title: Selective disruption of "late onset" sagittal banding patterns by ectopic expression of engrailed-2 in cerebellar Purkinje cells.
abstract: To explore the role of Engrailed proteins in development of the cerebellum, Engrailed-2 (En-2) was ectopically expressed in cerebellar Purkinje cells from the late embryonic stage into adulthood. The fundamental organization of Purkinje cell sagittal zones as revealed by the "early onset" markers L7-beta-gal and cadherin-8 was found to be virtually identical to that in wild type. In contrast, "late onset" sagittal banding patterns revealed by Purkinje cell markers zebrin I, zebrin II, and 9-O-acetyl GD3 Ganglioside (P-Path), and the granule cell marker NADPH-diaphorase, were disrupted. In general, although some evidence of banding was still detectable, boundaries defined by the latter markers were poorly defined, and the patterns overall took on a diffuse appearance. In parallel with the changes in late onset markers, anterograde tracing of spinocerebellar axons revealed a general diffusion of the mossy fiber projection pattern in lobule VIII and the anterior lobe. These observations suggest that at least two separate mediolateral boundary systems exist in the cerebellum, and these are differentially affected by ectopic En-2 expression. Alternatively, one boundary system exists that remains primarily intact in the mutant, but recognition of this system by a set of late developmental events is perturbed.
authors.affiliation: Division of Neuroscience and the Neurobiotechnology Center, The Ohio State University College of Medicine, Columbus, Ohio 43210, USA.
authors.forename: S L
authors.initials: SL
authors.lastname: Baader
authors.forename: M W
authors.initials: MW
authors.lastname: Vogel
authors.forename: S
authors.initials: S
authors.lastname: Sanlioglu
authors.forename: X
authors.initials: X
authors.lastname: Zhang
authors.forename: J
authors.initials: J
authors.lastname: Oberdick
mesh_terms: D000818:Animals; D001369:Axons / Q000378:metabolism; D019521:Body Patterning; D015820:Cadherins / Q000032:analysis; D002478:Cells, Cultured; D002525:Cerebellar Cortex / Q000196:embryology / Q000254:growth & development*; D005732:Gangliosides / Q000032:analysis; D015870:Gene Expression; D018507:Gene Expression Regulation, Developmental; D020662:Guanine Nucleotide Exchange Factors; D018398:Homeodomain Proteins / Q000235:genetics / Q000502:physiology*; D051379:Mice; D008822:Mice, Transgenic; D019599:Mossy Fibers, Hippocampal / Q000378:metabolism; D009252:NADPH Dehydrogenase / Q000032:analysis; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology*; D009434:Neural Pathways / Q000378:metabolism; D009479:Neuropeptides / Q000235:genetics; D011401:Promoter Regions, Genetic / Q000235:genetics; D011689:Purkinje Cells / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000502:physiology; D000099266:Engrailed 2 Protein
chemical_list: D015820:Cadherins; D005732:Gangliosides; D020662:Guanine Nucleotide Exchange Factors; D018398:Homeodomain Proteins; D009252:NADPH Dehydrogenase; D009419:Nerve Tissue Proteins; D009479:Neuropeptides; D011993:Recombinant Fusion Proteins; D000099266:Engrailed 2 Protein; C504541:Cdh8 protein, mouse; C104971:Pcp2 protein, mouse; C049132:9-O-acetyl-GD3 ganglioside