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Blood, Vol. 96 No. 1 (July 1), 2000:
pp. 234-241
Integrin-associated protein/CD47 regulates motile activity in
human B-cell lines through CDC42
Hitoshi Yoshida,
Yoshiaki Tomiyama,
Jun Ishikawa,
Kenji Oritani,
Itaru Matsumura,
Masamichi Shiraga,
Takafumi Yokota,
Yu Okajima,
Megumu Ogawa,
Jun-ichiro Miyagawa,
Tetsuo Nishiura, and
Yuji Matsuzawa
From the Department of Internal Medicine and Molecular Science and
the Department of Hematology and Oncology, Osaka University, Suita,
Japan.
Cell migration requires a dynamic interaction between the cell, its
substrate, and the cytoskeleton-associated motile apparatus. Integrin-associated protein (IAP)/CD47 is a 50-kd cell surface protein
that is physically associated with  3 integrins and that modulates
the functions of 3 integrins in various cells. However, in
B-lymphocytes that express 1 integrins but few 3 integrins, the
roles of IAP/CD47 remain to be determined. Cross-linking of IAP/CD47 by
the immobilized anti-IAP/CD47 monoclonal antibody (mAb) B6H12, but not
2D3, produced signals to promote polarization with lamellipodia, a
characteristic morphology during leukocyte migration, in pre-B and
mature B-cell lines (BALL, Nalm6, ONHL-1, Daudi), but not in myeloma
cell lines (RPMI8226, OPM-2). In the presence of the immobilized
fibronectin (FN), soluble B6H12 could increase the rate of the
polarization and activate migratory activity of BALL cells to FN in a
transwell filter assay. Furthermore, the dominant-negative form of
CDC42 completely blocked B6H12-induced morphologic and functional
changes without inhibiting phorbol 12-myristate 13-acetate-induced
spreading on FN in BALL cells, whereas the dominant-negative form of
Rac1 inhibited all these changes. These findings demonstrate that in
B-lymphocytes, IAP/CD47 may transduce the signals to activate the
migratory activity, in which CDC42 may be specifically involved, and
that IAP/CD47 shows synergistic effect with  41 on B-cell
migration. These findings would provide new insight into the role of
IAP/CD47 on B-cell function.
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