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Titolo:
Physiological roles of axonal ankyrins in survival of premyelinated axons and localization of voltage-gated sodium channels
Autore:
Bennett, V; Lambert, S;
Indirizzi:
Duke Univ, Med Ctr, Howard Hughes Med Inst, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 oward Hughes Med Inst, Durham, NC 27710 USA Duke Univ, Med Ctr, Dept Cell Biol, Durham, NC 27710 USA Duke Univ DurhamNC USA 27710 d Ctr, Dept Cell Biol, Durham, NC 27710 USA Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 Med Ctr, Dept Biochem, Durham, NC 27710 USA Univ Massachusetts, Sch Med, Dept Cell Biol, Worcester, MA 01545 USA Univ Massachusetts Worcester MA USA 01545 l Biol, Worcester, MA 01545 USA Univ Massachusetts, Sch Med, Neurosci Program, Worcester, MA 01545 USA Univ Massachusetts Worcester MA USA 01545 rogram, Worcester, MA 01545 USA
Titolo Testata:
JOURNAL OF NEUROCYTOLOGY
fascicolo: 4-5, volume: 28, anno: 1999,
pagine: 303 - 318
SICI:
0300-4864(199904)28:4-5<303:PROAAI>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ADHESION MOLECULES; T-LYMPHOMA CELLS; HUMAN ERYTHROCYTE ANKYRIN; X-LINKED HYDROCEPHALUS; INTERNAL CA2+ RELEASE; NERVOUS-SYSTEM; L1 FAMILY; IMMUNOGLOBULIN SUPERFAMILY; TRANSMEMBRANE GLYCOPROTEIN; STRUCTURAL REQUIREMENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
94
Recensione:
Indirizzi per estratti:
Indirizzo: Bennett, V Duke Univ, Med Ctr, Howard Hughes Med Inst, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 s Med Inst, Durham, NC 27710 USA
Citazione:
V. Bennett e S. Lambert, "Physiological roles of axonal ankyrins in survival of premyelinated axons and localization of voltage-gated sodium channels", J NEUROCYT, 28(4-5), 1999, pp. 303-318

Abstract

440 kD ankyrin-B and 480/270 kD ankyrin-G are membrane skeletal proteins with closely related biochemical properties yet distinctive physiological roles in axons. These proteins associate with spectrin-actin networks and also bind to integral membrane proteins including the L1 CAM family of cell adhesion molecules and voltage-gated sodium channels. 440 kD ankyrin-B is expressed with L1 in premyelinated axon tracts, and is essential for survival of these axons, at least in the case of the optic nerve. 440 ankyrin-B may collaborate with L1 in transcellular structures that mediate axon fasciculation and mechanically stabilize axon bundles, although these proteins may also be involved in axon pathfinding. Ankyrin-B (-/-) mice exhibit loss of L1 from premyelinated axon tracts and a similar, although much more severe, phenotype to L1 (-/-) mice and humans with L1 mutations. Ankyrin-B and L1 thus are candidates to collaborate in the same structural pathway and defects in this pathway can lead to nervous system malformations and mental retardation. 480/270 kD ankyrin-G are highly concentrated along with the L1CAM family members neurofascin and NrCAM at nodes of Ranvier and axon initial segments. Voltage-gated sodium channels bind directly to ankyrins, and are likely to associate in a ternary complex containing neurofascin/NrCAM, and ankyrin-G. Mice with ankyrin-G expression abolished in the cerebellum exhibitloss of ability of Purkinje neurons to fire action potentials, as well as loss of restriction of neurofascin/NrCAM to axon initial segments. Ankyrin-G thus is a key component in assembly of functional components of the axon initial segment and possibly the node of Ranvier.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 09:48:28