First Author | Bahjaoui-Bouhaddi M | Year | 1997 |
Journal | J Comp Neurol | Volume | 378 |
Issue | 2 | Pages | 180-95 |
PubMed ID | 9120059 | Mgi Jnum | J:38641 |
Mgi Id | MGI:86025 | Citation | Bahjaoui-Bouhaddi M, et al. (1997) Localized deposition of M-cadherin in the glomeruli of the granular layer during the postnatal development of mouse cerebellum. (Erratum 1997;382:139). J Comp Neurol 378(2):180-95 |
abstractText | M-cadherin is a Ca2+-dependent cell adhesion molecule of the cadherin family, initially localized at the areas of contact between myotubes during myogenesis, but also detected in the peripheral nerve and at the adult neuromuscular junction. In this study, searching for the expression of M-cadherin in the adult mouse brain, we observed a restricted expression of M-cadherin in one of the three layers of the cerebellar cortex: the granular layer. M-cadherin was accumulated in structures rich in synapses and other intercellular junctions where messy fibers connect granule cell dendrites, the glomeruli. This molecule was not expressed in the cerebellum during the first steps of postnatal cerebellar neurogenesis: granule cell proliferation and migration and Purkinje cell alignment. M-cadherin expression was first detected at postnatal day (P)11, after the establishment of the synaptic connections between messy fibers and granule cell dendrites. It then accumulated in glomeruli during their phase of maturation which is characterized by the formation of puncta adherentia between granule cell dendrites. M-cadherin was undetectable in the cerebella of the weaver and staggerer mutants, lacking granule cells, and therefore mature glomeruli and puncta adherentia. Furthermore, other components classically associated with intercellular junctions, i.e., alpha-caterin, beta-catenin and actin filaments, closely paralleled M-cadherin appearance and colocalized with M-cadherin in the mature glomeruli. M-cadherin, which appears as a molecular marker of glomerulus maturation, might be implicated in the formation, and be the ligand, of adherens junctions encountered in this structure. (C) 1997 Wiley-Liss, Inc. |