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Transfected NA1 and NA2 forms of human neutrophil Fc receptor III exhibit
antigenic and structural heterogeneity
PA Ory, MR Clark, AS Talhouk and IM Goldstein
Rosalind Russell Arthritis Research Laboratory, Department of Medicine,
University of California, San Francisco.
Human neutrophils express two polymorphic forms (NA1 and NA2) of Fc
receptor III (FcRIII), which differ structurally and antigenically. We
recently isolated FcRIII cDNAs from NA1NA1 and NA2NA2 homozygotes and
determined that they differ only at five nucleotides, predicting four amino
acid substitutions. To determine whether the cDNAs that we isolated
actually encode proteins that differ structurally and that react
appropriately with anti-NA1 and anti-NA2 antibodies, we transfected Chinese
hamster ovary (CHO) cells with constructs containing either the NA1 FcRIII
cDNA or the NA2 FcRIII cDNA. The receptors on transfected CHO cells were
then compared with the receptors on normal human neutrophils from an NA1NA2
heterozygote. After immunoprecipitation and treatment with N-glycanase,
receptors isolated from surface-labeled CHO cells transfected with the NA1
FcRIII cDNA had an apparent molecular mass of 29 Kd after sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), while the receptors
isolated from CHO cells transfected with the NA2 FcRIII cDNA had an
apparent molecular mass of 33 Kd. Identical 29-Kd and 33-Kd bands were
observed when receptors isolated from surface-labeled neutrophils of an
NA1NA2 heterozygote were treated similarly. Using a cell-free rabbit
reticulocyte lysate system, we translated NA1 FcRIII and NA2 FcRIII RNAs in
vitro and also found differences in the apparent molecular masses of the
two forms of the receptor. Finally, reactivity of transfected CHO cells
with anti-NA monoclonal and alloantibodies confirmed that the cDNAs we
isolated actually encode the NA1 and NA2 forms of neutrophil FcRIII.
Volume 77,
Issue 12,
pp. 2682-2687,
06/15/1991
Copyright © 1991 by The American Society of Hematology
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