Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases
Autore:
Shirotani, K; Tsubuki, S; Iwata, N; Takaki, Y; Harigaya, W; Maruyama, K; Kiryu-Seo, S; Kiyama, H; Iwata, H; Tomita, T; Iwatsubo, T; Saido, TC;
Indirizzi:
RIKEN, Brain Sci Inst, Lab Proteolyt Neurosci, Wako, Saitama 3510198, Japan RIKEN Wako Saitama Japan 3510198 t Neurosci, Wako, Saitama 3510198, Japan Univ Tokyo, Grad Sch Pharmaceut Sci, Dept Neuropathol & Neurosci, Tokyo 1130033, Japan Univ Tokyo Tokyo Japan 1130033 ropathol & Neurosci, Tokyo 1130033, Japan Saitama Med Sch, Dept Pharmacol, Moroyama, Saitama 3500495, Japan Saitama Med Sch Moroyama Saitama Japan 3500495 ma, Saitama 3500495, Japan Asahikawa Med Coll, Dept Anat, Asahikawa, Hokkaido 0788510, Japan Asahikawa Med Coll Asahikawa Hokkaido Japan 0788510 kkaido 0788510, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 24, volume: 276, anno: 2001,
pagine: 21895 - 21901
SICI:
0021-9258(20010615)276:24<21895:NDBABP>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOTHELIN-CONVERTING ENZYME; BLOOD-GROUP PROTEIN; NEUTRAL ENDOPEPTIDASE; EXTRACELLULAR LEVELS; MOLECULAR-CLONING; ALZHEIMER-DISEASE; CATHEPSIN-D; RAT-BRAIN; DEGRADATION; METALLOPROTEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Shirotani, K RIKEN, Brain Sci Inst, Lab Proteolyt Neurosci, 2-1 Hirosawa, Wako, Saitama3510198, Japan RIKEN 2-1 Hirosawa Wako Saitama Japan 3510198 a3510198, Japan
Citazione:
K. Shirotani et al., "Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases", J BIOL CHEM, 276(24), 2001, pp. 21895-21901

Abstract

To identify the amyloid beta peptide (A beta) 1-42-degrading enzyme whose activity is inhibited by thiorphan and phosphoramidon in vivo, we searched for neprilysin (NEP) homologues and cloned neprilysin-like peptidase (NEPLP) alpha, NEPLP beta, and NEPLP gamma cDNAs. We expressed NEP, phosphate-regulating gene with homologies to endopeptidases on the X chromosome (PEX), NEPLPs, and damage-induced neuronal endopeptidase (DINE) in 293 cells as 95-to 125-kDa proteins and found that the enzymatic activities of PEX, NEPLP alpha, and NEPLP beta, as well as those of NEP and DINE, were sensitive to thiorphan and phosphoramidon. Among the peptidases tested, NEP degraded both synthetic and cell-secreted A beta1-40 and A beta1-42 most rapidly and efficiently. PEX degraded cold A beta1-40 and NEPLP alpha degraded both cold A beta1-40 and A beta1-42, although the rates and the extents of the digestion were slower and less efficient than those exhibited by NEP, These data suggest that, among the endopeptidases whose activities are sensitive to thiorphan and phosphoramidon, NEP is the most potent A beta -degrading enzymein vivo. Therefore, manipulating the activity of NEP would be a useful approach in regulating A beta levels in the brain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 23:30:47