Ba. Hendrickson et al., LACK OF ASSOCIATION OF SECRETORY COMPONENT WITH IGA IN J-CHAIN-DEFICIENT MICE, The Journal of immunology, 157(2), 1996, pp. 750-754
J chain has been proposed to play a role in the mucosal transport of p
olymeric Igs (pIg) by the polymeric Ig receptor (pIgR). We have previo
usly reported the generation of J chain-deficient mice. These mice exh
ibited elevated serum IgA and depleted biliary and fecal IgA levels co
mpared with wild-type mice. We report here that, unlike the IgA levels
in bile and feces, IgA levels in local mucosal and glandular secretio
ns were not depressed in J chain-deficient mice. Breast milk, intestin
al mucosal surface, and nasal wash IgA levels in the mutant mice were
similar to wild-type mice while bronchoalveolar lavage IgA levels were
higher in the J chain-deficient animals. Western blot analysis with a
n Ab to secretory component (SC), the portion of the pIgR that remains
bound to pig in secretions, and immunoprecipitation with Abs directed
against IgA showed that secreted IgA was associated with SC in wild-t
ype but not J chain-deficient mice. The IgA in wild-type secretions wa
s polymeric while the secretion s of J chain-deficient mice contained
IgA monomers and other nonpolymeric IgA forms. Thus, J chain is not es
sential for IgA transport by intestinal, mammary, or respiratory epith
elia but is necessary for the stable association of pIgA with SC. Furt
her, we suggest that J chain-deficient IgA is transported into secreti
ons by a different mechanism than wild-type IgA.