title: Divergent impact of the polysialyltransferases ST8SiaII and ST8SiaIV on polysialic acid expression in immature neurons and interneurons of the adult cerebral cortex.
abstract: Polysialic acid (PSA) is a negatively charged carbohydrate polymer, which confers antiadhesive properties to the neural cell adhesion molecule NCAM and facilitates cellular plasticity during brain development. In mice, PSA expression decreases drastically during the first postnatal weeks and it gets confined to immature neurons and regions displaying structural plasticity during adulthood. In the brain, PSA is exclusively synthesized by the two polysialyltransferases ST8SiaII and ST8SiaIV. To study their individual contribution to polysialylation in the adult, we analyzed PSA expression in mice deficient for either polysialyltransferase. Focusing on the cerebral cortex, our results indicate that ST8SiaIV is solely responsible for PSA expression in mature interneurons and in most regions of cortical neuropil. By contrast, ST8SiaII is the major polysialyltransferase in immature neurons of the paleocortex layer II and the hippocampal subgranular zone. The numbers of cells expressing PSA or doublecortin, another marker of immature neurons, were increased in the paleocortex layer II of ST8SiaIV-deficient mice, indicating altered differentiation of these cells. Analysis of doublecortin expression also indicated that the production of new granule neurons in the subgranular zone of ST8SiaII-deficient mice is not affected. However, many of the immature granule neurons showed aberrant locations and morphology, suggesting a role of ST8SiaII in their terminal differentiation.
authors.affiliation: Cell Biology Department, Universitat de València, Burjassot, Spain. nacher@uv.es
authors.forename: J
authors.initials: J
authors.lastname: Nacher
authors.forename: R
authors.initials: R
authors.lastname: Guirado
authors.forename: E
authors.initials: E
authors.lastname: Varea
authors.forename: G
authors.initials: G
authors.lastname: Alonso-Llosa
authors.forename: I
authors.initials: I
authors.lastname: Röckle
authors.forename: H
authors.initials: H
authors.lastname: Hildebrandt
mesh_terms: D000818:Animals; D019002:CD56 Antigen / Q000096:biosynthesis; D002454:Cell Differentiation / Q000235:genetics; D002540:Cerebral Cortex / Q000166:cytology / Q000254:growth & development* / Q000378:metabolism*; D000089622:Doublecortin Domain Proteins; D018507:Gene Expression Regulation, Developmental / Q000235:genetics; D006624:Hippocampus / Q000166:cytology / Q000254:growth & development / Q000378:metabolism; D007395:Interneurons / Q000166:cytology / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D055495:Neurogenesis / Q000235:genetics; D009473:Neuronal Plasticity / Q000235:genetics; D009474:Neurons / Q000166:cytology / Q000378:metabolism*; D009479:Neuropeptides / Q000378:metabolism; D012794:Sialic Acids / Q000378:metabolism*; D012799:Sialyltransferases / Q000235:genetics*; D013234:Stem Cells / Q000166:cytology / Q000378:metabolism
chemical_list: D019002:CD56 Antigen; D000089622:Doublecortin Domain Proteins; D008869:Microtubule-Associated Proteins; C501063:Ncam1 protein, mouse; D009479:Neuropeptides; D012794:Sialic Acids; C021319:polysialic acid; C046778:CMP-N-acetylneuraminate-poly-alpha-2,8-sialosyl sialyltransferase; D012799:Sialyltransferases; C525848:ST8SiaIV protein, mouse