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Blood, 1 February 2001, Vol. 97, No. 3, pp. 777-784
PHAGOCYTES
Plasminogen-mediated matrix invasion and degradation by
macrophages is dependent on surface expression of annexin
II
Domenick J. Falcone,
Wolfgang Borth,
K. M. Faisal Khan, and
Katherine A. Hajjar
From the Departments of Pathology, Cell Biology,
Pediatrics, and Medicine, Joan and Sanford I. Weill Medical College of
Cornell University, New York, NY, and the Institute of Immunology,
University of Vienna, Vienna, Austria.
Genetic evidence demonstrates the importance of plasminogen
activation in the migration of macrophages to sites of injury and
inflammation, their removal of necrotic debris, and their clearance of
fibrin. These studies identified the plasminogen binding protein
annexin II on the surface of macrophages and determined its role in
their ability to degrade and migrate through extracellular matrices.
Calcium-dependent binding of annexin II to RAW264.7 macrophages was
shown using flow cytometry and Western blot analysis of EGTA eluates.
Ligand blots demonstrated that annexin II comigrates with one of
several proteins in lysates and membranes derived from RAW264.7
macrophages that bind plasminogen. Preincubation of RAW264.7
macrophages with monoclonal anti-annexin II IgG inhibited (35%) their
binding of 125I-Lys-plasminogen. Likewise, plasmin
binding to human monocyte-derived macrophages and THP-1 monocytes was
inhibited (50% and 35%, respectively) when cells were preincubated
with anti-annexin II IgG. Inhibition of plasminogen binding to annexin
II on RAW264.7 macrophages significantly impaired their ability to
activate plasminogen and degrade
[3H]-glucosamine-labeled extracellular matrices. The
migration of THP-1 monocytes through a porous membrane, in response to
monocyte chemotactic protein-1, was blocked when the membranes were
coated with extracellular matrix. The addition of plasminogen to the monocytes restored their ability to migrate through the matrix-coated membrane. Preincubation of THP-1 monocytes with anti-annexin II IgG
inhibited (60%) their plasminogen-dependent chemotaxis through the
extracellular matrix. These studies identify annexin II as a
plasminogen binding site on macrophages and indicate an important role
for annexin II in their invasive and degradative phenotype.
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