title: Cell surface expression of polysialic acid on NCAM is a prerequisite for activity-dependent morphological neuronal and glial plasticity.
abstract: Polysialic acid (PSA) on the extracellular domain of the neural cell adhesion molecule (NCAM) reduces cell adhesion and is considered an important regulator of cell surface interactions. The hypothalamo-neurohypophysial system (HNS), whose glia, neurons, and synapses undergo striking, reversible morphological changes in response to physiological stimulation, expresses high levels of PSA-NCAM throughout life. Light and electron microscopic immunocytochemistry in normal rats and rats in which cell transport was blocked with colchicine showed that PSA-NCAM is expressed in both HNS neurons and glia, particularly at the level of astrocytic processes that envelop neuronal profiles and can undergo remodeling. Moreover, we confirmed that the overall levels of PSA-NCAM were not greatly altered by stimulation (lactation and chronic salt ingestion). Nevertheless, PSA is essential to morphological plasticity. Using comparative ultrastructural analysis, we found that, after specific enzymatic removal of PSA from NCAM by microinjection of endoneuraminidase close to the hypothalamic magnocellular nuclei in vivo, there was no apparent withdrawal of astrocytic processes nor any increase in synaptic contacts normally induced by lactation and dehydration. Our observations demonstrate, therefore, that expression of PSA on cell surfaces in the adult HNS is indispensable to its capacity for activity-dependent morphological neuronal-glial and synaptic plasticity. The carbohydrate PSA on NCAM can thus be considered a necessary permissive factor to allow neuronal and glial remodeling to occur whenever the proper inductive stimulus intervenes.
authors.affiliation: Institut National de la Santé et de la Recherche Médicale U378, Institut François Magendie Université Victor Segalen Bordeaux II, F33077 Bordeaux, France. dionysia.theodosis@bordeaux.inserm.fr
authors.forename: D T
authors.initials: DT
authors.lastname: Theodosis
authors.forename: R
authors.initials: R
authors.lastname: Bonhomme
authors.forename: S
authors.initials: S
authors.lastname: Vitiello
authors.forename: G
authors.initials: G
authors.lastname: Rougon
authors.forename: D A
authors.initials: DA
authors.lastname: Poulain
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D005260:Female; D006026:Glycoside Hydrolases / Q000493:pharmacokinetics / Q000494:pharmacology; D007030:Hypothalamo-Hypophyseal System / Q000166:cytology / Q000378:metabolism; D008297:Male; D019006:Neural Cell Adhesion Molecules / Q000378:metabolism*; D009457:Neuroglia / Q000378:metabolism / Q000502:physiology*; D009473:Neuronal Plasticity / Q000502:physiology*; D009474:Neurons / Q000378:metabolism / Q000502:physiology*; D010904:Pituitary Gland, Posterior / Q000166:cytology / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D012794:Sialic Acids / Q000378:metabolism*; D013495:Supraoptic Nucleus / Q000187:drug effects / Q000378:metabolism
chemical_list: D019006:Neural Cell Adhesion Molecules; D012794:Sialic Acids; C021319:polysialic acid; D006026:Glycoside Hydrolases; C090534:endo-alpha-sialidase