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Release of elastase from monocytes adherent to a fibronectin-gelatin
surface
DL Xie, R Meyers and GA Homandberg
Department of Biochemistry, Rush-Presbyterian-St Luke's Medical Center,
Chicago, IL 60212-3864.
Fibronectin (Fn) is a circulating and extracellular matrix glycoprotein
that may serve to facilitate phagocytosis because of its ability to bind
many inflammatory ligands and to a monocyte receptor. Fn fragments have
been shown in many systems to have augmented properties over those of
native Fn. We show in this report that although Fn fragments did not cause
elastase release from monocytes in suspension, fragments did cause elastase
release from monocytes that were first bound to Fn- gelatin surfaces. An
amino-terminal 29-Kd and a 140-Kd integrin-binding fragment were
half-maximally active at 100 nmol/L, whereas the Arg-Gly- Asp-Ser
integrin-recognition peptide was half-maximally active at 100 mumol/L.
Fluid-phase Fn was ineffective yet blocked the activity of the Fn
fragments. Complexing of Fn with gelatin or with heparin partially removed
the blocking effect of Fn. Similar results were obtained with U- 937 cells.
Substitution of the Fn-gelatin surface with bovine articular cartilage also
promoted elastase release. Therefore, in conditions in vivo in which
monocytes bind to tissue surface, a high ratio of Fn fragments to native Fn
may upregulate certain monocyte activities such as protease release.
Volume 81,
Issue 1,
pp. 186-192,
01/01/1993
Copyright © 1993 by The American Society of Hematology
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