Endogenous fibronectin of blood polymorphonuclear leukocytes: stimulus-induced secretion and proteolysis by cell surface-bound elastase

Experimental Cell Research
R SalcedoM Patarroyo

Abstract

In an accompanying study, we described the presence of intact fibronectin, a large adhesive molecule, in the specific granules of blood PMNs. Secretion of fibronectin by blood PMNs is poorly understood, and the fate of this fibronectin is practically unknown. In the present study we demonstrate that nanomolar concentrations of phorbol ester or the chemoattractants fMLP, PAF, and LTB4 induce fibronectin secretion from blood PMNs. Phorbol ester induced secretion of approximately 85% of the total fibronectin content, as well as expression of small amounts on the cell surface of the activated PMNs. Secreted fibronectin was proteolytically cleaved and, after 20 min, four major fragments of 150, 120, 90, and 80 kDa containing a midchain epitope were identified by Western blot analysis. Kinetic studies indicated that fibronectin was rapidly secreted as an intact molecule and that proteolysis started within minutes and proceeded for at least 1 h. If cells were removed after 5 min TPA treatment, no further proteolysis of the secreted fibronectin was observed, indicating participation of cell-bound proteinases. From a cocktail of proteinase inhibitors, PMSF was the most active in suppressing fibronectin proteolysis. Studies with specific...Continue Reading

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