Abstract:
:Hematopoietic cells express multiple receptors which bind the Fc domain of IgG. We utilized transfection of COS-1 cells, a cell line which lacks endogenous Fc receptors, to study the expression and function of Fc gamma RI, the high affinity Fc gamma receptor in the absence of other Fc gamma receptors. Fc gamma RI was efficiently expressed in transiently transfected COS-1 cells as measured by flow cytometry and the binding of IgG sensitized RBCs (EA). In addition, analysis at the single cell level demonstrated that individually transfected COS-1 cells release cytosolic free Ca2+ [(Ca2+)i] upon activation with anti-Fc gamma RI antibody. The calcium response required Fc gamma RI cross-linking. COS-1 cells transfected with mutant Fc gamma RI lacking the cytosolic domain expressed Fc gamma receptors and bound EA as well as wild type receptors, but failed to induce an increase in [Ca2+]i. These data indicate that Fc gamma RI in the absence of other Fc gamma receptors mediates a calcium signal and that the cytoplasmic domain of Fc gamma RI contains the elements required for calcium dependent signal transduction.
journal_name
Immunobiologyjournal_title
Immunobiologyauthors
Indik Z,Chien P,Levinson AI,Schreiber ADdoi
10.1016/s0171-2985(11)80640-6subject
Has Abstractpub_date
1992-08-01 00:00:00pages
183-92issue
2-4eissn
0171-2985issn
1878-3279pii
S0171-2985(11)80640-6journal_volume
185pub_type
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