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Putting J Chain Back on the Map: How Might Its Expression Define Plasma Cell Development?

Journal

JOURNAL OF IMMUNOLOGY
Volume 193, Issue 7, Pages 3248-3255

Publisher

AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1400531

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Funding

  1. National Institutes of Health [R01OD0549]
  2. National Institute of Allergy and Infectious Diseases Institutional training grants in Cardiac and Vascular Cell Biology and Immunity and Infection [5T32HL072751, T32AI007540]

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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 2 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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