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Human low-affinity IgG receptor Fc gamma RIIa (CD32) introduced into mouse
fibroblasts mediates phagocytosis of sensitized erythrocytes
WB Tuijnman, PJ Capel and JG van de Winkel
Department of Immunology, University Hospital Utrecht, The Netherlands.
Multiple isoforms of human (h) Fc gamma RII are currently recognized. We
set up experiments to evaluate the significance of different hFc gamma RII
(CD32) isoforms in the uptake of IgG-coated particles. Therefore, a panel
of stable hFc gamma RII-transfected fibroblasts was constructed to study
phagocytosis. It was observed that over 40% of 3T6 fibroblasts transfected
with hFc gamma RIIa cDNA phagocytose human erythrocytes (E) coated with
mouse (m) IgG1 or mIgG2a (EA). This was in contrast to cells expressing a
tail-minus variant of Fc gamma RII (hFc gamma RIItail-). Fibroblasts
transfected with hFc gamma RIIb1 cDNA infrequently internalized EA. There
was no difference in EA binding by these transfectants; all three clones
formed more than 80% EA-rosettes. Uptake of particles was dependent on the
degree of E sensitization, and was inhibitable by CD32 monoclonal antibody
AT10. Preincubation of cells with cytochalasin D blocked internalization
completely, with no effect on binding. This shows that phagocytosis
underlies the observed E internalization. Immunofluorescence studies using
an anticathepsin D antiserum showed the maturation of phagosomes,
containing antibody- coated E, into lysosomes. In conclusion, our studies
show, for the first time, that fibroblasts possess the basic machinery for
ingestion of erythrocytes, and are capable of phagocytosis only when
equipped with an appropriate receptor. hFc gamma RIIa and, to a lesser
extent hFc gamma RIIb1, are suited for this task, which seems dictated by
the cytoplasmic domain.
Volume 79,
Issue 7,
pp. 1651-1656,
04/01/1992
Copyright © 1992 by The American Society of Hematology
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