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Titolo:
Localization of 1-afadin at puncta adhaerentia-like junctions between the mossy fiber terminals and the dendritic trunks of pyramidal cells in the adult mouse hippocampus
Autore:
Nishioka, H; Mizoguchi, A; Nakanishi, H; Mandai, K; Takahashi, K; Kimura, K; Satoh-Moriya, A; Takai, Y;
Indirizzi:
Osaka Univ, Grad Sch Med, Fac Med, Dept Mol Biol & Biochem, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 Biochem, Suita, Osaka 5650871, Japan JCR Pharmaceut Co Ltd, Japan Sci & Technol Corp, ERATO, Takai Biotimer Project, Kobe, Hyogo 6512241, Japan JCR Pharmaceut Co Ltd Kobe Hyogo Japan 6512241 Kobe, Hyogo 6512241, Japan Kyoto Univ, Fac Med, Dept Anat & Neurobiol, Kyoto 6068501, Japan Kyoto Univ Kyoto Japan 6068501 pt Anat & Neurobiol, Kyoto 6068501, Japan
Titolo Testata:
JOURNAL OF COMPARATIVE NEUROLOGY
fascicolo: 2, volume: 424, anno: 2000,
pagine: 297 - 306
SICI:
0021-9967(20000821)424:2<297:LO1APA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLIOVIRUS RECEPTOR GENE; ADHESION MOLECULE; SYNAPTIC VESICLE; BINDING PROTEIN; HOMOLOG; AFADIN; EXPRESSION; CADHERINS; COMPLEX; CLONING;
Keywords:
synapse; cell-cell junction; F-actin-binding protein; PDZ domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Takai, Y Osaka Univ, Grad Sch Med, Fac Med, Dept Mol Biol & Biochem, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 Suita, Osaka 5650871, Japan
Citazione:
H. Nishioka et al., "Localization of 1-afadin at puncta adhaerentia-like junctions between the mossy fiber terminals and the dendritic trunks of pyramidal cells in the adult mouse hippocampus", J COMP NEUR, 424(2), 2000, pp. 297-306

Abstract

We have recently found a novel cell-cell adhesion system at cadherin-basedadherens junctions. This system consists of at least two components: nectin, an immunoglobulin-like cell adhesion molecule with Ca2+-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-afadinand 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 differentiallydistributed in the hippocampus and suggest that l-afadin localized at the puncta adhaerentia-like junctions in the mossy fiber terminals may regulatethe structural and functional organization of these complex synaptic structures. J. Comp. Neurol. 424:297-306, 2000. (C) 2000 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 11:07:15