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Expression of integrins and examination of their adhesive function in
normal and leukemic hematopoietic cells
JL Liesveld, JM Winslow, KE Frediani, DH Ryan and CN Abboud
Hematology Unit, University of Rochester Medical Center, NY 14642.
Adhesion of hematopoietic progenitor cells to marrow-derived adherent cells
has been noted for erythroid, myeloid, and lymphoid precursors. In this
report, we have characterized very late antigen (VLA) integrin expression
on normal CD34+ marrow progenitors, on leukemic cell lines, and on blasts
from patients with acute myelogenous or monocytic leukemias. CD34+
progenitor cells expressed the integrin beta 1 chain (CD29), VLA-4 alpha
(CD49d), and VLA-5 alpha (CD49e). The myeloid lines KG1 and KG1a also
expressed CD49d and CD49e as did the Mo7e megakaryoblastic line. CD29,
CD18, and CD11a were also present on each of these cell lines. Only the
Mo7e line expressed the cytoadhesins GPIIbIIIa or GPIb. Binding of KG1a to
marrow stroma was partially inhibited by antibodies to CD49d and its
ligand, vascular cell adhesion molecule (VCAM-1). The majority of leukemic
blasts studied expressed CD49d and CD49e as well. Blasts from patients with
acute myelomonocytic leukemia consistently bound to stroma at levels
greater than 20%, and adhesion to stroma could in some cases be partly
inhibited by anti- CD49d. No role for glycosylphosphatidyl-inositol
(GPI)-linked structures was demonstrated in these binding assays because
the adhesion of leukemic blasts to stroma was not diminished after
treatment with phosphatidylinositol-specific phospholipase C (PI-PLC).
These studies indicate that CD34+ myeloid progenitors, myeloid leukemic
cell lines, and leukemic blasts possess a similar array of VLA integrins.
Their functional importance individually or in combination with other
mediators of attachment in adhesion, transendothelial migration, and
differentiation has yet to be fully elucidated.
Volume 81,
Issue 1,
pp. 112-121,
01/01/1993
Copyright © 1993 by The American Society of Hematology
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