PTP-MEG2 is activated in polycythemia vera erythroid progenitor cells and is required for growth and expansion of erythroid cells

Blood. 2003 Dec 15;102(13):4354-60. doi: 10.1182/blood-2003-04-1308. Epub 2003 Aug 14.

Abstract

Polycythemia vera (PV) is a human clonal hematologic disorder. Previously we demonstrated that erythroid colony-forming cells (ECFCs) from PV patients contained a hyperactive membrane-associated tyrosine phosphatase. We now show that this phosphatase corresponded to protein tyrosine phosphatase (PTP)-MEG2, an intracellular enzyme with a putative lipid-binding domain. The increased activity of PTP-MEG2 in PV cells is due to its elevated distribution in the membrane fraction. With the development of ECFCs to mature red cells, the protein level of PTP-MEG2 decreased gradually, but membrane-associated PTP-MEG2 was sustained for a longer period of time in PV cells, which correlated with an enhanced colony-forming capability of the cells. Importantly, expression of dominant-negative mutant forms of PTP-MEG2 suppressed in vitro growth and expansion of both normal and PV ECFCs. The data indicate that PTP-MEG2 has an important role in the development of erythroid cells.

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

  • Cell Division
  • Cells, Cultured
  • Colony-Forming Units Assay
  • Enzyme Activation
  • Enzyme Induction
  • Erythroid Precursor Cells / cytology
  • Erythroid Precursor Cells / enzymology*
  • Gene Targeting
  • Genes, Dominant
  • Humans
  • Membrane Proteins / physiology
  • Phosphorylation
  • Polycythemia Vera / enzymology*
  • Polycythemia Vera / pathology
  • Protein Processing, Post-Translational
  • Protein Tyrosine Phosphatases / genetics
  • Protein Tyrosine Phosphatases / physiology*
  • Protein Tyrosine Phosphatases, Non-Receptor
  • Recombinant Fusion Proteins / physiology

Substances

  • Membrane Proteins
  • Recombinant Fusion Proteins
  • PTPN9 protein, human
  • Protein Tyrosine Phosphatases
  • Protein Tyrosine Phosphatases, Non-Receptor