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Departments of
*
Pediatric Research and
Pediatrics, The National Hospital, Oslo, Norway; and
Department of Infectious Diseases, Washington University School of Medicine, St. Louis, MO 63110
Activation-induced death of T cells regulates immune responses and
is considered to involve apoptosis induced by ligation of Fas and TNF
receptors. The role of other receptors in signaling T cell death is
less clear. In this study we demonstrate that activation of specific
epitopes on the Ig variable domain of CD47 rapidly induces apoptosis of
T cells. A new mAb, Ad22, to this site induces apoptosis of Jurkat
cells and CD3
-stimulated PBMC, as determined by morphological
changes, phosphatidylserine exposure on the cell surface, uptake of
propidium iodide, and true counts by flow cytometry. In contrast,
apoptosis was not observed following culture with anti-CD47 mAbs
2D3 or B6H12 directed to a distant or closely adjacent region,
respectively. CD47-mediated cell death was independent of CD3, CD4,
CD45, or p56lck involvement as demonstrated by
studies with variant Jurkat cell lines deficient in these signaling
pathways. However, coligation of CD3 and CD47 enhanced
phosphatidylserine externalization on Jurkat cells with functional CD3.
Furthermore, normal T cells required preactivation to respond with
CD47-induced apoptosis. CD47-mediated cell death appeared to proceed
independent of Fas or TNF receptor signaling and did not involve
characteristic DNA fragmentation or requirement for IL-1ß-converting
enzyme-like proteases or CPP32. Taken together, our data demonstrate
that under appropriate conditions, CD47 activation results in very
rapid T cell death, apparently mediated by a novel apoptotic pathway.
Thus, CD47 may be critically involved in controlling the fate of
activated T cells.
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