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  • Title: [Binding of IgA1 to monocyte/macrophage cell lines (THP-1, U937) in IgA nephropathy--a possible role of O-glycan in the IgA1 molecule].
    Author: Horii A, Hiki Y, Saitoh M, Kanamori A, Iwase H, Hotta K, Kobayashi Y.
    Journal: Nihon Jinzo Gakkai Shi; 1995 Oct; 37(10):558-63. PubMed ID: 7474508.
    Abstract:
    IgA1 is an exceptional serum glycoprotein because it has O-glycans in the hinge region. It has been observed that the monocyte/macrophages infiltrate within the glomeruli in IgA-N. On the other hand, it is well established that the carbohydrate side chains (N-glycans) of the IgG molecule play a role in the binding of IgG to Fc receptors. Therefore, the binding of IgA1 to monocyte/macrophage cell lines was observed with the aim of clarifying the role of the O-glycan side chains in IgA-N in the initial mechanism of glomerular damage due to the interaction between the O-glycan chains on the IgA1 molecule and infiltrating monocyte/macrophages. Two human myelomonocytic cell lines, THP-1 and U-937, were activated and incubated with separated IgA1 (IgA-N, n = 16; other glomerulonephritides (other GN), n = 15; healthy controls, n = 9). The binding attitude of IgA1 to the cell lines was observed by flow immunofluorometry using a FACScan. FACScan showed that the binding of IgA1 to both of the stimulated monocyte/macrophage cell lines was increased in IgA-N compared to the normal controls and other GN. The binding of IgA1 to THP-1 was partially, but definitely inhibited by adding 100 mM melibiose (19.6 +/- 7.7%) and galactose (13.1 +/- 2.9%), but not glucose (2.9 +/- 2.2%), lactose (4.7 +/- 4.7%) and mannose (3.3 +/- 3.3%). These results suggested that THP-1 had a receptor that recognized the O-glycan in the IgA1 hinge region.(ABSTRACT TRUNCATED AT 250 WORDS)
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