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Blood, 15 February 2001, Vol. 97, No. 4, pp. 1070-1078
PHAGOCYTES
Regulation of plasminogen binding to neutrophils
Thomas Herren,
Timothy A. Burke,
Merce Jardi,
Jordi Felez, and
Edward F. Plow
From the Joseph J. Jacobs Center for Thrombosis and
Vascular Biology, Department of Molecular Cardiology, The Cleveland
Clinic Foundation, Cleveland, OH, and the Institut Recerca
Oncològica, Departamento Receptores Celulares, Barcelona, Spain.
Plasminogen plays an integral role in the inflammatory response,
and this participation is likely to depend on its interaction with cell
surfaces. It has previously been reported that isolation of
human neutrophils from blood leads to a spontaneous increase in their
plasminogen-binding capacity, and the basis for this up-regulation has
been explored as a model for mechanisms for modulation of plasminogen
receptor expression. Freshly isolated human peripheral blood
neutrophils exhibited relatively low plasminogen binding, but when
cultured for 20 hours, they increased this capacity dramatically, up to
50-fold. This increase was abolished by soybean trypsin inhibitor and
was susceptible to carboxypeptidase B treatment, implicating
proteolysis and exposure of carboxy-terminal lysines in the enhanced
interaction. In support of this hypothesis, treatment of neutrophils
with elastase, cathepsin G, or plasmin increased their plasminogen
binding, and specific inhibitors of elastase and cathepsin G suppressed
the up-regulation that occurred during neutrophil culture. When
neutrophils were stimulated with phorbol ester, their plasminogen
binding increased rapidly, but this increase was insensitive to the
protease inhibitors. These results indicate that plasminogen binding to
neutrophils can be up-regulated by 2 distinct pathways. A major pathway
with the propensity to markedly up-regulate plasminogen binding depends
upon the proteolytic remodeling of the cell surface. In response to
thioglycollate, neutrophils recruited into the peritoneum of mice were
shown to bind more plasminogen than those in peripheral blood,
suggesting that modulation of plasminogen binding by these or other
pathways may also occur in vivo.
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