Receptor-type protein-tyrosine phosphatase mu is expressed in specific vascular endothelial beds in vivo

Exp Cell Res. 1999 Apr 10;248(1):329-38. doi: 10.1006/excr.1999.4428.

Abstract

We investigated the localization of receptor-type protein-tyrosine phosphatase mu (RPTPmu) in tissues by immunofluorescence. RPTPmu immunoreactivity was found almost exclusively within vascular endothelial cells. RPTPmu was more abundant in the arterial tree than in the venous circulation. This pattern of expression was opposite to that of the von Willebrand factor and demonstrated a lack of difference in expression of VE-cadherin. RPTPmu was undetectable in the endocardium. In agreement with previous work on nonendothelial cell lines, RPTPmu was exclusively at the lateral aspects of endothelial cells in vivo and at cell-cell contacts as well as ex vivo in two- or three-dimensional endothelial cell cultures, and expression levels were upregulated by cell density. RPTPmu was detected in few other cells: bronchial and biliary epithelia and cardiocytes (intercalated discs). Our results identify RPTPmu as a new marker of endothelial cell heterogeneity and suggest a possible role in endothelial-specific functions, involving cell-cell contact.

Publication types

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

MeSH terms

  • Animals
  • Cattle
  • Cells, Cultured
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / enzymology*
  • Humans
  • Protein Tyrosine Phosphatases / biosynthesis*
  • Rats
  • Rats, Wistar
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2
  • Receptor-Like Protein Tyrosine Phosphatases, Class 8
  • Receptors, Opioid, mu
  • Swine

Substances

  • Receptors, Opioid, mu
  • PTPRN protein, human
  • Protein Tyrosine Phosphatases
  • Ptprn protein, rat
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2
  • Receptor-Like Protein Tyrosine Phosphatases, Class 8