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5ß1 Integrin and Regulates Adhesion of Human T Cell Leukemia Virus Type 1-Infected T Cells to Fibronectin1
First Department of Internal Medicine, Ehime University School of Medicine, Shigenobu, Ehime, Japan
In this study we have analyzed the adhesion molecules
associated with and the biologic function of SFA-1/PETA-3 (CD151) in
human T cell leukemia virus type 1 (HTLV-1)-infected T cells and in
freshly isolated adult T cell leukemia (ATL) cells using an
anti-CD151 mAb. The anti-CD151 mAb coprecipitated
5ß1 integrin from HTLV-1-infected T cells.
Conversely, an anti-5 integrin mAb coprecipitated
CD151. The anti-CD151 mAb inhibited the adhesion of HTLV-1-infected
T cells to fibronectin but did not have any effect on their adhesion to
laminin, collagen type I, or collagen type IV. Moreover, antisense
CD151 oligonucleotide-treated HTLV-1-infected T cells showed
significant inhibition of adhesion to fibronectin. These findings
showed that the CD151 molecule was associated with the
5ß1 integrin molecule and that it enhanced
5ß1 integrin-mediated adhesion to
fibronectin. In addition, the expression levels of CD151,
4ß1 integrin, and
5ß1 integrin on ATL cells from lymph nodes
of lymphoma-type ATL patients were significantly higher than those on
circulating ATL cells from leukemia-type ATL patients. This suggests
that the increased expression of these integrins may contribute to
lymphoma formation through the adhesion of ATL cells to the
extracellular matrix and dendritic cells, rather than contributing to
transmigration.
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