Expression of ezrin in glial tubes in the adult subventricular zone and rostral migratory stream.
Ezrin is a member of the ERM (ezrin-radixin-moesin) family of membrane-cytoskeletal linking proteins. ERM proteins are involved in a wide variety of cellular functions including cell motility, signal transduction, cell-cell interaction and cell-matrix recognition. A recent in situ hybridization study showed that the mRNA encoding ezrin is expressed in neurogenic regions of the mature brain including the subventricular zone (SVZ) and rostral migratory stream (RMS); however, the specific cell types expressing ezrin and their relationship to migrating and proliferating cells in these regions have not been characterized previously. In this study, we used immunocytochemistry to perform double labeling with a variety of cell-type specific markers to characterize the expression of ezrin in the SVZ and RMS of adult mice. Ezrin was expressed at high levels in both the SVZ and RMS where ezrin-immunopositive processes formed a trabecular network surrounding the proliferating and migrating cells. Ezrin-positive cells co-labeled with the glial makers S100beta and GFAP (glial fibrillary acidic protein), but only minimally with the early neuronal markers beta III tubulin and polysialylated form of neural cell adhesion molecule 1 (PSA-NCAM), indicating that ezrin was expressed primarily in the glial tube cells. Ezrin positive cells also expressed beta-catenin, a membrane-complex protein previously implicated in the regulation of stem-cell proliferation and neuronal migration. Glial tube cells act as both precursors of, and a physical channel for, migrating neuroblasts. Bi-directional signals between glial tube cells and migrating neuroblasts have been shown to regulate the rates of both proliferation of the precursor cells and migration of the newly generated neuroblasts. Our finding that ezrin and beta-catenin are both present at the cell membrane of the glial tube cells suggests that these proteins may be involved in those signaling processes.
Cleary
M A
MA
Department of Psychiatry, Yale University School of Medicine, 300 George Street, 8304, New Haven, CT 06511, USA.
Uboha
N
N
Picciotto
M R
MR
Beech
R D
RD
D000818:Animals; D015153:Blotting, Western; D001973:Bromodeoxyuridine / Q000378:metabolism; D002465:Cell Movement / Q000502:physiology*; D049109:Cell Proliferation; D002552:Cerebral Ventricles / Q000166:cytology*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D004525:Efferent Pathways / Q000378:metabolism*; D015870:Gene Expression / Q000502:physiology*; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D007150:Immunohistochemistry / Q000379:methods; D051379:Mice; D009414:Nerve Growth Factors / Q000378:metabolism; D039842:Neural Cell Adhesion Molecule L1 / Q000378:metabolism; D009457:Neuroglia / Q000378:metabolism*; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins / Q000378:metabolism; D012794:Sialic Acids / Q000378:metabolism; D014404:Tubulin / Q000378:metabolism; D051176:beta Catenin / Q000378:metabolism; D000099149:Ezrin
D001973:Bromodeoxyuridine; D003598:Cytoskeletal Proteins; D005904:Glial Fibrillary Acidic Protein; D009414:Nerve Growth Factors; D039842:Neural Cell Adhesion Molecule L1; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins; D012794:Sialic Acids; D014404:Tubulin; D051176:beta Catenin; D000099149:Ezrin; C462941:beta3 tubulin, mouse; C103469:polysialyl neural cell adhesion molecule