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Blood, 15 July 2001, Vol. 98, No. 2, pp. 374-382
IMMUNOBIOLOGY
The functional interactions between CD98,  1-integrins, and
CD147 in the induction of U937 homotypic aggregation
Jae Youl Cho,
David A. Fox,
Vaclav Horejsi,
Kimitaka Sagawa,
Keith M. Skubitz,
David
R. Katz, and
Benjamin Chain
From the Department of Immunology, Windeyer Institute of
Medical Sciences, University College London, England; Department of
Internal Medicine, University of Michigan, Ann Arbor; Institute of
Molecular Genetics, Academy of Sciences of the Czech Republic, Prague;
Department of Transfusion Medicine, Kurume University, Kurume, Fukouka,
Japan; and the University of Minnesota, Minnesota Medical School,
University Hospital, Minneapolis.
CD98 is expressed on both hematopoietic and nonhematopoietic
cells and has been implicated in a variety of different aspects of cell
physiology and immunobiology. In this study, the functional interactions between CD98 and other adhesion molecules on the surface
of the promonocyte line U937 are examined by means of a quantitative
assay of cell aggregation. Several of the CD98 antibodies induced
homotypic aggregation of these cells without affecting cellular
viability or growth. Aggregation induced by CD98 antibodies could
be distinguished from that induced by  1-integrin (CD29)
ligation by lack of sensitivity to EDTA and by increased sensitivity to deoxyglucose. Aggregation induced via CD98
and CD29 could also be distinguished by the pattern of protein tyrosine phosphorylation induced. Some CD29 antibodies partially inhibited CD98-induced aggregation, and these antibodies were neither agonistic for aggregation nor inhibitors of 1-integrin binding to substrates. Conversely, some CD98 antibodies were potent inhibitors of
CD29-induced aggregation. Antibodies to 2 integrins also
partially inhibited CD98-induced aggregation. Unexpectedly, 2 antibodies to CD147, an immunoglobulin superfamily member whose
function has remained unclear, were also potent inhibitors of both the
aggregation and the protein tyrosine phosphorylation induced via CD98
ligation. The results of this study support a central role for CD98
within a multimolecular unit that regulates cell aggregation.
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