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Blood, 15 April 2005, Vol. 105, No. 8, pp. 3295-3302.
Prepublished online as a Blood First Edition Paper on December 30, 2004; DOI 10.1182/blood-2004-10-4083.
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NEOPLASIA
A rapid translocation of CD45RO but not CD45RA to lipid rafts in IL-6-induced proliferation in myeloma
Fu-Jun Li,
Naohiro Tsuyama,
Hideaki Ishikawa,
Masanori Obata,
Saeid Abroun,
Shangqin Liu,
Ken-ichiro Otsuyama,
Xu Zheng,
Zi Ma,
Yasuko Maki, and
Michio M. Kawano
From the Department of Bio-Signal Analysis, Graduate School of Medicine, Yamaguchi University, Ube, Yamaguchi, Japan.
CD45, a receptor-type tyrosine phosphatase, is required for interleukin-6 (IL-6)-induced proliferation in human myeloma cells, which express the shortest isoform, CD45RO, but not the longest isoform, CD45RA. Here, we showed that IL-6 induced the translocation of CD45 to lipid rafts in an isoform-dependent manner. In myeloma cells, CD45RO was translocated to lipid rafts more rapidly than CD45RB, but exogenously expressed CD45RA was not translocated. When an IL-6R -transfected B-cell line was stimulated with IL-6, CD45RA was not translocated, although CD45RB was. We further confirmed that the translocated CD45 bound to IL-6R, Lyn, and flotillin-2, and this was followed by the dephosphorylation of the negative regulatory Tyr507 of Lyn. CD45 also bound to phosphoprotein associated with glycosphingolipid-enriched microdomains (PAGs), which were subsequently dephosphorylated, resulting in the release of C-terminal src kinase (Csk) from lipid rafts. Therefore, these results indicate that a rapid translocation of CD45RO to lipid rafts may be responsible for IL-6-induced proliferation, and that the change from CD45RA to CD45RO confers the ability to respond to IL-6 in human myeloma cells. (Blood. 2005;105:3295-3302)
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