Abstract:
:The high affinity receptor that binds the Fc domain of immunoglobulin G (IgG) subclasses 1 and 3 (Fc gamma RI) mediates important immune defense functions by inducing cell surface changes on human leukocytes. In this article, we document direct high affinity binding of Fc gamma RI to the actin filament cross-linking protein, actin-binding protein (ABP). In the absence of IgG, all Fc gamma RI molecules in undifferentiated cells of myeloid line U937 bound to ABP over a 9-fold range of Fc gamma RI expression induced by human IFN-gamma. Binding of IgG to U937 cells constitutively expressing Fc gamma RI or to COS cells genetically transfected to express Fc gamma RI rapidly decreased the avidity of Fc gamma RI for ABP. This finding suggests the existence of a pathway communicating a signal between a functional IgG receptor and intracellular components involved in the effector responses to Fc gamma RI-ligand interaction.
journal_name
Celljournal_title
Cellauthors
Ohta Y,Stossel TP,Hartwig JHdoi
10.1016/0092-8674(91)90179-3subject
Has Abstractpub_date
1991-10-18 00:00:00pages
275-82issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(91)90179-3journal_volume
67pub_type
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