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© The Rockefeller University Press, 0021-9525/1998//203 $5.00
The Journal of Cell Biology, Volume 142, Number 1, , 1998 203-216

Articles

Involvement of Receptor-like Protein Tyrosine Phosphatase {zeta}/RPTPβ and Its Ligand Pleiotrophin/Heparin-binding Growth-associated Molecule (HB-GAM) in Neuronal Migration



Nobuaki Maeda and Masaharu Noda

Division of Molecular Neurobiology, National Institute for Basic Biology, and Department of Molecular Biomechanics, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan

Pleiotrophin/heparin-binding growth-associated molecule (HB-GAM) is a specific ligand of protein tyrosine phosphatase {zeta} (PTP{zeta})/receptor-like protein tyrosine phosphatase β (RPTPβ) expressed in the brain as a chondroitin sulfate proteoglycan. Pleiotrophin and PTP{zeta} isoforms are localized along the radial glial fibers, a scaffold for neuronal migration, suggesting that these molecules are involved in migratory processes of neurons during brain development. In this study, we examined the roles of pleiotrophin-PTP{zeta} interaction in the neuronal migration using cell migration assay systems with glass fibers and Boyden chambers. Pleiotrophin and poly-L-lysine coated on the substratums stimulated cell migration of cortical neurons, while laminin, fibronectin, and tenascin exerted almost no effect. Pleiotrophin-induced and poly-L-lysine–induced neuronal migrations showed significant differences in sensitivity to various molecules and reagents. Polyclonal antibodies against the extracellular domain of PTP{zeta}, PTP{zeta}-S, an extracellular secreted form of PTP{zeta}, and sodium vanadate, a protein tyrosine phosphatase inhibitor, added into the culture medium strongly suppressed specifically the pleiotrophin-induced neuronal migration. Furthermore, chondroitin sulfate C but not chondroitin sulfate A inhibited pleiotrophin-induced neuronal migration, in good accordance with our previous findings that chondroitin sulfate constitutes a part of the pleiotrophin-binding site of PTP{zeta}, and PTP{zeta}-pleiotrophin binding is inhibited by chondroitin sulfate C but not by chondroitin sulfate A. Immunocytochemical analysis indicated that the transmembrane forms of PTP{zeta} are expressed on the migrating neurons especially at the lamellipodia along the leading processes. These results suggest that PTP{zeta} is involved in the neuronal migration as a neuronal receptor of pleiotrophin distributed along radial glial fibers.

Key Words: PTP{zeta} • pleiotrophin • neuronal migration • receptor-like protein tyrosine phosphatase • proteoglycan

Abbreviations used in this paper: anti-NFH, anti-highly phosphorylated neurofilament; CMF-HBSS, Ca2+- and Mg2+-free Hanks' balanced salt solution; CNS, central nervous system; E, embryonic day; HB-GAM, heparin-binding growth-associated molecule; MAP, microtubule-associated protein; PTP, protein tyrosine phosphatase; RPTP, receptor-like PTP; SA-HRP, streptavidin-conjugated horseradish peroxidase.

Address all correspondence to Dr. Masaharu Noda, Division of Molecular Neurobiology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji-cho, Okazaki 444-8585, Japan. Tel.: 81 564 55-7590. Fax: 81 564 55-7595. E-mail: madon{at}nibb.ac.jp


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