94 Virella

Fig. 6.1 Ultrastructure of a mature plasma cell. Note the eccentric nucleus with clumped chromatin,
the large cytoplasm containing abundant, distended, endoplasmic reticulum. (Electron microphoto-
graph courtesy of Professor P. Groscurth, M. D., Institute of Anatomy, University of Zurich, Switzer-
land.)

chains are synthesized, transported to the endoplasmic reticulum, where they are glycosy-
lated, but secretion requires association to light chains to form a complete immunoglobu-
lin molecule. If light chains are not synthesized or heavy chains are synthesized in excess,
the free heavy chains associate via their CH1 domain with a heavy-chain binding protein,
which is believed to be responsible for their intracytoplasmic retention. In rare cases, the
free heavy chains are structurally abnormal and are secreted. Free heavy chains are usually
retained in circulation because of their molecular weight—about twice that of light chains.
Polymeric immunoglobulins (IgM, IgA) have one additional polypeptide chain, the J
chain. This chain is synthesized by all plasma cells, including those that produce IgG. How-
ever, it is only incorporated to polymeric forms of IgM and IgA. It is thought that the J chain
has some role in initiating polymerization, as shown in Figure 6.2. IgM proteins are as-
sembled in two steps. First, the monomeric units are assembled. Then, five monomers and
one J chain will be combined via covalent bonds to result in the final pentameric molecule.
This assembly seems to coincide with secretion in some cells in which only monomeric
subunits are found intracellularly. However, in other cells the pentameric forms can be
found intracellularly and secretion seems linked to glycosylation.
Secretory IgA is also assembled in two stages, but each one takes place in a different
cell. Dimeric IgA, containing two monomeric subunits and a J chain joined together by disul-
fide bridges, is predominantly synthesized by submucosal plasma cells, although a minor
portion may also be synthesized in the bone marrow. Secretory component (SC), on the other
hand, is synthesized in the epithelial cells, where the final assembly of secretory IgA takes
place. Two different biological functions have been postulated for the secretory component.
First, SC is responsible for secretion of IgA by mucosal membranes. The process in-
volves uptake of dimeric IgA, assembly of IgA-SC complexes, and secretion by the mu-
cosal cells.
The uptake of dimeric IgA by mucosal cells is mediated by a glycoprotein related to
SC, the polyimmunoglobulin receptor (Poly-IgR). Poly-IgR is constituted by a single