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11 Patry C, Sibille Y, Lehuen A, Monteiro RC: Identification of FcαR (CD89) isoforms generated by alternative splicing that are differentially expressed between blood monocytes and alveolar macrophages. J Immunol 1996, 156:4442-4448.
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12 De Wit TPM, Morton HC, Capel PJA, van de Winkel JGJ: Structure of the gene for the human myeloid IgA Fc receptor (CD89) J Immunol 1995, 155:1203-1209.
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0033557751
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Identification of residues in the first domain of human Fcα receptor essential for interaction with IgA
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This paper describes the affinity of IgA for recombinant CD89 using a biosensor and the location of residues essential for IgA binding in the first extracellular domain
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14 Wines BD, Hulett MD, Jamieson GP, Trist HM, Spratt JM, Hogarth PM: Identification of residues in the first domain of human Fcα receptor essential for interaction with IgA. J Immunol 1999, 162:2146-2153. This paper describes the affinity of IgA for recombinant CD89 using a biosensor and the location of residues essential for IgA binding in the first extracellular domain.
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0031820723
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Down-regulation of Fcα receptors on blood cells of IgA nephropathy patients: Evidence for a negative regulatory role of serum IgA
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This study investigates the expression of CD89 on IgA-N blood phagocytes using monoclonal antibodies specific for epitopes located outside IgA binding site. Patient FcαR are markedly decreased on the cell surface of monocytes, which inversely correlates with serum IgA levels. Surface expression is rapidly up-regulated by incubation at 37°C. In vitra experiments show that polymeric IgA induces a marked decrease in FcαR expression on cultured monocytes from normal individuals. It also shows that patient cells have more endogenous IgA bound to surface FcαR, which is linked to renal lesions. Furthermore, patient IgA binds more avidly to FcαR than control IgA
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18 Grossetête B, Launay P, Lehuen A, Jungers P, Bach JF, Monteiro RC: Down-regulation of Fcα receptors on blood cells of IgA nephropathy patients: evidence for a negative regulatory role of serum IgA. Kidney Int 1998, 53:1321-1335. This study investigates the expression of CD89 on IgA-N blood phagocytes using monoclonal antibodies specific for epitopes located outside IgA binding site. Patient FcαR are markedly decreased on the cell surface of monocytes, which inversely correlates with serum IgA levels. Surface expression is rapidly up-regulated by incubation at 37°C. In vitra experiments show that polymeric IgA induces a marked decrease in FcαR expression on cultured monocytes from normal individuals. It also shows that patient cells have more endogenous IgA bound to surface FcαR, which is linked to renal lesions. Furthermore, patient IgA binds more avidly to FcαR than control IgA.
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19
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Altered expression of monocyte IgA Fc receptors is associated with defective endocytosis in patients with alcoholic cirrhosis: Potential role of IFN-γ
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19 Silvain C, Patry C, Launay P, Lehuen A, Monteiro RC: Altered expression of monocyte IgA Fc receptors is associated with defective endocytosis in patients with alcoholic cirrhosis: potential role of IFN-γ. J Immunol 1995, 155:1606-1618.
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0030052523
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20 Reterink TJ, Levarht EW, Klar-Mohamad N, Van Es LA, Daha MR: Transforming growth factor-beta 1 (TGF-β1) down-regulates IgA Fc-receptor (CD89) expression on human monocytes. Clin Exp Immunol 1996, 103:161-166.
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0029597781
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24 Morton HC, Vandenherikoudijk IE, Vossebeld P, Snijders A, Verhoeven AJ, Capel PJA, van de Winkel JGJ: Functional association between the human myeloid immunoglobulin A Fc receptor (CD89) and FcRγ chain: molecular basis for CD89/FcRγ chain association. J Biol Chem 1995, 270:29781-29787.
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25
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0033548477
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Alternative endocytic pathway for IgA Fc receptors (CD89) depends on lack of FcRγ association and protects against degradation of bound ligand
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This study demonstrated the existence of two types of CD89 on the cell surface, associated and unassociated with FcRγ chain. γ-Less FcαR binds monomeric and polymeric IgA and is the main type of receptor expressed on blood cells. They are important to internalize, recycle, and protect IgA against degradation, playing an important role in IgA homeostasis
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25 Launay P, Patry C, Lehuen A, Pasquier B, Blank U, Monteiro RC: Alternative endocytic pathway for IgA Fc receptors (CD89) depends on lack of FcRγ association and protects against degradation of bound ligand. J Biol Chem 1999, 274:7216-7225. This study demonstrated the existence of two types of CD89 on the cell surface, associated and unassociated with FcRγ chain. γ-Less FcαR binds monomeric and polymeric IgA and is the main type of receptor expressed on blood cells. They are important to internalize, recycle, and protect IgA against degradation, playing an important role in IgA homeostasis.
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