Structural Requirements for Polymeric Immunoglobulin Assembly and Association with
نویسندگان
چکیده
Both IgM and IgA exist as polymeric immunoglobulins. IgM is assembled into pentamers with J chain and hexamers lacking J chain. In contrast, polymeric IgA exists mostly as dimers with J chain. Both IgM and IgA possess an 18-amino acid extension of the C terminus (the tail-piece (tp)) that participates in polymerization through a penultimate cysteine residue. The IgM (mtp) and IgA (atp) tail-pieces differ at seven amino acid positions. However, the tail-pieces by themselves do not determine the extent of polymerization. We now show that the restriction of polymerization to dimers requires both Ca3 and atp and that more efficient dimer assembly occurs when Ca2 is also present; the dimers contain J chain. Formation of pentamers containing J chain requires Cm3, Cm4, and the mtp. IgM-atp is present mainly as hexamers lacking J chain, and mmgm-mtp forms tetramers and hexamers lacking J chain, whereas IgA-mtp is present as high order polymers containing J chain. In addition, there is heterogeneous processing of the Nlinked carbohydrate on IgA-mtp, with some remaining in the high mannose state. These data suggest that in addition to the tail-piece, structural motifs in the constant region domains are critical for polymer assembly and J chain incorporation.
منابع مشابه
Structural requirements for polymeric immunoglobulin assembly and association with J chain.
Both IgM and IgA exist as polymeric immunoglobulins. IgM is assembled into pentamers with J chain and hexamers lacking J chain. In contrast, polymeric IgA exists mostly as dimers with J chain. Both IgM and IgA possess an 18-amino acid extension of the C terminus (the tail-piece (tp)) that participates in polymerization through a penultimate cysteine residue. The IgM (mutp) and IgA (alphatp) tai...
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