In:
The Journal of Immunology, The American Association of Immunologists, Vol. 160, No. 12 ( 1998-06-15), p. 5979-5989
Abstract:
Previous studies have discerned two forms of polymeric mouse IgM: moderately cytolytic (complement-activating) pentamer, which contains J chain, and highly cytolytic hexamer, which lacks J chain. To investigate the relationships among polymeric structure, J chain content, and cytolytic activity, we produced IgM in J chain-deficient and J chain-proficient mouse hybridoma cell lines. Both hexamer and pentamer were produced in the absence as well as the presence of J chain. Hexameric IgM activated (guinea pig) complement approximately 100-fold more efficiently than did J chain-deficient pentamer, which, in turn, was more active than J chain-containing pentamer. These results are consistent with the hypothesis that J chain-containing pentamer cannot activate complement. We also analyzed the structure of IgM-S337, in which the μ-chain bears the C337S substitution. Like normal IgM, IgM-S337 was formed as a hexamer and as both J chain deficient- and J chain-containing pentamers. Unlike normal IgM, IgM-S337 dissociated in SDS into various subunits. For IgM-S337 pentamer, the predominant subunits migrated as μ2κ2 and μ4κ4, and the subunit distribution was unaltered by J chain. However, J chain was found only in the μ2κ2 species, suggesting that some arrangement of inter-μ bonds directs incorporation of J chain. IgM-S337 hexamer also dissociated to μ2κ2 and μ4κ4, but also yielded several species migrating much more slowly in SDS-PAGE than wild-type μ12κ12. To account for these forms, we propose that each μ-chain can interact with three other μ-chains and that some hexameric molecules contain two catenated μ6κ6 circles.
Type of Medium:
Online Resource
ISSN:
0022-1767
,
1550-6606
DOI:
10.4049/jimmunol.160.12.5979
Language:
English
Publisher:
The American Association of Immunologists
Publication Date:
1998
detail.hit.zdb_id:
1475085-5
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