Midkine binds to 37-kDa laminin binding protein precursor, leading to nuclear transport of the complex.
Midkine ( MK) is a heparin binding multifunctional protein that promotes cell survival and cell migration. MK was found to bind to 37-kDa laminin binding protein precursor ( LBP), a precursor of 67-kDa laminin receptor, with K(d) of 1.1 nM between MK and LBP-glutathione-S-transferase fusion protein. The binding was inhibited by laminin, anti- LBP, amyloid beta-peptide, and heparin; the latter two are known to bind to MK. In CMT-93 mouse rectal carcinoma cells, LBP was mostly located in the cytoplasm as revealed by immunostaining with anti- LBP antibody. That a portion of LBP or 67-kDa laminin receptor was located at the surface of these cells was verified by inhibition of cell attachment to laminin-coated dishes by anti- LBP antibody. When MK was added to culture medium of these cells, a part of LBP migrated to the nucleus. The movement occurred concomitantly with nuclear transport of biotin-labeled MK. These findings suggested that the binding of MK to LBP caused nuclear translocation of the molecular complex.[1]References
- Midkine binds to 37-kDa laminin binding protein precursor, leading to nuclear transport of the complex. Salama, R.H., Muramatsu, H., Zou, K., Inui, T., Kimura, T., Muramatsu, T. Exp. Cell Res. (2001) [Pubmed]
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