The expression of receptor tyrosine phosphatases is responsive to sciatic nerve crush

Mol Cell Neurosci. 1998 Oct;12(3):93-104. doi: 10.1006/mcne.1998.0707.

Abstract

Given the importance of phosphotyrosine signaling in growth cone dynamics, we have examined the embryonic and adult expression of receptor-like protein tyrosine phosphatases in sensory neurons and studied their responsiveness to nerve lesions in young adult animals. The phosphatases LAR, PTPsigma, and PTPalpha are expressed in most neurons of E14 and E18 rat embryo dorsal root ganglia, while BEM-1 is expressed in a more restricted subset of these neurons. These phosphatases continue to be expressed in young adult animals, suggesting that they have roles in mature as well as in developing dorsal root ganglia neurons. After an experimental sciatic nerve crush, the expression of the phosphatase genes was significantly and differentially altered in these neurons. PTPsigma mRNA was increased by 50% after 3 days, while LAR and PTPalpha expression dropped by 50 and 20%, respectively. BEM-1 mRNA levels were unaltered. These data show that mRNA levels of specific tyrosine phosphatase genes are highly responsive to nerve damage and may be reset to a new and potentially optimal pattern of expression more conducive for nerve regeneration. We propose that tyrosine phosphatases are not only involved in primary axonogenesis but can also now be implicated in the molecular control of adult nerve repair.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aging / metabolism
  • Animals
  • Fixatives
  • Formaldehyde
  • Ganglia, Spinal / cytology
  • Ganglia, Spinal / embryology
  • Ganglia, Spinal / growth & development
  • Ganglia, Spinal / metabolism
  • Nerve Crush*
  • Neurons / cytology
  • Perfusion
  • Polymers
  • Protein Tyrosine Phosphatases / genetics
  • Protein Tyrosine Phosphatases / metabolism*
  • RNA, Messenger / metabolism
  • Rats
  • Rats, Wistar
  • Sciatic Nerve / physiology*

Substances

  • Fixatives
  • Polymers
  • RNA, Messenger
  • Formaldehyde
  • Protein Tyrosine Phosphatases
  • paraform