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IgA nephropathy (IgAN) is characterized by raised serum  IgA and predominant mesangial IgA deposits of polymeric nature. The expression  of IgA receptor molecules in white blood cells and glomerular mesangial cells  has recently attracted much attention in relation to the uptake of IgA by  these cells. This study investigates the expression of IgA Fc receptor  (FcαR1 or CD89), asialoglycoprotein receptor (ASGPR), and polymeric Ig  receptor (pIgR) in cultured glomerular mesangial cells. Using a sensitive  nested reverse transcription-PCR, mRNA encoding for FcαR1, pIgR, or the  H2 chain of ASGPR was not demonstrated on human mesangial cells. U937, HepG2,  and HT29 cell lines, used as positive controls, strongly expressed the  FcαR1, ASGPR, and pIgR mRNA, respectively, under similar experimental  conditions. Flow cytometry also demonstrated the presence of surface proteins  for FcαR1, ASGPR, and pIgR on the respective control cell lines but not  on human mesangial cells. Expression of FcαR1 mRNA on cultured U937  cells was upregulated by tumor necrosis factor-α. However, tumor  necrosis factor-α, interleukin-1β, or transforming growth  factor-β failed to induce the expression of FcαR1 on human  mesangial cells. Human serum IgA or secretory IgA bound to human mesangial  cells, HepG2, or the U937 cell line in a dose-dependent manner. The binding of  purified IgA to human mesangial cells was not blocked by preincubation with  human IgG, IgM, orosomucoid, asialoorosomucoid, anti-CD89 antibody (My43), or  anti-secretory component antibody. The present study concluded that there was  an absence of FcαR1, ASGPR, or pIgR on human mesangial cells. These  findings suggest that the predominant binding of human IgA to human mesangial  cells is mediated by other mechanisms.

Absence of CD89, Polymeric Immunoglobulin Receptor, and Asialoglycoprotein Receptor on Human Mesangial Cells