Aminopeptidase P--a cell-surface antigen of endothelial and lymphoid cells: catalytic and immuno-histotopical evidences.
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.
Institute of Physiological Chemistry, Medical Faculty, Martin-Luther-University Halle, Germany.
J
J
Lasch
S
S
Moschner
H
H
Sann
S
S
Zellmer
R
R
Koelsch
D000626:Aminopeptidases / Q000737:chemistry*; D000818:Animals; D000954:Antigens, Surface / Q000737:chemistry; D004727:Endothelium / Q000201:enzymology* / Q000276:immunology; D005455:Fluorescent Antibody Technique; D007525:Isoelectric Focusing; D008214:Lymphocytes / Q000201:enzymology* / Q000276:immunology; D011817:Rabbits
D000954:Antigens, Surface; D000626:Aminopeptidases; C022750:X-Pro aminopeptidase