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J. Cell Biol.,
Volume 144, Number 4, February 22, 1999 767-775
* Laboratoire Allergie, Centre de recherché Louis-Charles Simard, Pavillon Notre-Dame, Centre Hospitalier Université de
Montréal (CHUM), Montreal, Quebec H2L 4M1, Canada; The vitronectin receptor, Laboratory for Parasitic Diseases, National Institutes of Health,
Bethesda, Maryland 20892; § Immunex Research Development Corporation, Seattle, Washington 98101; and Division of
Infectious Diseases, Washington University, St. Louis, Missouri 63110
v
3 integrin, plays
an important role in tumor cell invasion, angiogenesis,
and phagocytosis of apoptotic cells. CD47, a member of
the multispan transmembrane receptor family, physically and functionally associates with vitronectin receptor (VnR). Although vitronectin (Vn) is not a ligand of
CD47, anti-CD47 and 3 mAbs suppress Vn, but not fibronectin (Fn) binding and function. Here, we show
that anti-CD47, anti-3 mAb and Vn, but not Fn, inhibit sCD23-mediated proinflammatory function
(TNF-, IL-12, and IFN-
release). Surprisingly, anti-CD47 and 3 mAbs do not block sCD23 binding to
v+3+ T cell lines, whereas Vn and an v mAb (clone
AMF7) do inhibit sCD23 binding, suggesting the VnR
complex may be a functional receptor for sCD23.
sCD23 directly binds v+3+/CD47
cell lines, but coexpression of CD47 increases binding. Moreover, sCD23 binds purified v protein and a single human v
chain CHO transfectant. We conclude that the VnR
and its associated CD47 molecule may function as a
novel receptor for sCD23 to mediate its proinflammatory activity and, as such, may be involved in the inflammatory process of the immune response.
;
IFN-
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