title: [Morphology and development of neural transplants of AMOG-deficient mice].
abstract: The adhesion molecule on glia (AMOG) has been reported to function as cell adhesion molecule and also to constitute the beta 2-subunit of the murine Na,K-ATPase. In order to elucidate these functions in vivo, Magyar et al. have generated mice carrying a targeted deletion of the AMOG gene. These mice exhibit behaviourally normal development till postnatal day P16. At this time, they develop muscular weakness, incoordination, and tremor. Death invariably occurs 24-36 hours after onset of the symptoms. Histological and ultrastructural examination of brain sections show enlarged ventricles, brain edema, and swelling of astrocyte end feet. However, no disturbances of the architecture or cell migration in the brain can be detected. In order to identify long-term consequences of AMOG deficiency which might not yet be detectable at the time of death, we have established a CNS grafting model. The embryonal brain anlage (E10.5-E13.5) was grafted into the caudoputamen of wild type mice. The graft recipients are sacrificed up to 7 months after the procedure. Both wild type and AMOG deficient grafts develop and form solid neural tissue with neurons, myelinated axons, glial cells, and ventricular structures, as shown by histological and immunocytochemical analysis. However, no differences in grafts derived from wild type, heterozygous, and AMOG-deficient donors can be detected. Proliferation has been examined by BrdU immunocytochemistry. The blood-brain barrier as examined by repeated magnetic resonance imaging after injection of Gadolinium-DTPA has been shown to be largely reconstituted five weeks after grafting.
authors.affiliation: Institut für Neuropathologie, Departement Pathologie, Zürich, Schweiz.
authors.forename: S
authors.initials: S
authors.lastname: Isenmann
authors.forename: S
authors.initials: S
authors.lastname: Brandner
authors.forename: U
authors.initials: U
authors.lastname: Sure
authors.forename: J P
authors.initials: JP
authors.lastname: Magyar
authors.forename: M
authors.initials: M
authors.lastname: Schachner
authors.forename: A
authors.initials: A
authors.lastname: Aguzzi
mesh_terms: D000251:Adenosine Triphosphatases; D000375:Aging; D000818:Animals; D001253:Astrocytes / Q000473:pathology; D001921:Brain / Q000254:growth & development / Q000473:pathology*; D001929:Brain Edema / Q000235:genetics / Q000473:pathology; D016380:Brain Tissue Transplantation / Q000473:pathology* / Q000502:physiology*; D027682:Cation Transport Proteins; D015816:Cell Adhesion Molecules, Neuronal / Q000235:genetics* / Q000378:metabolism; D002455:Cell Division; D016326:Extracellular Matrix Proteins / Q000235:genetics* / Q000378:metabolism; D016332:Fetal Tissue Transplantation / Q000473:pathology / Q000502:physiology; D005904:Glial Fibrillary Acidic Protein / Q000032:analysis; D007150:Immunohistochemistry; D051379:Mice; D008818:Mice, Neurologic Mutants; D009419:Nerve Tissue Proteins / Q000172:deficiency*; D009457:Neuroglia / Q000166:cytology / Q000473:pathology / Q000502:physiology; D009474:Neurons / Q000166:cytology / Q000473:pathology / Q000502:physiology*; D017384:Sequence Deletion; D000254:Sodium-Potassium-Exchanging ATPase / Q000096:biosynthesis; D016708:Synaptophysin / Q000032:analysis
chemical_list: C504191:Atp1b2 protein, mouse; D027682:Cation Transport Proteins; D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D005904:Glial Fibrillary Acidic Protein; D009419:Nerve Tissue Proteins; D016708:Synaptophysin; D000251:Adenosine Triphosphatases; D000254:Sodium-Potassium-Exchanging ATPase