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(Received for publication, July 17, 1995) CD16, the low affinity Fc
Volume 270,
Number 43,
Issue of October 27, 1995 pp. 25762-25770
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Receptor III) Isoforms
PHAGOCYTIC SIGNALING BY ASSOCIATED AND
SUBUNITS IN
CHINESE HAMSTER OVARY CELLS
receptor III for IgG
(Fc
RIII), exists as a polypeptide-anchored form (Fc
RIIIA or
CD16A) in human natural killer cells and macrophages and as a
glycosylphosphatidylinositol-anchored form (Fc
RIIIB or CD16B) in
neutrophils. CD16A requires association of the
subunit of
Fc
RI or the
subunit of the TCR-CD3 complex for cell surface
expression. The CD16B is polymorphic and the two alleles are termed NA1
and NA2. In this study, CD16A and the two alleles of CD16B have been
expressed in Chinese hamster ovary (CHO) cells and their ligand binding
and phagocytic properties analyzed. The two allelic forms of CD16B
showed a similar affinity toward human IgG1. However, the NA1 allele
showed approximately 2-fold higher affinity for the IgG3 than the NA2
allele. Although all three forms of CD16 efficiently bound rabbit
IgG-coated erythrocytes (EA), only CD16A coexpressed with the
subunit phagocytosed EA. The phagocytosis mediated by CD16A expressed
on CHO cells was independent of divalent cations but dependent on
intact microfilaments. CHO cells expressing CD16A-
and CD16A-
chimeras also phagocytosed EA. The phagocytosis was specifically
inhibited by tyrphostin-23, a tyrosine kinase inhibitor. In summary,
our results demonstrate that glycosylphosphatidylinositol-anchored
CD16B alleles differ from CD16A in their ability to mediate
phagocytosis. Furthermore, since studies with other Fc
Rs have
shown that CHO cells lack the phagocytic pathway mediated by the
cytoplasmic domain of Fc
Rs, the phagocytosis of EA by CHO cells
stably transfected with CD16A and CD16A-subunit chimera provides an
ideal system to dissect the phagocytic signaling pathways mediated by
these Fc
R-associated subunits.
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