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E(CD103)
7 Mediates Adhesion to Intestinal Microvascular Endothelial Cell Lines Via an E-Cadherin-Independent Interaction1
*
The Lymphocyte Biology Section, Division of Rheumatology, Immunology, and Allergy, and
Pulmonary and Critical Care Division, Brigham and Women’s Hospital, Boston, MA 02115; and
Medical College of Wisconsin, Milwaukee, WI 53226
Integrins are important for T cell interactions with endothelial
cells. Because the integrin 
E
7 is
expressed on some circulating gut-homing T cells and as T cell numbers
are reduced in the intestinal lamina propria of
E-deficient mice, we evaluated whether
E7 mediates binding to intestinal
endothelial cells. We found that
anti-E7 mAbs partially blocked the
binding of cultured intraepithelial T cells to human intestinal
microvascular endothelial cells (HIMEC). Furthermore,
E7-transfected K562 cells bound more
efficiently than vector-transfected K562 cells to HIMEC. Finally, HIMEC
bound directly to an E7-Fc fusion
protein. These interactions were partially blocked by
anti-E7 mAbs, and endothelial cell
binding to the E7-Fc was dependent upon
the metal ion-dependent adhesion site within the E A
domain. Of note, the HIMEC lacked expression of E-cadherin, the only
known E7 counterreceptor as assessed by
functional studies, flow cytometry, and RT-PCR. Thus,
HIMEC/E7 binding was independent of
E-cadherin. In addition, this interaction appeared to be tissue
selective, as HIMEC bound to the E7-Fc,
whereas microvascular endothelial cells from the skin did not. Finally,
there was evidence for an E7 ligand on
intestinal endothelial cells in vivo, as
E7 expression enhanced lymphocyte binding
around vessels in the lamina propria in tissue sections. Thus, we have
defined a novel interaction for E7 at a
nonepithelial location. These studies suggest a role for
E7 in interactions with the intestinal
endothelium that may have implications for intestinal T cell homing or
functional responses.
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