Calcium signalling by the high affinity macrophage Fc gamma receptor requires the cytosolic domain.

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

Immunobiology

journal_title

Immunobiology

authors

Indik Z,Chien P,Levinson AI,Schreiber AD

doi

10.1016/s0171-2985(11)80640-6

subject

Has Abstract

pub_date

1992-08-01 00:00:00

pages

183-92

issue

2-4

eissn

0171-2985

issn

1878-3279

pii

S0171-2985(11)80640-6

journal_volume

185

pub_type

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