STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES

ENGELHARDT W, GORCZYTZA H, BUTTERWECK A, MONKEMANN H, Frey J (1991)
EUROPEAN JOURNAL OF IMMUNOLOGY 21(9): 2227-2238.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ;
Abstract
Two isotypes of the monocyte/macrophage as well as B cell Fc-gamma receptor type II (FcRIIa and FcRIIb2, respectively) mainly differ in the length (76 vs. 44 amino acids) and amino acid sequence of their cytoplasmic domains. Only the eight amino acids just behind the putative transmembrane region are identical. Despite this marked difference, both FcRII mediate endocytosis of immune complexes. To determine the functional significance of the cytoplasmic domains, we expressed truncated FcRIIa and FcRIIb2 in FcR- BHK-21 cells. Mutants of both receptors containing only one amino acid (tail-minus) of the cytoplasmic domain failed to mediate immune complex uptake. The significance of the cytoplasmic domain of the receptors could be further demonstrated using a chimeric FcRIII-FcRIIa construct. Therefore we expressed an FcRIII lacking the hydrophobic carboxyl terminus (containing the putative phosphatidyl - inositol - glycan anchor site) fused inframe to the transmembrane and cytoplasmic domain of the FcRIIa in BHK-21 cells. In contrast to the wild type FcRIII, this chimeric receptor mediated immune complex uptake indistinguishable from that mediated by the FcRIIa. Receptor mutants with relatively short cytoplasmic domains (FcRIIb2: 13, and FcRIIa: 16 amino acids) revealed, that these short amino acid stretches are sufficient to allow reduced receptor-mediated endocytosis of bound ligand. Furthermore, using FcRIIa deletion mutants with a cytoplasmic domain consisting of 62, 46, and 28 amino acids, respectively, we found that the capability of these mutants to mediate immune complex uptake decreased gradually with the truncation of the cytoplasmic tails. Thus, only short amino acids sequences of the cytoplasmic domain are sufficient to enable an, albeit reduced, receptor-mediated endocytosis.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

ENGELHARDT W, GORCZYTZA H, BUTTERWECK A, MONKEMANN H, Frey J. STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES. EUROPEAN JOURNAL OF IMMUNOLOGY. 1991;21(9):2227-2238.
ENGELHARDT, W., GORCZYTZA, H., BUTTERWECK, A., MONKEMANN, H., & Frey, J. (1991). STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES. EUROPEAN JOURNAL OF IMMUNOLOGY, 21(9), 2227-2238.
ENGELHARDT, W., GORCZYTZA, H., BUTTERWECK, A., MONKEMANN, H., and Frey, J. (1991). STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES. EUROPEAN JOURNAL OF IMMUNOLOGY 21, 2227-2238.
ENGELHARDT, W., et al., 1991. STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES. EUROPEAN JOURNAL OF IMMUNOLOGY, 21(9), p 2227-2238.
W. ENGELHARDT, et al., “STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES”, EUROPEAN JOURNAL OF IMMUNOLOGY, vol. 21, 1991, pp. 2227-2238.
ENGELHARDT, W., GORCZYTZA, H., BUTTERWECK, A., MONKEMANN, H., Frey, J.: STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES. EUROPEAN JOURNAL OF IMMUNOLOGY. 21, 2227-2238 (1991).
ENGELHARDT, W, GORCZYTZA, H, BUTTERWECK, A, MONKEMANN, H, and Frey, Jürgen. “STRUCTURAL REQUIREMENTS OF THE CYTOPLASMIC DOMAINS OF THE HUMAN MACROPHAGE FC-GAMMA RECEPTOR-IIA AND B-CELL FC-GAMMA RECEPTOR-IIB2 FOR THE ENDOCYTOSIS OF IMMUNE-COMPLEXES”. EUROPEAN JOURNAL OF IMMUNOLOGY 21.9 (1991): 2227-2238.
This data publication is cited in the following publications:
This publication cites the following data publications:

10 Citations in Europe PMC

Data provided by Europe PubMed Central.

Biotechnological approaches for the production of prebiotics and their potential applications.
Panesar PS, Kumari S, Panesar R., Crit. Rev. Biotechnol. 33(4), 2013
PMID: 22985065
Differential requirement of lipid rafts for FcγRIIA mediated effector activities.
Vieth JA, Kim MK, Pan XQ, Schreiber AD, Worth RG., Cell. Immunol. 265(2), 2010
PMID: 20728077
Epitope mapping of new monoclonal antibodies recognizing distinct human FcRII (CD32) isoforms.
Weinrich V, Sondermann P, Bewarder N, Wissel K, Frey J., Hybridoma 15(2), 1996
PMID: 8743290
In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcgammaRII) phosphorylation.
Bewarder N, Weinrich V, Budde P, Hartmann D, Flaswinkel H, Reth M, Frey J., Mol. Cell. Biol. 16(9), 1996
PMID: 8756631
Structure/function relationships of Fc gamma receptors in phagocytosis.
Indik ZK, Park JG, Hunter S, Schreiber AD., Semin. Immunol. 7(1), 1995
PMID: 7612895
Fc receptor-mediated signal transduction.
Lin CT, Shen Z, Boros P, Unkeless JC., J. Clin. Immunol. 14(1), 1994
PMID: 8132732

40 References

Data provided by Europe PubMed Central.

The Fc receptor for IgG on human natural killer cells: phenotypic, functional, and comparative studies with monoclonal antibodies.
Perussia B, Trinchieri G, Jackson A, Warner NL, Faust J, Rumpold H, Kraft D, Lanier LL., J. Immunol. 133(1), 1984
PMID: 6233371

Pearse, Trends Biochem. Sci. 5(), 1980

Höning, 0
Transport of macrophage Fc receptors and Fc receptor-bound ligands to lysosomes.
Ukkonen P, Lewis V, Marsh M, Helenius A, Mellman I., J. Exp. Med. 163(4), 1986
PMID: 3950548

Sinclair, Immunol. Today 8(), 1987

Davis, J. Biol. Chem. 262(), 1987
Internalization of the human immunodeficiency virus does not require the cytoplasmic domain of CD4.
Bedinger P, Moriarty A, von Borstel RC 2nd, Donovan NJ, Steimer KS, Littman DR., Nature 334(6178), 1988
PMID: 3260353
Requirements for modulation of the CD4 molecule in response to phorbol myristate acetate. Role of the cytoplasmic domain.
Sleckman BP, Bigby M, Greenstein JL, Burakoff SJ, Sy MS., J. Immunol. 142(5), 1989
PMID: 2783943
Structural features of the cytoplasmic region of CD4 required for internalization.
Shin J, Doyle C, Yang Z, Kappes D, Strominger JL., EMBO J. 9(2), 1990
PMID: 2105883
Fc receptor phosphorylation during receptor-mediated control of B-cell activation.
Hunziker W, Koch T, Whitney JA, Mellman I., Nature 345(6276), 1990
PMID: 2190097

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 1832386
PubMed | Europe PMC

Search this title in

Google Scholar