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Departments of
*
Cell Biology,
Pharmacology, and
Protein Expression, Human Genome Sciences, Inc., Rockville, MD 20850; and
§
Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892
The receptor specificity and signal transduction pathway has been
identified and characterized for a truncated form of myeloid progenitor
inhibitory factor-1 (MPIF-124–99). MPIF-1 binds
specifically to sites, in particular CCR1, shared with macrophage
inflammatory protein-1
(MIP-1) on the surface of human monocytes
and dendritic cells, as inferred by its ability to compete for
[125I]MIP-1, but not for [125I]MIP-1ß
or [125I]monocyte chemotactic protein-1(MCP-1) binding to
intact cells. Based on calcium flux, MPIF-1 is an agonist on
CCR1-transfected HEK-293 cells, monocytes, and dendritic cells, but not
on CCR5-, CCR8-, or CX3CR1-transfected cells. The
inhibitory effect of guanosine
5'-O-(3-thio-triphosphate) (GTP-
S) or pertussis toxin
pretreatment on MPIF-1 binding and calcium mobilization, respectively,
indicates the involvement of G proteins in the interaction of MPIF-1
and its receptor(s). The increase in intracellular free calcium
concentration following MPIF-1 treatment is mainly due to the influx of
calcium from an extracellular pool. However, a portion of the
intracellular free calcium concentration is derived from a
phospholipase C inhibitor-sensitive intracellular pool. MPIF-1 induces
a rapid dose-dependent release of [3H]arachidonic acid
from monocytes that is dependent on extracellular calcium and is
blocked by phospholipase A2 (PLA2) inhibitors.
Furthermore, PLA2 activation is shown to be necessary for
filamentous actin formation in monocytes. Thus, the MPIF-1 signal
transduction pathway appears to include binding to CCR1; transduction
by G proteins; effector function by phospholipase C, protein kinase C,
calcium flux, and PLA2; and cytoskeletal
remodeling.
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