Transport of Oligomeric Iga of Systemic Origin Into External Secretions

  • Gabriel Virella
  • Paul C. Montgomery
  • Isabel M. Lemaitre-Coelho
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 107)


Secretory IgA (s-IgA) is thought to be synthesized predominantly by plasma cells located around the mucosae and glandular epithelia (1–3), the main argument being the failure of radiolabeled monomeric IgA to be transferred to secretions (1,4). It is also believed that submucosal plasma cells synthesize predominantly dimeric IgA molecules that are selectively transferred (5,6). Brandtzaeg (7) has suggested that the J-chain present in dimeric IgA allows recognition by mucosal cells, perhaps through binding to surface-bound secretory component (SC). Indeed, radiolabeled s-IgA containing bound SC is not transported to secretions after intravenous administration(8). However, the absolute requirement for s-IgA to be regionally produced remains to be explained. It is known that systemic plasma cells can produce dimeric IgA with J-chain, as demonstrated in humans and dogs with IgA myeloma (9,10), and there is no reason to believe that this is an exclusive characteristic of malignant IgA-producing plasma cells. Thus, it is difficult to postulate any mechanism that would exclude these molecules from mucosal transport.


Saliva Sample Secretory Component External Secretion Monoclonal Component Relative Clearance 
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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Gabriel Virella
    • 1
  • Paul C. Montgomery
    • 2
  • Isabel M. Lemaitre-Coelho
    • 3
  1. 1.Department of Basic and Clinical Immunology and MicrobiologyMedical University of South CarolinaCharlestonUSA
  2. 2.Department of Microbiology and Center for Oral Health ResearchUniversity of Pennsylvania School of Dental MedicinePhiladelphiaUSA
  3. 3.Institute of Cellular Pathology, Unit of Experimental MedicineUniversity of LouvainBrusselsBelgium

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