title: Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory ensheathing glia, a growth-promoting class of macroglia.
abstract: The molecular mechanisms that drive glia-glial interactions and glia-neuronal interactions during the development of the nervous system are poorly understood. A number of membrane-bound cell adhesion molecules have been shown to play a role, although the precise nature of their involvement is unknown. One class of molecules with cell adhesive properties used in the nervous system is the serine-esterase-like family of transmembrane proteins. A member of this class, a glia-specific protein called gliotactin, has been shown to be necessary for the development of the glial sheath in the peripheral nervous system of Drosophila melanogaster. Gliotactin is essential for the development of septate junctions in the glial sheath of individual and neighboring glia. Mutations that remove this protein result in paralysis and eventually death due to a breakdown in the glial-based blood-nerve barrier. To study the role of gliotactin during vertebrate nervous system development, we have isolated a potential vertebrate gliotactin homologue from mice and rat and found that it corresponds to neuroligin 3. Using a combination of RT-PCR and immunohistochemistry, we have found that neuroligin 3 is expressed during the development of the nervous system in many classes of glia. In particular neuroligin 3 is expressed in the olfactory ensheathing glia, retinal astrocytes, Schwann cells, and spinal cord astrocytes in the developing embryo. This expression is developmentally controlled such that in postnatal and adult stages, neuroligin 3 continues to be expressed at high levels in the olfactory ensheathing glia, a highly plastic class of glia that retain many of their developmental characteristics throughout life.
authors.affiliation: Department of Zoology, University of British Columbia, Vancouver, Canada.
authors.forename: M
authors.initials: M
authors.lastname: Gilbert
authors.forename: J
authors.initials: J
authors.lastname: Smith
authors.forename: A J
authors.initials: AJ
authors.lastname: Roskams
authors.forename: V J
authors.initials: VJ
authors.lastname: Auld
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D001253:Astrocytes / Q000166:cytology / Q000378:metabolism; D001369:Axons / Q000378:metabolism* / Q000648:ultrastructure; D015816:Cell Adhesion Molecules, Neuronal; D002454:Cell Differentiation / Q000502:physiology*; D004331:Drosophila melanogaster / Q000254:growth & development / Q000378:metabolism; D004950:Esterases / Q000378:metabolism; D005727:Ganglia, Spinal / Q000166:cytology / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental / Q000502:physiology; D006133:Growth Substances / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009420:Nervous System / Q000166:cytology / Q000254:growth & development* / Q000378:metabolism; D009457:Neuroglia / Q000378:metabolism*; D009474:Neurons / Q000378:metabolism; D009830:Olfactory Bulb / Q000166:cytology / Q000254:growth & development / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D012160:Retina / Q000166:cytology / Q000378:metabolism; D012583:Schwann Cells / Q000166:cytology / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013116:Spinal Cord / Q000166:cytology / Q000378:metabolism; D014714:Vertebrates / Q000033:anatomy & histology / Q000378:metabolism
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; D006133:Growth Substances; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C094064:gliotactin; C098004:neuroligin 3; D004950:Esterases; C022635:serine esterase