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First published online 5 October 2004
doi: 10.1242/jcs.01423

Journal of Cell Science 117, 5405-5415 (2004)
Published by The Company of Biologists 2004
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Research Article

{alpha}4ß1- and {alpha}6ß1-integrins are functional receptors for midkine, a heparin-binding growth factor

Hisako Muramatsu1, Peng Zou1, Hiromichi Suzuki1, Yoshihiro Oda1, Guo-Yun Chen1, Nahoko Sakaguchi1, Sadatoshi Sakuma2, Nobuaki Maeda3,4, Masaharu Noda3, Yoshikazu Takada5 and Takashi Muramatsu1,*

1 Department of Biochemistry and Division of Disease Models, Center for Neural Disease and Cancer, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan
2 Cell Signals, 75-1 Ono-cho, Tsurumi-ku, Yokohama 230-0046, Japan
3 Division of Molecular Neurobiology, National Institute for Basic Biology, Myodaiji-cho, Okazaki 444-8585, Japan
4 Department of Developmental Neuroscience, Tokyo Metropolitan Institute for Neuroscience, 2-6 Musashidai, Fuchu, Tokyo 183-8526, Japan
5 University of California Davis Medical Center, 4645 2nd Avenue, Sacramento, CA 95817, USA

* Author for correspondence (e-mail: tmurama{at}med.nagoya-u.ac.jp)

Accepted 29 July 2004

Midkine is a heparin-binding growth factor that promotes the growth, survival, migration and differentiation of various target cells. So far, receptor-type protein tyrosine phosphatase {zeta}, low-density-lipoprotein-receptor-related protein and anaplastic lymphoma kinase have been identified as receptors for midkine. We found ß1 integrin in midkine-binding proteins from 13-day-old mouse embryos. ß1-Integrin bound to a midkine-agarose column and was eluted mostly with EDTA. Further study revealed that the {alpha}-subunits capable of binding to midkine were {alpha}4 and {alpha}6. Purified {alpha}4ß1- and {alpha}6ß1-integrins bound midkine. Anti-{alpha}4 antibody inhibited the midkine-dependent migration of osteoblastic cells, and anti-{alpha}6 antibody inhibited the midkine-dependent neurite outgrowth of embryonic neurons. After midkine treatment, tyrosine phosphorylation of paxillin, an integrin-associated molecule, was transiently increased in osteoblastic cells. Therefore, we concluded that {alpha}4ß1- and {alpha}6ß1-integrins are functional receptors for midkine. We observed that the low-density-lipoprotein-receptor-related-protein-6 ectodomain was immunoprecipitated with {alpha}6ß1-integrin and {alpha}4ß1-integrin. The low-density-lipoprotein-receptor-related-protein-6 ectodomain was also immunoprecipitated with receptor-type protein tyrosine phosphatase {zeta}. {alpha}4ß1- and {alpha}6ß1-Integrins are expected to co-operate with other midkine receptors, possibly in a multimolecular complex that contains other midkine receptors.

Key words: Cell migration, Growth factor, Integrin, LDL-receptor related protein, Midkine




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