Abstract
We have recently found a novel cell-cell adhesion system at cadherin-based adherens junctions. This system consists of at least two components: nectin, an immunoglobulin-like cell adhesion molecule with Ca(2+)-independent homophilic binding activity, and l-afadin, an actin filament-binding protein that connects nectin to the actin cytoskeleton. In the present study, we investigated immunocytochemically the localization of l-afadin in the mouse hippocampus. At the light microscopic level, l-afadin immunoreactivity was demonstrated as flattened disks in the stratum lucidum of the CA3 area. By immunoelectron microscopy, signals for l-afadin were highly concentrated in a symmetrical manner at the puncta adhaerentia-like junctions between the mossy fiber terminals and the dendritic trunks of pyramidal cells. We furthermore immunostained the hippocampus with antibodies recognizing both l-afadin and s-afadin, a small splicing variant of l-afadin that is identical to AF-6. Immunoreactivity for l- and s-afadins was demonstrated not only as the flattened disks similar to that for l-afadin, but also as numerous fine dots widely distributed in all synaptic layers of the CA1 and CA3 areas. The latter finding may correspond with the recent report by Buchert et al. (1999, J. Cell. Biol. 144:361-371), who found that s-afadin (AF-6) and/or l-afadin was localized at the postsynaptic membranes of asymmetric synaptic junctions. Our present results indicate that l- and s-afadins are differentially distributed in the hippocampus and suggest that l-afadin localized at the puncta adhaerentia-like junctions in the mossy fiber terminals may regulate the structural and functional organization of these complex synaptic structures.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.