LAR tyrosine phosphatase receptor: a developmental isoform is present in neurites and growth cones and its expression is regional- and cell-specific

Mol Cell Neurosci. 1998 Apr;10(5-6):271-86. doi: 10.1006/mcne.1998.0663.

Abstract

Transgenic mice and Drosophila mutant studies demonstrate that the leukocyte common antigen-related (LAR) protein tyrosine phosphatase (PTPase) receptor is required for formation of neural networks. We assessed the hypothesis that alternative splicing of the LAR extracellular region contributes to this function by establishing temporospatial expression patterns of LAR isoforms containing an alternatively spliced extracellular nine amino acid segment (LAR alternatively spliced element-c; LASE-c). LASE-c was present in multiple alternatively spliced and truncated LAR transcripts. In contrast to LAR isoforms without LASE-c, levels of LAR transcripts and protein isoforms containing LASE-c were primarily present during development, suggesting a mechanism for developmental regulation of LAR function. In situ analysis demonstrated increasingly region- and cell-specific expression of LASE-c during maturation. Immunostaining revealed LASE-c-containing LAR protein along neurites and in growth cones. The discovery of highly regulated, temporospatial extracellular domain alternative splicing of LAR-type PTPase receptors points to a novel mechanism by which these receptors might influence network formation.

Publication types

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

MeSH terms

  • Animals
  • Animals, Newborn / genetics
  • Animals, Newborn / growth & development*
  • Brain Mapping
  • Cells, Cultured
  • Down-Regulation / genetics
  • Female
  • Gene Expression Regulation, Developmental*
  • Humans
  • Isoenzymes / biosynthesis*
  • Isoenzymes / genetics
  • Nerve Tissue Proteins*
  • Neurites / metabolism
  • Neurites / physiology*
  • Neurons / metabolism
  • Neurons / physiology
  • Organ Specificity / genetics
  • PC12 Cells
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatases / biosynthesis*
  • Protein Tyrosine Phosphatases / genetics
  • RNA, Messenger / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2
  • Receptors, Cell Surface / biosynthesis*
  • Receptors, Cell Surface / genetics
  • Transcription, Genetic

Substances

  • Isoenzymes
  • Nerve Tissue Proteins
  • RNA, Messenger
  • Receptors, Cell Surface
  • PTPRF protein, human
  • Protein Tyrosine Phosphatases
  • Ptprf protein, rat
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2