Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Distribution of a human brain carboxypeptidase B capable of cleaving beta-amyloid precursor protein (APP) in normal and Alzheimer's diseased brain
Autore:
Itoh, K; Matsumoto, A;
Indirizzi:
Kobe Univ, Sch Med, Dept Pathol, Chuo Ku, Kobe, Hyogo 6500017, Japan Kobe Univ Kobe Hyogo Japan 6500017 l, Chuo Ku, Kobe, Hyogo 6500017, Japan Kobe Univ, Sch Med, Dept Radiat Biophys & Genet, Chuo Ku, Kobe, Hyogo 6500017, Japan Kobe Univ Kobe Hyogo Japan 6500017 t, Chuo Ku, Kobe, Hyogo 6500017, Japan
Titolo Testata:
ACTA HISTOCHEMICA ET CYTOCHEMICA
fascicolo: 4, volume: 34, anno: 2001,
pagine: 275 - 283
SICI:
0044-5991(2001)34:4<275:DOAHBC>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
MISSENSE MUTATIONS; GENE; CLEAVAGE; A-BETA(1-42); CHOLESTEROL; DERIVATIVES; PEPTIDES;
Keywords:
Alzheimer's disease; carboxypeptidase B; beta-amyloid protein; beta-amyloid precursor protein; immunohistochemistry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Itoh, K Case Western Reserve Univ, Sch Med, Dept Neurosci, Rm 658,2109 Adelbert Rd, Cleveland, OH 44106 USA Case Western Reserve Univ Rm 658,2109 Adelbert Rd Cleveland OH USA 44106
Citazione:
K. Itoh e A. Matsumoto, "Distribution of a human brain carboxypeptidase B capable of cleaving beta-amyloid precursor protein (APP) in normal and Alzheimer's diseased brain", ACT HIST CY, 34(4), 2001, pp. 275-283

Abstract

The processing of P-amyloid precursor protein (APP) is considered criticalfor understanding the pathogenesis of Alzheimer's disease (AD). To elucidate the significance of APP processing enzyme, we studied immunohistochemically the distribution of APP-processing protease (human carboxypeptidase B: HBCPB) in the normal control brains and AD brains, using anti-C14 antibody which recognizes C-terminal 14 amino acids of HBCPB. In the control brains,intense and diffuse C14-immunoreactivity was observed in the cytoplasm of pyramidal neurons of the hippocampus. Moderate immunoreactivity was found in the cortical and subcortical neurons. In AD brains, C14-immunoreactivity was markedly decreased in the brain regions examined except for the brain stem and cerebellum. However, HBCPB was shown to be colocalized with beta -amyloid protein (A beta) in neuritic plaques. In addition, neuritic plaques included C14-immunoreactive microglia/macrophages. Our present studies indicate that the expression of a novel APP-processing protease is impaired in AD brains and may suggest the possible role of HBCPB in the pathogenesis ofAD.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 04:19:12