Aminopeptidase P--a cell-surface antigen of endothelial and lymphoid cells: catalytic and immuno-histotopical evidences

Biol Chem. 1998 Jun;379(6):705-9. doi: 10.1515/bchm.1998.379.6.705.

Abstract

The physiological function of the GPI-anchored ectoenzyme aminopeptidase P (APP) is still elusive. Most researchers suppose that this enzyme inactivates biologically active peptides like bradykinin, neuropeptide tyrosine (NPY) and others (Vanhoof et al., 1995). We demonstrate by immunohistology with a specific antibody raised in rabbits and measurement of enzymatic activity in suspensions and of confluent monolayers on microscopic coverslips ('monolayer kinetics') that APP is a cell surface enzyme (ectoenzyme) of endothelial and lymphoid cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminopeptidases / chemistry*
  • Animals
  • Antigens, Surface / chemistry
  • Endothelium / enzymology*
  • Endothelium / immunology
  • Fluorescent Antibody Technique
  • Isoelectric Focusing
  • Lymphocytes / enzymology*
  • Lymphocytes / immunology
  • Rabbits

Substances

  • Antigens, Surface
  • Aminopeptidases
  • X-Pro aminopeptidase