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Titolo:
MEMBRANE TOPOLOGY OF THE GLUR1 GLUTAMATE-RECEPTOR SUBUNIT - EPITOPE MAPPING BY SITE-DIRECTED ANTIPEPTIDE ANTIBODIES
Autore:
MOLNAR E; MCILHINNEY RAJ; BAUDE A; NUSSER Z; SOMOGYI P;
Indirizzi:
UNIV OXFORD,MRC,ANAT NEUROPHARMACOL UNIT,MANSFIELD RD OXFORD OX1 3TH ENGLAND
Titolo Testata:
Journal of neurochemistry
fascicolo: 2, volume: 63, anno: 1994,
pagine: 683 - 693
SICI:
0022-3042(1994)63:2<683:MTOTGG>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT PROTEIN-KINASE; CENTRAL-NERVOUS-SYSTEM; AMINO-ACID RECEPTORS; RAT DENTATE GYRUS; GRANULE CELLS; SUBCELLULAR-DISTRIBUTION; ACETYLCHOLINE-RECEPTOR; FUNCTIONAL EXPRESSION; MOLECULAR-CLONING; BINDING-SITES;
Keywords:
ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLE PROPIONATE; ANTIPEPTIDE ANTIBODIES; TOPOLOGY; HIPPOCAMPUS; DENTATEGYRUS; IMMUNOCYTOCHEMISTRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
59
Recensione:
Indirizzi per estratti:
Citazione:
E. Molnar et al., "MEMBRANE TOPOLOGY OF THE GLUR1 GLUTAMATE-RECEPTOR SUBUNIT - EPITOPE MAPPING BY SITE-DIRECTED ANTIPEPTIDE ANTIBODIES", Journal of neurochemistry, 63(2), 1994, pp. 683-693

Abstract

In order to define the membrane topology of the GluR1 glutamate receptor subunit, we have examined the location of epitopes. Antibodies were produced against peptides corresponding to putative extracellular and intracellular segments of the rat brain GluR1 glutamate receptor subunit. Immunocytochemistry at the electron microscopic level in the dentate gyrus of the hippocampal formation showed that epitopes for the antiserum to the N-terminal part of the subunit are located at the extracellular face of the plasma membrane, whereas the antigenic determinants for the antiserum to the C-terminal part are found at the intracellular face of the postsynaptic membrane. Furthermore, antibodies to the N-terminal residues 253-267 reacted similarly with both intact and permeabilized synaptosomes, whereas the binding of antibodies to the C-terminal residues 877-889 increased about 1.6-fold following permeabilization. Our data suggest that the N- and C-terminal regions are located on the opposite side of the membrane and, therefore, the GluR1 subunit probably has an odd number of membrane spanning segments. The antibody cross-reactivities in different species and their effect on ligand binding activity were also established.

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Documento generato il 25/09/20 alle ore 09:02:04