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* Veterinary Molecular Biology, Montana State University, Bozeman, MT 59717; and
Department of Pathology, University of Michigan School of Medicine, Ann Arbor, MI 48109
Previous studies reported that L-selectin (CD62L) on human
peripheral blood neutrophils serves as an E-selectin ligand. This study
shows that CD62L acquired E-selectin-binding activity following phorbol
ester (PMA) treatment of the Jurkat T cell line and
anti-CD3/IL-2-driven proliferation of human T lymphocytes in vitro.
The recombinant porcine E-selectin/human Ig chimera P11.4 showed
neuraminidase-sensitive and calcium-dependent attachment to
PMA-stimulated human Jurkat T cells in a flow cytometry assay. The
anti-CD62L mAb (DREG 56) blocked this binding interaction by
60% and P11.4 precipitated CD62L from detergent lysates of
PMA-activated Jurkat cells. In contrast, P11.4 precipitated minimal
amounts of CD62L from detergent lysates of nonactivated human PBL. As
reported previously, P-selectin glycoprotein ligand 1 and a distinct
130-kDa glycoprotein were the major species in these precipitates.
However, T cell activation on plate-immobilized anti-CD3 and growth
in low-dose IL-2 increased the percentage of CD62L molecules with
E-selectin-binding activity. After two cycles of activation and
culture, 60–70% of the CD62L was precipitated with the P11.4
chimera. These cultured T lymphoblasts rolled avidly on both E-selectin
and P-selectin at physiologic levels of linear shear stress. The DREG
56 Ab partially blocked rolling on the E-selectin substrate, whereas no
effect was seen on P-selectin. Thus, CD62L on human cultured T
lymphoblasts is one of several glycoproteins that interacts directly
with E-selectin and contributes to rolling under
flow.
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