Identification of a novel Fcα receptor expressed by human mesangial cells

Barratt, Jonathan; Greer, Morag R.; Pawluczyk, Izabella Z. A.; Allen, Alice C.; Bailey, E.; Buck, Katharine; Feehally, John

doi:10.1046/j.1523-1755.2000.00043.x

Cited by 50 publications

(31 citation statements)

References 54 publications

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“…However, none of the known IgA receptors (CD89, asialoglycoprotein receptor, and polymeric immunoglobulin receptor) is expressed on human mesangial cells (24,67,(89)(90)(91). Among the recently identified candidate receptors that may mediate binding of IgA1 and IgA1 complexes are CD71 (transferrin receptor) (88,(91)(92)(93) and the Fcα/μ receptor (94).…”

Section: Biological Activities Of Iga1-containing Immune Complexesmentioning

confidence: 99%

IgA Glycosylation and IgA Immune Complexes in the Pathogenesis of IgA Nephropathy

Novák

Julian

Tomana

et al. 2008

Seminars in Nephrology

176

134

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Section: Biological Activities Of Iga1-containing Immune Complexesmentioning

confidence: 99%

IgA Glycosylation and IgA Immune Complexes in the Pathogenesis of IgA Nephropathy

Novák

Julian

Tomana

et al. 2008

Seminars in Nephrology

176

134

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“…An IgA-specific receptor was reported on kidney mesangial cells [85]. This receptor was distinct from other known IgA receptors such as FcαRI, pIgR, or ASGPR because these are not expressed on mesangial cells [86,87] [81].…”

Section: Interaction Of the Transferrin Receptor With The Iga1 Immunementioning

confidence: 99%

IgA and IgA-specific receptors in human disease: structural and functional insights into pathogenesis and therapeutic potential

Gomes

Herr

2006

Springer Semin Immun

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IgA antibodies play an important role in humoral immunity. IgA is the predominant antibody in mucosal secretions and the second most prevalent in the serum. It occupies a unique position among human antibodies in that it can both trigger and suppress inflammatory responses, depending on the situation. Recent structural and functional studies have revealed details of the structure of IgA and its interaction with key cell-surface receptors. We look at the role IgA and IgA receptors (particularly FcalphaRI) play in the pathogenesis of diseases such as IgA nephropathy and other autoimmune conditions. Finally, we address the potential of IgA as a therapeutic tool to either trigger specific inflammatory responses to destroy target cells or suppress inflammatory responses in the case of autoimmune diseases, and the promise of mucosal vaccines for eliciting specific IgA responses to pathogens in mucosal environments.

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“…34,57 These conflicting results are possibly resolved by the recent publication, by a British group, showing the expression of mRNA transcripts with partial identity to CD89 on human MC in vitro, using RT-PCR. 58 The transcripts detected were located in the area of the extracellular domain 2 of CD89. Thus, although mRNA sequences with partial identity to CD89 are present in MCs, it is unlikely that the binding of IgA is mediated via these transcripts, because it has been shown that the binding of IgA to CD89 is mediated via the extracellular domain 1.…”

Section: Iga Receptorsmentioning

confidence: 98%

“…59 These authors, too, were unable to demonstrate CD89 on the surface of MCs, or in culture medium, using Western blots. 58 Consequently, the transcript fragments they identified may encode a new protein with partial homology to CD89. This hypothesis originates from the recent discovery of genes mapping to chromosome 19Q13.4 that encode a family of type I transmembrane proteins with significant homology: CD89, paired Ig-like receptors, killer inhibitor receptors, leukocyte Ig-like receptor, and Ig-like transcripts.…”

Section: Iga Receptorsmentioning

confidence: 99%

IgA-Nephropathy: how does IgA activate the mesangial cell?

Westerhuis

Kitahara

Floege

2001

Clinical and Experimental Nephrology

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Immunoglobulin (Ig)A-nephropathy (IgAN), the most common glomerulonephritis worldwide, is immunohistochemically characterized by the deposition of IgA in the renal mesangium. The mechanism of binding and deposition of IgA in the kidney is still not clear. It has been demonstrated that IgA-binding to mesangial cells (MCs) is followed by cell activation, as indicated by the enhanced expression of proinflammatory cytokines, the nuclear transcriptional factor (NF)kB, or the protooncogene c-jun. The binding of IgA to MC is mediated via the Fc part of the immunoglobulin, as demonstrated by blocking experiments using Fc-fragments of IgA. The known myeloid Fc receptor for IgA (FcαRI/CD89), as well as other known receptors able to bind IgA (asialoglycoprotein receptor, mannose receptor, secretory component), are not expressed on MC. However the hepatic asialoglycoprotein receptor, as well as the myeloid FcαRI, play an important role in the clearance of IgA from the circulation. In patients with IgAN, this function seems to be impaired, possibly as a consequence of reduced glycosylation of the hinge region of IgA1 which affects IgA-receptor interactions. This could lead to increased plasma levels of IgA, resulting in increased binding of IgA to MC via a hitherto unidentified Fc receptor for IgA. Recently, the expression of mRNA transcripts with partial identity to CD89 was reported on human MC in vitro. These transcripts could be part of this new receptor, with partial homology to recently discovered genes that map to chromosome 19Q13.4 and encode a family of type I transmembrane proteins.

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Identification of a novel Fcα receptor expressed by human mesangial cells

Cited by 50 publications

References 54 publications

IgA Glycosylation and IgA Immune Complexes in the Pathogenesis of IgA Nephropathy

IgA Glycosylation and IgA Immune Complexes in the Pathogenesis of IgA Nephropathy

IgA and IgA-specific receptors in human disease: structural and functional insights into pathogenesis and therapeutic potential

IgA-Nephropathy: how does IgA activate the mesangial cell?

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