Localizing PRL-2 expression and determining the effects of dietary Mg(2+) on expression levels

Histochem Cell Biol. 2016 Jul;146(1):99-111. doi: 10.1007/s00418-016-1427-6. Epub 2016 Mar 25.

Abstract

The phosphatase of regenerating liver (PRL) is a group of protein tyrosine phosphatases that play a key role in cancer progression and metastasis. We previously showed that PRL-2 modulates intracellular Mg(2+) levels and sustains cancer phenotypes by binding to the Mg(2+) transporter CNNM3. However, the physiological functions of PRL-2 in animals remain largely unknown. To better understand which cell types are associated with PRL-2 function, we characterized its expression in mouse tissues using a PRL-2 β-galactosidase reporter mouse model. Our results demonstrated that PRL-2 was ubiquitously expressed, with the highest expression levels observed in the hippocampal pyramidal neurons, ependymal cells, cone and rod photoreceptor cells, endocardium, vascular and bronchial smooth muscle, and collecting ducts in the kidney. On the other hand, PRL-2 expression was undetectable or very low in the parenchymal cells of the liver and pancreas. Our results also indicated that PRL-2 is involved in cell-type-specific Mg(2+) homeostasis and that PRL-2 expression is potentially inversely regulated by dietary Mg(2+) levels.

Keywords: CNNM; Magnesium homeostasis; PRL-2; PTP4A2; Tyrosine phosphatase.

MeSH terms

  • Animals
  • Dietary Supplements*
  • Female
  • Homeostasis / drug effects
  • Immediate-Early Proteins / analysis*
  • Immediate-Early Proteins / biosynthesis*
  • Immediate-Early Proteins / metabolism
  • Magnesium / administration & dosage
  • Magnesium / metabolism
  • Magnesium / pharmacology*
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Protein Tyrosine Phosphatases / analysis*
  • Protein Tyrosine Phosphatases / biosynthesis*
  • Protein Tyrosine Phosphatases / metabolism

Substances

  • Immediate-Early Proteins
  • Protein Tyrosine Phosphatases
  • Ptp4a2 protein, mouse
  • Magnesium