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*
Centre for Molecular Medicine and Therapeutics, British Columbia Research Institute for Children’s and Women’s Health, and Department of Medicine, University of British Columbia, Vancouver, British Columbia, Canada; and
Department of Infectious Diseases, Washington University School of Medicine, St. Louis, MO 63110
SHPS-1 (SH2-domain bearing protein tyrosine phosphatase (SHP)
substrate-1), a member of the inhibitory-receptor superfamily that is
abundantly expressed in macrophages and neural tissue, appears to
regulate intracellular signaling events downstream of receptor
protein-tyrosine kinases and integrin-extracellular matrix molecule
interactions. To investigate the function of SHPS-1 in a hematopoietic
cell line, SHPS-1 was expressed in Ba/F3 cells, an IL-3-dependent
pro-B-cell line that lacks endogenous SHPS-1 protein. Interestingly,
expression of either SHPS-1, or a mutant lacking the intracellular
domain of SHPS-1 (
CT SHPS-1), resulted in the rapid formation of
macroscopic Ba/F3 cell aggregates. As the integrin-associated
protein/CD47 was shown to be a SHPS-1 ligand in neural cells, we
investigated whether CD47 played a role in the aggregation of
SHPS-1-expressing Ba/F3 cells. In support of this idea, aggregate
formation was inhibited by an anti-CD47 Ab. Furthermore,
erythrocytes from control, but not from CD47-deficient mice, were able
to form rosettes on SHPS-1-expressing Ba/F3 cells. Because erythrocytes
do not express integrins, this result suggested that SHPS-1-CD47
interactions can take place in the absence of a CD47-integrin
association. We also present evidence that the amino-terminal Ig domain
of SHPS-1 mediates the interaction with CD47. Although SHPS-1-CD47
binding likely triggers bidirectional intracellular signaling
processes, these results demonstrate that this interaction can also
mediate cell-cell adhesion.
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