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J. Biol. Chem., Vol. 263, Issue 15, 7007-7015, May, 1988
DC Altieri and TS Edgington
Initiation of the coagulation protease cascade as it assembles on cell
surfaces requires limited proteolytic activation of the zymogen factor X.
Not previously suspected to be the ligand of an organizing receptor on cell
surfaces, we now describe that factor X specifically associates with cells
of monocyte lineage and we identify the high affinity receptor for this
zymogen. Following stimulation with ADP (10 microM), or with the ionophore
ionomycin (1 microM), isolated human monocytes bind 125I-factor X in a
saturable fashion with a dissociation constant (Kd) of 21.8-44.9 nM.
Equilibrium binding analyses indicate that the reaction is optimal at room
temperature, requires Ca2+ ions, and saturates at 128,500 +/- 21,300
molecules of 125I-factor X specifically associated with the cell surface.
Molar excess of unlabeled factor X inhibits and reverses the binding,
whereas the homologous gamma- carboxylated coagulation proteins factors II,
VII, IX, IXa, and Xa are without effect. Similarly, chelation of divalent
ions immediately dissociates bound 125I-factor X. The monoblast cell line U
937 and the monocytic cell line THP-1 when stimulated with ADP or
ionomycin, bind 125I-factor X with characteristics similar to monocytes.
Receptor identity was explored using antibodies to the leukocyte adhesive
receptors Mac-1, LFA-1, and p150.95. Monoclonal antibodies specific for the
alpha subunit of Mac-1 (M 1/70, LM 2/1) or for the common beta subunit (TS
1/18, 60.3) bound equally to resting and ADP- or ionomycin- stimulated
cells and also completely blocked the binding of 125I-factor X to
stimulated monocytes, U 937, or THP-1 cells. To distinguish between
modulatory effects of the monoclonal antibodies and direct spatial
hindrance binding of 125I-factor X to Mac-1 was analyzed directly. OKM10
anti-alpha subunit of Mac-1 monoclonal antibody immunoprecipitated
125I-factor X chemically cross-linked to its receptor on stimulated cells.
In addition, the complement protein fragment C3bi, which is a recognized
ligand for Mac-1, competitively inhibited the association of 125I-factor X.
These findings indicate that human blood monocytes and less differentiated
cells of this lineage possess an inducible receptor specific for factor X;
and also support the conclusion that the heterodimeric leukocyte adhesive
receptor Mac-1 functions as the specific receptor structure. We suggest
that the novel properties of this receptor may be of importance in the
organization and regulation of certain coagulation protease cascades on the
monocyte surface.
The saturable high affinity association of factor X to ADP-stimulated monocytes defines a novel function of the Mac-1 receptor
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.
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