Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PHOSPHORYLATION OF NATIVE AND TRUNCATED ISOFORMS OF PROTEIN-TAU BY THE DOUBLE-STRANDED DNA-DEPENDENT PROTEIN-KINASE (DNA-PK) SHOWS THAT THEPRIMARY PHOSPHORYLATION SITES ARE LOCALIZED BETWEEN AMINO-ACID-RESIDUES-212-231 OF THE LONGEST-TAU
Autore:
WU JM; CHEN YP; HSIEH TC; BRANDT R; LEE G;
Indirizzi:
NEW YORK MED COLL,DEPT BIOCHEM & MOL BIOL VALHALLA NY 10595 HARVARD UNIV,SCH MED,CTR NEUROL DIS BOSTON MA 02115
Titolo Testata:
Biochemistry and molecular biology international
fascicolo: 1, volume: 40, anno: 1996,
pagine: 21 - 31
SICI:
1039-9712(1996)40:1<21:PONATI>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; NUCLEAR-TAU; SER(262); BRAIN; STATE; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Wu et al., "PHOSPHORYLATION OF NATIVE AND TRUNCATED ISOFORMS OF PROTEIN-TAU BY THE DOUBLE-STRANDED DNA-DEPENDENT PROTEIN-KINASE (DNA-PK) SHOWS THAT THEPRIMARY PHOSPHORYLATION SITES ARE LOCALIZED BETWEEN AMINO-ACID-RESIDUES-212-231 OF THE LONGEST-TAU", Biochemistry and molecular biology international, 40(1), 1996, pp. 21-31

Abstract

Alzheimer's disease (AD) is pathologically characterized by the appearance of neurofibrillary tangles (NFT), senile plaques, and loss of subpopulation of neuronal cells. The NFT is composed of paired helical filaments (PHT) with extensively modified protein tau as its primary constituent. Previously we had reported on the hyperphosphorylation of tau by a double-stranded-DNA-stimutated protein kinase (DNA-PK). In this communication, we have compared the DNA-PK mediated phosphorylation of native and truncated tau s with that catalyzed by the cAMP-dependent protein kinase (PKA). In addition, we have attempted to map the primary site(s) of phosphorylation of tau by DNA-PK. Our results suggest that DNA-PK phosphorylates tau at sites substantially different from those targeted by PKA. Furthermore, we show that the primary phosphorylation sites lie between amino acid residues 212-231 (using numbering system for the longest tau, which is the isoform with four ''repeats'' and a 58 amino acid ''insert'' at the carboxyl- and amino-termini, respectively, of the protein molecule).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 18:44:00