Characterisation of enkephalinase (EC 3.4.24.11) activity on various leukemic cells expressing the common acute lymphocytic leukemia antigen (CALLA).
The deduced amino acid sequences of CALLA, a cell surface marker of human acute lymphocytic leukemia, and human enkephalinase (neutral endopeptidase, EC 3.4.24.11) were recently reported to be almost identical. We show that membranes of CALLA+ cells of the REH lymphoblastic cell line as well as blast cells derived from the blood or bone marrow of patients with acute lymphocytic leukemia display high enkephalinase activity. This activity was abrogated by several enkephalinase inhibitors at concentrations closely similar to those required to inhibit pure human enkephalinase. However, these compounds did not significantly modify the rate of REH cell proliferation in vitro. Hence, the functional role, if any, of the high peptidase activity in lymphoblastic cells remains to be established.
Arock
M
M
Laboratoire d'Hématologie, Faculté de Pharmacie, Paris, France.
Gros
C
C
Devillier
P
P
Guillosson
J J
JJ
Schwartz
J C
JC
D000943:Antigens, Differentiation / Q000032:analysis*; D000951:Antigens, Neoplasm / Q000032:analysis*; D001853:Bone Marrow / Q000201:enzymology; D002455:Cell Division / Q000187:drug effects; D002460:Cell Line / Q000187:drug effects; D002462:Cell Membrane / Q000201:enzymology; D004151:Dipeptides / Q000494:pharmacology; D006020:Glycopeptides / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D015260:Neprilysin / Q000037:antagonists & inhibitors / Q000276:immunology / Q000378:metabolism*; D054198:Precursor Cell Lymphoblastic Leukemia-Lymphoma / Q000201:enzymology* / Q000276:immunology; D015244:Thiorphan / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D000943:Antigens, Differentiation; D000951:Antigens, Neoplasm; D004151:Dipeptides; D006020:Glycopeptides; C042591:kelatorphan; D015244:Thiorphan; D015260:Neprilysin; C008890:phosphoramidon