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Differential activation-dependent regulation of integrin function in
cultured human T-leukemic cell lines
JL Mobley, E Ennis and Y Shimizu
Department of Microbiology and Immunology, University of Michigan Medical
School, Ann Arbor 48109-0620.
T lymphocytes isolated from human peripheral blood express beta 1 (VLA) and
LFA-1 integrins, but strong binding to integrin ligands occurs only after
the delivery of an activation stimulus to the T cell. To gain further
insight into activation-dependent regulation of integrin function, we have
analyzed integrin activity on three different T- leukemic cell lines:
Jurkat, CEM, and H9. This analysis shows important mechanistic differences
in integrin regulation. First, phorbol ester treatment results in increased
beta 1 integrin-dependent adhesion of both Jurkat and CEM cells to
fibronectin, but decreased adhesion of H9 cells. Second, certain activation
stimuli that upregulate beta 1 integrin activity in peripheral T cells are
nonfunctional in these T- cell lines. Third, analysis of a panel of Jurkat
mutants lacking surface expression of CD2 and/or CD3 shows that
CD2-mediated upregulation of beta 1 integrin activity is dependent on
expression of CD3, whereas CD28-mediated upregulation is not dependent on
either CD2 or CD3 expression. Fourth, all T-cell lines tested show an
inability to adhere to purified ICAM-1 via LFA-1. The selective alterations
in integrin regulation in these cell lines relative to peripheral blood T
cells provide important insights into the intracellular processes involved
in integrin activation.
Volume 83,
Issue 4,
pp. 1039-1050,
02/15/1994
Copyright © 1994 by The American Society of Hematology
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