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Detection of an L-selectin ligand on a hematopoietic progenitor cell line
SM Oxley and R Sackstein
Division of Bone Marrow Transplantation, H. Lee Moffitt Cancer Center,
University of South Florida College of Medicine, Tampa.
L-selectin, the peripheral lymph node "homing receptor," is an adhesion
protein that mediates lymphocyte binding to lymph node high endothelial
venules. Ligands for this protein have been identified only on endothelial
cells, and recent murine studies indicate that CD34 on endothelial cells is
an L-selectin ligand. To investigate whether CD34 expressed on
hematopoietic cells functions as an L-selectin ligand, we used an in vitro
binding assay to examine lymphocyte adherence to KG1a, a CD34+ human
hematopoietic progenitor cell line. We observed specific
L-selectin-mediated adherence of lymphocytes to KG1a: the binding was
calcium-dependent, was strictly inhibited by anti-L-selectin antibodies and
by carbohydrate ligands of L-selectin, and was abrogated by induction of
L-selectin shedding from the lymphocyte membrane by treatment with phorbol
esters. However, blocking studies using anti- CD34 antibodies, and
experiments using KG1a cells sorted for CD34 expression and COS-7 cells
transfected with full-length CD34 cDNA indicate that the ligand on KG1a is
not CD34; moreover, RPMI 8402, a CD34+ cell line, does not support
lymphocyte adherence in the binding assay. Treatment of KG1a with the
enzymes neuraminidase, chymotrypsin, and bromelain abrogated lymphocyte
binding to the cells, indicating that the ligand is a glycoprotein. These
experiments show that CD34 on hematopoietic cells is not an L-selectin
ligand and provide the first evidence of a ligand for L-selectin present on
a non-endothelial cell.
Volume 84,
Issue 10,
pp. 3299-3306,
11/15/1994
Copyright © 1994 by The American Society of Hematology
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