Please use this identifier to cite or link to this item:
https://ahro.austin.org.au/austinjspui/handle/1/13428
Title: | Extracellular mutations of non-obese diabetic mouse FcgammaRI modify surface expression and ligand binding. | Austin Authors: | Gavin, A L;Hamilton, J A;Hogarth, P Mark | Affiliation: | Austin Research Institute, Austin Hospital, Heidelberg, Victoria 3084, Australia | Issue Date: | 19-Jul-1996 | Publication information: | The Journal of Biological Chemistry; 271(29): 17091-9 | Abstract: | The non-obese diabetic mouse (NOD) expresses a unique form of the high affinity receptor for IgG (FcgammaRI), 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 FcgammaRI from BALB/c mice, while the specificity for ligand is retained. Kinetic analysis revealed that while the association rate of IgG with FcgammaRI from NOD mice (FcgammaRI-NOD) and FcgammaRI from BALB/c mice (FcgammaRI-BALB) is similar, IgG bound much more tightly to FcgammaRI-NOD as revealed by a profoundly diminished dissociation rate. Transfection studies demonstrated that FcgammaRI-NOD was expressed at one-tenth of the level of FcgammaRI-BALB. Although mouse FcgammaRI was previously not known to associate with the FcepsilonRI gamma-subunit, transfection of COS-7 cells demonstrates that like human FcgammaRI, mouse FcgammaRI is also able to associate with this signaling subunit. Furthermore, expression levels of FcgammaRI-NOD were not restored by the presence of the FcepsilonRI gamma-subunit. The difference in the levels of expression was mapped to mutations in the extracellular region of FcgammaRI-NOD as replacement of the extracellular domains with those of human FcgammaRI or FcgammaRI-BALB restored expression to that of human FcgammaRI or FcgammaRI-BALB. | Gov't Doc #: | 8663283 | URI: | https://ahro.austin.org.au/austinjspui/handle/1/13428 | Journal: | The Journal of biological chemistry | URL: | https://pubmed.ncbi.nlm.nih.gov/8663283 | Type: | Journal Article | Subjects: | Amino Acid Sequence Animals Bone Marrow.immunology Bone Marrow Cells Cell Line Cercopithecus aethiops DNA Primers DNA, Complementary Diabetes Mellitus, Type 1.genetics.immunology Flow Cytometry Humans Immunoglobulin G.metabolism Kinetics Ligands Macrophages.immunology Mice Mice, Inbred BALB C Mice, Inbred NOD Molecular Sequence Data Mutagenesis, Site-Directed Polymerase Chain Reaction Receptors, IgG.biosynthesis.genetics.metabolism Recombinant Fusion Proteins.biosynthesis.metabolism Sequence Homology, Amino Acid Spleen.immunology Substrate Specificity Transfection |
Appears in Collections: | Journal articles |
Show full item record
Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.