces, we show that PTP-delta is a homophilic cell adhesion molecule. A variety of chick neurons adhere strongly to an Fc fusion protein containing the PTP-delta ECD. Additionally, substrate-bound PTP-delta ECD fusion protein strongly promotes neurite outgrowth from forebrain neurons; this effect is separable from its effect on adhesion. Our results indicate that PTP-delta is a neurite-promoting cell adhesion molecule for CNS neurons.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Baculoviridae / genetics
  • CHO Cells
  • Catalytic Domain
  • Cell Adhesion / physiology
  • Cell Adhesion Molecules, Neuronal / chemistry
  • Cell Adhesion Molecules, Neuronal / genetics
  • Cell Adhesion Molecules, Neuronal / metabolism
  • Chick Embryo
  • Cloning, Molecular
  • Cricetinae
  • Gene Expression Regulation, Developmental
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Molecular Sequence Data
  • Neurites / enzymology*
  • Neurons / cytology*
  • Neurons / enzymology*
  • Neurons / ultrastructure
  • Prosencephalon / cytology
  • Protein Binding / physiology
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / genetics*
  • Protein Tyrosine Phosphatases / metabolism*
  • RNA, Messenger / analysis
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2
  • Recombinant Fusion Proteins / genetics
  • Sequence Homology, Amino Acid
  • Transfection

Substances

  • Cell Adhesion Molecules, Neuronal
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • PTPRD protein, human
  • Protein Tyrosine Phosphatases
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2