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CD10 (CALLA)/neutral endopeptidase 24.11 modulates inflammatory peptide-
induced changes in neutrophil morphology, migration, and adhesion proteins
and is itself regulated by neutrophil activation
MA Shipp, GB Stefano, SN Switzer, JD Griffin and EL Reinherz
Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA
02115.
The common acute lymphoblastic leukemia antigen (CALLA, CD10), which is
expressed on early lymphoid progenitors and neutrophils, is the zinc
metalloprotease, neutral endopeptidase 24.11 (NEP, "enkephalinase"). The
CD10 cell surface enzyme is known to hydrolyze a variety of biologically
active peptides including met-enkephalin, formyl-met-leu- phe (f-MLP), and
substance P. These three CD10/NEP substrates induce the migration and
aggregation of neutrophils, suggesting that each of the peptides can
function as a mediator of neutrophil inflammatory responses. Recently,
inhibition of CD10/NEP was found to reduce the concentration of
metenkephalin needed to activate human and invertebrate granulocytes by
several orders of magnitude. Herein we show that f-MLP and substance P
induce rapid changes in neutrophil morphology, migration, and adhesion
molecule expression, including upregulation of Mo1 (CD11b/CD18) and
shedding of LAM-1 (also known as LECAM-1, Leu8, or TQ-1, the human
homologue of murine gp100MEL14). Importantly, these coordinated changes are
potentiated by inhibition of cell surface CD10/NEP enzymatic activity.
Neutrophil cell surface CD10/NEP enzymatic activity is also shown to be
regulated by the activation state of the cell during the time period in
which the enzyme has its most pronounced effects. These results suggest
that in neutrophils, CD10/NEP functions to control responsiveness to
multiple inflammatory peptides.
Volume 78,
Issue 7,
pp. 1834-1841,
10/01/1991
Copyright © 1991 by The American Society of Hematology
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