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Induction of phagocytosis by a protein tyrosine kinase
ZK Indik, JG Park, XQ Pan and AD Schreiber
Department of Medicine, University of Pennsylvania School of Medicine,
Philadelphia.
The transmission of extracellular signals to cellular targets by many
noncatalytic surface receptors is dependent on interaction between
cytoplasmic protein tyrosine kinases (PTKs) and tyrosine-containing
sequences in the cytoplasmic domain of the receptor or an associated
subunit. Isoforms of each of the three classes of the noncatalytic Fc gamma
receptors, Fc gamma RI, Fc gamma RII, and Fc gamma RIII, are able to
transmit a phagocytic signal in transfected COS-1 cells. Both Fc gamma RI
and Fc gamma RIIIA require the gamma subunit for this signaling event. The
protein tyrosine kinase Syk dramatically enhances phagocytosis mediated by
both these receptors and increases the number of cells able to mediate
phagocytosis. Two gamma chain cytoplasmic YXXL sequences are required for
this effect. The action of Syk is less pronounced on the phagocytic Fc
gamma RII receptor, Fc gamma RIIA, which does not require the gamma chain
for phagocytosis. However, Syk allows phagocytosis by the nonphagocytic Fc
gamma RII receptor Fc gamma RIIB2, which contains only a single YXXL
sequence, when an additional tyrosine-containing sequence, YMTL, is
introduced. These studies indicate that the efficiency of phagocytosis is
markedly enhanced by the presence of a specific protein tyrosine kinase.
Volume 85,
Issue 5,
pp. 1175-1180,
03/01/1995
Copyright © 1995 by The American Society of Hematology

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