Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Identification of the amino acids on a neuronal glutamate receptor recognized by an autoantibody from a patient with paraneoplastic syndrome
Autore:
Carlson, NG; Gahring, LC; Rogers, SW;
Indirizzi:
Univ Utah, Med Ctr, EIHG, HMBG, Salt Lake City, UT 84112 USA Univ Utah Salt Lake City UT USA 84112 HMBG, Salt Lake City, UT 84112 USA Salt Lake City VA, Ctr Geriatr Res Educ & Clin, Salt Lake City, UT USA Salt Lake City VA Salt Lake City UT USA c & Clin, Salt Lake City, UT USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE RESEARCH
fascicolo: 6, volume: 63, anno: 2001,
pagine: 480 - 485
SICI:
0360-4012(20010315)63:6<480:IOTAAO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
EATON MYASTHENIC SYNDROME; RASMUSSENS-ENCEPHALITIS; CALCIUM CHANNELS; ANTIBODY-BINDING; AUTOIMMUNITY; ACTIVATION; DEGENERATION; INHIBITION; EXTENSIONS; DISORDERS;
Keywords:
glutamate; receptor; autoantibody; neurodegeneration; epitope;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Rogers, SW Univ Utah, Med Ctr, EIHG, HMBG, Rm 2410,15 N 2030 E, Salt Lake City, UT 84112 USA Univ Utah Rm 2410,15 N 2030 E Salt Lake City UT USA 84112 2 USA
Citazione:
N.G. Carlson et al., "Identification of the amino acids on a neuronal glutamate receptor recognized by an autoantibody from a patient with paraneoplastic syndrome", J NEUROSC R, 63(6), 2001, pp. 480-485

Abstract

Autoantibodies from a patient with paraneoplastic disease were identified previously to bind to the glutamate receptor (GluR) subunit GluR5 and to function as potential allosteric modulators of receptor activity (Gahring et al, [1995] Mol Med 1:245-253). In the present study we have used deletion mapping and mutagenesis to define the residues in GluR5 bound by this autoreactivity. The autoantibody contact residues include residues K497, N508, K510, E512, and to a lesser extent Q507, Residues 507-512 confer autoantibodyspecificity of the autoreactivity to GluR5. These residues have been shownin crystallographic studies (Armstrong et al, [1998] Nature 395: 913-917) to participate in a loop structure, whereas residue K497 is located on a beta-strand. Notably, this binding spans tyrosine 504, a residue important informing the agonist-binding site. We propose that autoantibody binding of essential residues in this GluR5 autoantigenic region defines a subunit-specific allosteric regulatory site on neuronal glutamate receptors and suggests how receptor dysfunction and region-specific neuronal death in the braincan progress in certain autoimmune neurological diseases. J, Neurosci. Res. 63. 480-485, 2001. (C) 2001 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 18:01:15