Protein-tyrosine phosphatase H1 controls growth hormone receptor signaling and systemic growth

J Biol Chem. 2007 Nov 30;282(48):35405-15. doi: 10.1074/jbc.M705814200. Epub 2007 Oct 4.

Abstract

Several protein-tyrosine phosphatases (PTPs) have been implicated in the control of growth hormone receptor (GHR) signaling, but none have been shown to affect growth in vivo. We have applied a battery of molecular and cellular approaches to test a family-wide panel of PTPs for interference with GHR signaling. Among the subset of PTPs that showed activity in multiple readouts, we selected PTP-H1/PTPN3 for further in vivo studies and found that mice lacking the PTP-H1 catalytic domain show significantly enhanced growth over their wild type littermates. In addition, PTP-H1 mutant animals had enhanced plasma and liver mRNA expression of insulin-like growth factor 1, as well as increased bone density and mineral content. These observations point to a controlling role for PTP-H1 in modulating GHR signaling and systemic growth through insulin-like growth factor 1 secretion.

MeSH terms

  • Animals
  • Catalytic Domain
  • Cell Proliferation
  • Female
  • Humans
  • Insulin-Like Growth Factor I / metabolism*
  • Liver / metabolism
  • Male
  • Mice
  • Mice, Knockout
  • Models, Biological
  • Mutation
  • Phosphorylation
  • Protein Tyrosine Phosphatase, Non-Receptor Type 3 / chemistry*
  • Protein Tyrosine Phosphatase, Non-Receptor Type 3 / physiology
  • RNA, Messenger / metabolism
  • Receptors, Somatotropin / metabolism*
  • Signal Transduction

Substances

  • RNA, Messenger
  • Receptors, Somatotropin
  • Insulin-Like Growth Factor I
  • Protein Tyrosine Phosphatase, Non-Receptor Type 3