| First Author | Hendrickson BA | Year | 1995 |
| Journal | J Exp Med | Volume | 182 |
| Issue | 6 | Pages | 1905-11 |
| PubMed ID | 7500036 | Mgi Jnum | J:75843 |
| Mgi Id | MGI:2177918 | Doi | 10.1084/jem.182.6.1905 |
| Citation | Hendrickson BA, et al. (1995) Altered hepatic transport of immunoglobulin A in mice lacking the J chain. J Exp Med 182(6):1905-11 |
| abstractText | We have created J chain knockout mice to define the physiologic role of the J chain in immunoglobulin synthesis and transport. The J chain is covalently associated with pentameric immunoglobulin (Ig) M and dimeric IgA and is also expressed in most IgG-secreting cells. J chain-deficient mice have normal serum IgM and IgG levels but markedly elevated serum IgA. Although polymeric IgA was present in the mutant mice, a larger proportion of their serum IgA was monomeric than was found in wild-type mouse serum. Bile and fecal IgA levels were decreased in J chain-deficient mice compared with wild-type mice, suggesting inefficient transport of J chain-deficient IgA by hepatic polymeric immunoglobulin receptors (pIgR). The pIgR-mediated transport of serum-derived IgA from wild-type and mutant mice was assessed in Madin-Darby canine kidney (MDCK) cells transfected with the pIgR. These studies revealed selective transport by pIgR-expressing MDCK cells of wild-type IgA but not J chain-deficient IgA. We conclude that although the J chain is not required for IgA dimerization, it does affect the efficiency of polymerization or have a role in maintaining IgA dimer stability. Furthermore, the J chain is essential for efficient hepatic pIgR transport of IgA. |
