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Vitronectin (S protein) augments the functional activity of monocyte
receptors for IgG and complement C3b
CJ Parker, RN Frame and MR Elstad
Department of Medicine, University of Utah School of Medicine, Salt Lake
City.
An arginine-glycine-aspartic acid sequence (RGD in the single letter code
for amino acids) is present in the cell attachment site of both vitronectin
and fibronectin. Inasmuch as fibronectin and synthetic peptides containing
RGD enhance ingestion of opsonized particles by monocytes, we investigated
the effects of vitronectin on phagocytosis by monocytes of sheep
erythrocytes bearing IgG (EA) or complement C3b (EC3b). Peripheral blood
monocytes were isolated by countercurrent elutriation and allowed to adhere
to slides that had been coated with either vitronectin or fibronectin.
Next, EA or EC3b were incubated with the adherent monocytes, and
phagocytosis was subsequently quantified. Vitronectin caused the same dose
dependent increase in phagocytosis as fibronectin. The augmentation of
phagocytosis of EA induced by vitronectin could be inhibited by the F(ab')2
fragments of anti- vitronectin IgG but not by preimmune F(ab')2. The
maximum phagocytosis of EA induced by vitronectin could not be enhanced by
the addition of fibronectin, suggesting that vitronectin and fibronectin
act on the same population of monocytes and that the two proteins stimulate
the same mechanism through which the enhanced phagocytosis is mediated.
Fibronectin and vitronectin caused a tenfold increase in the attachment of
EC3b to monocytes, but phagocytosis was augmented minimally. These studies
demonstrate that vitronectin modulates interactions between monocytes and
opsonized particles.
Volume 71,
Issue 1,
pp. 86-93,
01/01/1988
Copyright © 1988 by The American Society of Hematology
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