Abstract
Secretory immunoglobulins consist of IgA or IgM, secretory component (SC) and joining (J) chain. J chain is a 15 kilodalton polypeptide that participates in the intracellular polymerization of IgA and IgM and is found in plasma cells1. J chain was also found at earlier stages of B cell differentiation before the onset of immunoglobulin synthesise2. IgA or IgM is produced by plasma cells, polymerized intracellularly and secreted into the lamina propria of glandular tissues. SC, which is localized in the basolateral membrane of glandular tissues, functions as a receptor for J chain-containing polymeric immunoglobulins3. Ontogenically, it has been reported that SC and IgM are expressed at an early gestational age while IgA usually appears later4,5. However, the exact development of the secretory immune system in the human fetus has not been examined extensively.
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Moro, I., Saito, I., Asano, M., Takahashi, T., Iwase, T. (1991). Ontogeny of the Secretory IgA System in Humans. In: Mestecky, J., Blair, C., Ogra, P.L. (eds) Immunology of Milk and the Neonate. Advances in Experimental Medicine and Biology, vol 310. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3838-7_5
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DOI: https://doi.org/10.1007/978-1-4615-3838-7_5
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