In:
European Journal of Biochemistry, Wiley, Vol. 228, No. 3 ( 1995-03), p. 587-595
Abstract:
Murine class III receptors for IgG (mFcγRIII) are composed of an IgG‐binding α chain associated with a γ subunit dimer. These receptors have been shown to trigger the release of serotonin and tumor necrosis factor‐α [Daëron, M., Latour, S., Hückel, C., Bonnerot, C. & Fridman, W. H. (1992) Immunobiology 185 , 159–174], and are involved in endocytosis and phagocytosis [Daëron, M., Malbec, O., Bonnerot, C., Latour, S., Segal, D. M. & Fridman, W. H. (1994) J. Immunol. 152 , 783–792]. Using a transfection model where the cDNA encoding mFcγRIII was stably transfected into the rat basophilic leukemia cell line RBL‐2H3, we found that the functional efficiency of mFcγRIII is correlated with its ability to increase the intracellular Ca 2+ concentration and to stimulate inositol phosphate metabolism. The deletion of intracellular sequences of the α subunit did not alter the ability of mFcγRIII to trigger the Ca 2+ and phosphatidylinositol 4,5‐bisphosphate [PtdIns(4,5) P 2 ] response. After substitution of the intracellular domain of mFcγRII for that of mFcγRIIIγ, but not that of mFcγRIIIα, the chimeric receptor was also able to trigger Ca 2+ and PtdIns(4,5) P 2 responses. In contrast, all transfected receptors induced protein kinase C translocation. Furthermore, dimerization of the receptor was sufficient for the initiation of this protein kinase C translocation while a further cross‐linking was necessary for the induction of the Ca 2+ and PtdIns(4,5) P 2 responses. Protein kinase C translocation therefore can be dissociated from Ca 2+ mobilization, PtdIns(4,5) P 2 turnover and mast cell secretory responses induced by murine FcγRIII.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1995.228.issue-3
DOI:
10.1111/j.1432-1033.1995.0587m.x
Language:
English
Publisher:
Wiley
Publication Date:
1995
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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