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Titolo:
Protein 4.1 in forebrain postsynaptic density preparations - Enrichment of4.1 gene products and detection of 4.1R binding proteins
Autore:
Scott, C; Keating, L; Bellamy, M; Baines, AJ;
Indirizzi:
Univ Kent, Dept Biosci, Canterbury CT2 7NJ, Kent, England Univ Kent Canterbury Kent England CT2 7NJ nterbury CT2 7NJ, Kent, England
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 4, volume: 268, anno: 2001,
pagine: 1084 - 1094
SICI:
0014-2956(200102)268:4<1084:P4IFPD>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
MEMBRANE CYTOSKELETAL PROTEIN-4.1; BETA-II SPECTRIN; ERYTHROCYTE-MEMBRANE; RAT-BRAIN; ALPHA-INTERNEXIN; GLYCOPHORIN-C; NMDA RECEPTOR; KINASE-C; SKELETAL PROTEIN-4.1; DENDRITIC SPINES;
Keywords:
cytoskeleton; alpha-internexin; postsynaptic densities; protein 4.1; spectrin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Baines, AJ Univ Kent, Dept Biosci, Canterbury CT2 7NJ, Kent, England Univ Kent Canterbury Kent England CT2 7NJ 2 7NJ, Kent, England
Citazione:
C. Scott et al., "Protein 4.1 in forebrain postsynaptic density preparations - Enrichment of4.1 gene products and detection of 4.1R binding proteins", EUR J BIOCH, 268(4), 2001, pp. 1084-1094

Abstract

4.1 Proteins are a family of multifunctional cytoskeletal components (4.1R, 4.1G, 4.1N and 4.1B) derived from four related genes, each of which is expressed in the nervous system. Using subcellular fractionation, we have investigated the possibility that 4.1 proteins are components of forebrain postsynaptic densities, cellular compartments enriched in spectrin and actin, whose interaction is regulated by 4.1R. Antibodies to each of 4.1R, 4.1G, 4.1N and 4.1B recognize polypeptides in postsynaptic density preparations. Of these, an 80-kDa 4.1R polypeptide is enriched 11-fold in postsynaptic density preparations relative to brain homogenate. Polypeptides of 150 and 125kDa represent 4.1B; of these, only the 125 kDa species is enriched (threefold). Antibodies to 4.1N recognize polypeptides of approximate to 115, 100,90 and 65 kDa, each enriched in postsynaptic density preparations relativeto brain homogenate. Minor 225 and 200 kDa polypeptides are recognized selectively by specific anti-4.1G antibodies: the 200 kDa species is enriched 2.5-fold. These data indicate that specific isoforms of all four 4.1 proteins are components of postsynaptic densities. Blot overlay analyses indicatethat, in addition to spectrin and actin, postsynaptic density polypeptidesof 140. 115, 72 and 66 kDa are likely to be 4.1R-interactive. Of these, 72kDa and 66 kDa polypeptides were identified as neurofilament L, and alpha -internexin, respectively. A complex containing 80 kDa 4.1R, alpha -internexin and neurofilament L was immunoprecipitated with anti-4.1R antibodies from brain extract. We conclude that 4.1R interacts with the characteristic intermediate filament proteins of postsynaptic densities, and that the 4.1 proteins have the potential to mediate the interactions of diverse components of postsynaptic densities.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 19:48:21