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Titolo:
Protein kinase C alpha and beta 1 isoforms are regulators of alpha-secretory proteolytic processing of amyloid precursor protein in vivo
Autore:
Rossner, S; Mendla, K; Schliebs, R; Bigl, V;
Indirizzi:
Paul Flechsig Inst Brain Res, Dept Neurochem, D-04109 Leipzig, Germany Paul Flechsig Inst Brain Res Leipzig Germany D-04109 09 Leipzig, Germany Boehringer Ingelheim KG, Dept Biol Res, D-55216 Ingelheim, Germany Boehringer Ingelheim KG Ingelheim Germany D-55216 216 Ingelheim, Germany
Titolo Testata:
EUROPEAN JOURNAL OF NEUROSCIENCE
fascicolo: 8, volume: 13, anno: 2001,
pagine: 1644 - 1648
SICI:
0953-816X(200104)13:8<1644:PKCAAB>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; CALPHOSTIN-C; RATS; METALLOPROTEASE; SEQUENCE; ISOZYMES; BINDING; BRAIN;
Keywords:
Alzheimer's disease; amyloid precursor protein processing; animal model; guinea pig; microencephalopathy; neocortex; protein kinase C isoforms; translocation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Rossner, S Paul Flechsig Inst Brain Res, Dept Neurochem, Jahnallee 59, D-04109 Leipzig, Germany Paul Flechsig Inst Brain Res Jahnallee 59 Leipzig Germany D-04109
Citazione:
S. Rossner et al., "Protein kinase C alpha and beta 1 isoforms are regulators of alpha-secretory proteolytic processing of amyloid precursor protein in vivo", EUR J NEURO, 13(8), 2001, pp. 1644-1648

Abstract

We have recently shown that in utero treatment of guinea pigs with the DNAmethylating substance methylazoxymethanol acetate (MAM) results in neocortical microencephalopathy, increased protein kinase C (PKC) activity and altered processing of the amyloid precursor protein (APP) in neocortex of offspring. Here we show that PKC alpha and PKC beta1 are the key regulators of alpha -secretory APP processing in guinea pig neocortex under these experimental conditions in vivo. This conclusion is based on the selective translocation of PKC alpha and PKC beta1 isoforms to the cell membrane in MAM-treated guinea pigs, as revealed by Western blot analysis and by immunocytochemistry. Additionally, we observed that [H-3]phorbol ester binding to proteinkinase C increased by 38% and enhanced basal PKC activity by 58% in the neocortex of microencephalic guinea pigs. Inhibition of PKC alpha /PKC beta1 by Go6976 abolished this difference, suggesting that constitutive overactivation of these PKC isoforms accounts for the increase in total PKC activity. We also observed a strong positive correlation between levels of alpha -secretase-processed APP and PKC activity in the neocortex of individual animals, providing further evidence for a significant role of classical PKC isoforms in nonamyloidogenic APP processing.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:23:55