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

@article{Lasch1998AminopeptidasePC,
  title={Aminopeptidase P--a cell-surface antigen of endothelial and lymphoid cells: catalytic and immuno-histotopical evidences.},
  author={J{\"u}rgen Lasch and S Moschner and Heiner Sann and Sebastian Zellmer and Regine Koelsch},
  journal={Biological chemistry},
  year={1998},
  volume={379 6},
  pages={705-9}
}
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… CONTINUE READING