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Volume 271, Number 29, Issue of July 19, 1996 pp. 17091-17099
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Extracellular Mutations of Non-obese Diabetic Mouse FcRI Modify Surface Expression and Ligand Binding

(Received for publication, February 9, 1996, and in revised form, April 15, 1996)

Amanda L. Gavin , John A. Hamilton ^§ and P. Mark Hogarth

From the  Austin Research Institute, Austin Hospital, Heidelberg, Victoria 3084 and the ^§ University of Melbourne, Department of Medicine, Royal Melbourne Hospital, Parkville, Victoria 3050, Australia

The non-obese diabetic mouse (NOD) expresses a unique form of the high affinity receptor for IgG (FcRI), containing multiple mutations that result in substitutions and insertions of amino acids and a truncated cytoplasmic tail. As a result of these major changes, receptor affinity for IgG increases 10-fold over that of wild-type FcRI from BALB/c mice, while the specificity for ligand is retained. Kinetic analysis revealed that while the association rate of IgG with FcRI from NOD mice (FcRI-NOD) and FcRI from BALB/c mice (FcRI-BALB) is similar, IgG bound much more tightly to FcRI-NOD as revealed by a profoundly diminished dissociation rate.

Transfection studies demonstrated that FcRI-NOD was expressed at one-tenth of the level of FcRI-BALB. Although mouse FcRI was previously not known to associate with the FcRI -subunit, transfection of COS-7 cells demonstrates that like human FcRI, mouse FcRI is also able to associate with this signaling subunit. Furthermore, expression levels of FcRI-NOD were not restored by the presence of the FcRI -subunit. The difference in the levels of expression was mapped to mutations in the extracellular region of FcRI-NOD as replacement of the extracellular domains with those of human FcRI or FcRI-BALB restored expression to that of human FcRI or FcRI-BALB.

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