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*
Gastroenterology Division, Brigham and Women’s Hospital, and
Departments of Medicine and Pathology, and
Combined Program in Pediatric Gastroenterology and Nutrition, Children’s Hospital, Harvard Medical School, Boston, MA 02115; and
Department of Medicine, University of Alabama and Veteran’s Affairs Medical Center, Birmingham, AL 35294
The neonatal Fc receptor (FcRn) for IgG, an MHC class I-related
molecule, functions to transport IgG across polarized epithelial cells
and protect IgG from degradation. However, little is known about
whether FcRn is functionally expressed in immune cells. We show here
that FcRn mRNA was identifiable in human monocytes, macrophages, and
dendritic cells. FcRn heavy chain was detectable as a 45-kDa protein in
monocytic U937 and THP-1 cells and in purified human intestinal
macrophages, peripheral blood monocytes, and dendritic cells by Western
blot analysis. FcRn colocalized in vivo with macrosialin (CD68) and
Ncl-Macro, two macrophage markers, in the lamina propria of human small
intestine. The heavy chain of FcRn was associated with the
2-microglobulin (2m) light chain in U937
and THP-1 cells. FcRn bound human IgG at pH 6.0, but not at pH 7.5.
This binding could be inhibited by human IgG Fc, but not Fab. FcRn
could be detected on the cell surface of activated, but not resting,
THP-1 cells. Furthermore, FcRn was uniformly present intracellularly in
all blood monocytes and intestinal macrophages. FcRn was detectable on
the cell surface of a significant fraction of monocytes at lower levels
and on a small subset of tissue macrophages that expressed high levels
of FcRn on the cell surface. These data show that FcRn is functionally
expressed and its cellular distribution is regulated in monocytes,
macrophages, and dendritic cells, suggesting that it may confer novel
IgG binding functions upon these cell types relative to typical
Fc
Rs: FcRI, FcRII, and FcRIII.
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