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*
Department of Pathology, New York University School of Medicine and Kaplan Cancer Center, New York, NY 10016;
Department of Immunology and Medical Genetics, University of Toronto, Toronto, Ontario, Canada;
Boston University Medical Center, Boston, MA 02118;
§
Department of Immunology, University of Toronto, Toronto, Ontario, Canada;
¶
Department of Pathology, McMaster University, Hamilton, Ontario, Canada; and
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Division of Immunology and Allergy, University Hospital, Lausanne, Switzerland
T560, a mouse B lymphoma that originated in gut-associated lymphoid
tissue, expresses receptors that bind dimeric IgA and IgM in a mutually
inhibitory manner but have little affinity for monomeric IgA. Evidence
presented in this paper indicates that the receptor is poly-Ig receptor
(pIgR) known in humans and domestic cattle to bind both IgA and IgM.
The evidence includes the demonstration that binding of IgM is J chain
dependent, and that pIg-precipitated receptor has an appropriate
Mr of 116120 kDa and can be detected on
immunoblots with specific rabbit anti-mouse pIgR. Overlapping
RT-PCR performed using template mRNA from T560 cells and
oligonucleotide primer pairs designed from the published sequence of
mouse liver pIgR indicate that T560 cells express mRNA virtually
identical with that of the epithelial cell pIgR throughout its
external, transmembrane, and intracytoplasmic coding regions. Studies
using mutant IgAs suggest that the C
2 domain of dimeric IgA is not
involved in high-affinity binding to the T560 pIgR. Inasmuch as this
mouse B cell pIgR binds IgM better than IgA, it is similar to human
pIgR and differs from rat, mouse, and rabbit epithelial cell pIgRs that
bind IgA but not IgM. Possible explanations for this difference are
discussed. All clones of T560 contain some cells that spontaneously
secrete both IgG2a and IgA, but all of the IgA recoverable from the
medium and from cell lysates is monomeric; it cannot be converted to
secretory IgA by T560 cells.
This article has been cited by other articles:
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