Putting J chain back on the map: how might its expression define plasma cell development?

CD Castro, MF Flajnik - The Journal of Immunology, 2014 - journals.aai.org
CD Castro, MF Flajnik
The Journal of Immunology, 2014journals.aai.org
Joining chain (J chain) is a small polypeptide that regulates multimerization of secretory IgM
and IgA, the only two mammalian Igs capable of forming multimers. J chain also is required
for poly-Ig receptor–mediated transport of these Ig classes across the mucosal epithelium. It
is generally assumed that all plasma cells express J chain regardless of expressed isotype,
despite the documented presence of J chain− plasma cells in mammals, specifically in all
monomeric IgA-secreting cells and some IgG-secreting cells. Compared with most other …
Abstract
Joining chain (J chain) is a small polypeptide that regulates multimerization of secretory IgM and IgA, the only two mammalian Igs capable of forming multimers. J chain also is required for poly-Ig receptor–mediated transport of these Ig classes across the mucosal epithelium. It is generally assumed that all plasma cells express J chain regardless of expressed isotype, despite the documented presence of J chain− plasma cells in mammals, specifically in all monomeric IgA-secreting cells and some IgG-secreting cells. Compared with most other immune molecules, J chain has not been studied extensively, in part because of technical limitations. Even the reported phenotype of the J chain–knockout mouse is often misunderstood or underappreciated. In this short review, we discuss J chain in light of the various proposed models of its expression and regulation, with an added focus on its evolutionary significance, as well as its expression in different B cell lineages/differentiation states.
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