title: Development and migration of Purkinje cells in the mouse cerebellar primordium.
abstract: The mode of Purkinje cell migration in the mouse cerebellar primordium was examined immunohistochemically, by marking Purkinje cells with anti-spot 35 antibody and labeling them with 5'-bromodeoxyuridine. The cells migrated radially from the neuroepithelium of the fourth ventricle towards the cortical surface between the 13th and 17th days (E13-E17) of gestation. Regional differences in the migratory process were evident: the final settlement of the Purkinje cells proceeded earlier in the lateral and posterior parts of the primordium, exhibiting latero-medial and posteroventral-anterodorsal diminishing sequences. To elucidate the factors involved in the migration, the arrangement of radial glial fibers, and expression of the cell adhesion molecule, tenascin, were examined immunohistochemically with the monoclonal antibody 1D11, a marker for both immature and mature astroglia, and an anti-tenascin antibody. At E14, 1D11-immunopositive fibers were seen to extend from the ventricle to the pial surface, and the cell bodies of immature glia migrated after E15 towards the cortex, shortening the radial processes whose end-feet were attached to the pia mater. Tenascin, which possesses a neuron-glial adhesiveness, was also expressed on the radial fibers during the migration of the Purkinje cells. The fibers were closely apposed to the migratory Purkinje cells, and their arrangement and orientation accorded with the migratory direction of the Purkinje cells. Further, changes in the molecular species of antigens detected by both the 1D11 and anti-tenascin antibodies were observed by immunoblotting analysis during the course of cerebellar development. These findings suggest that the arrangement of radial glia and expression of adhesion molecules may be involved in the control and guidance of Purkinje cell migration.
authors.affiliation: Department of Anatomy, School of Medicine, Keio University, Tokyo, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Yuasa
authors.forename: K
authors.initials: K
authors.lastname: Kawamura
authors.forename: K
authors.initials: K
authors.lastname: Ono
authors.forename: T
authors.initials: T
authors.lastname: Yamakuni
authors.forename: Y
authors.initials: Y
authors.lastname: Takahashi
mesh_terms: D000818:Animals; D015153:Blotting, Western; D001973:Bromodeoxyuridine; D064092:Calbindin 1; D064026:Calbindins; D002135:Calcium-Binding Proteins; D015816:Cell Adhesion Molecules, Neuronal / Q000096:biosynthesis; D002465:Cell Movement; D002531:Cerebellum / Q000196:embryology* / Q000378:metabolism / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins / Q000096:biosynthesis; D007150:Immunohistochemistry; D051379:Mice; D008809:Mice, Inbred C3H; D008854:Microscopy, Electron; D009419:Nerve Tissue Proteins / Q000096:biosynthesis; D016900:Neurofilament Proteins / Q000096:biosynthesis; D011689:Purkinje Cells / Q000502:physiology*; D064030:S100 Calcium Binding Protein G; D019063:Tenascin; D014746:Vimentin / Q000096:biosynthesis
chemical_list: C576499:Calb1 protein, mouse; D064092:Calbindin 1; D064026:Calbindins; D002135:Calcium-Binding Proteins; D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D009419:Nerve Tissue Proteins; D016900:Neurofilament Proteins; D064030:S100 Calcium Binding Protein G; D019063:Tenascin; D014746:Vimentin; D001973:Bromodeoxyuridine