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J. Biol. Chem., Vol. 269, Issue 5, 3159-3166, Feb, 1994
GS Elemer and TS Edgington
Selected agonists convert the leukocyte integrin alpha M beta 2 on
monocytes from a low to a high affinity state competent to bind factor X
and fibrinogen. Conformational changes of alpha M beta 2 re hypothesized to
account for this functional transition. Here we report that cytochalasins
known to interfere with actin filaments induce the alpha M beta 2
functional transition. Upon exposure to cytochalasin B, isolated human
blood monocytes and cells of the monocytic cell line THP- 1 bound
125I-factor X (X) or 125I-fibrinogen (Fg) in a Ca(2+)- dependent, saturable
manner. Monoclonal antibodies (mAbs) to the alpha M subunit and the common
beta 2 subunit of leukocyte integrins inhibited X and Fg binding, whereas
mAbs to the alpha chains of the other leukocyte integrins had no effect.
Anti-alpha M mAb immunoprecipitated 125I-X that had been chemically
cross-linked to its cognate receptor. Specific binding was not associated
with an increased surface density of beta 2 integrins consistent with
conformational remodeling of the receptor. Simultaneous analysis of actin
forms in viable monocytes indicated a dynamic redistribution of cellular
actin. The transient increase in G actin concurrent with an agonist action
such as cytochalasin or ADP was reversed by an increase in F actin
coincident with X/Ca2+ binding. A potential role of actin redistribution in
alpha M beta 2 functional transition is supported by the finding that cells
in which cellular actin is restricted to G rather than F form bound X and
initiated a rapid coagulant response. We propose that a transient
disassembly of actin filaments may relieve constraints on alpha M beta 2
via the cytoplasmic domains, permitting the conformational dynamics
required for recognition of ligands.
Microfilament reorganization is associated with functional activation of alpha M beta 2 on monocytic cells
Department of Immunology, Scripps Research Institute, La Jolla, California 92037.
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