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Cell-type-specific processing of the amyloid precursor protein by Presenilin during Drosophila development.

Loewer, Alexander ; Soba, Peter ; Beyreuther, Konrad ; Paro, Renato ; Merdes, Gunter (2004)
Cell-type-specific processing of the amyloid precursor protein by Presenilin during Drosophila development.
In: EMBO reports, 5 (4)
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

The cleavage of proteins within their transmembrane domain by Presenilin (PS) has an important role in different signalling pathways and in Alzheimer's disease. Nevertheless, not much is known about the regulation of PS activity. It has been suggested that substrate recognition by the PS complex depends only on the size of the extracellular domain independent of the amino-acid sequence and that PS activity is constitutive in all cells that express the minimal components of the complex. We report here the development of an in vivo reporter system that allowed us to analyse the processing of human amyloid precursor protein (APP) and the Notch receptor tissue specifically during Drosophila development in the living organism. Using this system, we demonstrate differences between APP and Notch processing and show that PS-mediated cleavage of APP can be regulated in different cell types independent of the size of the extracellular domain.

Typ des Eintrags: Artikel
Erschienen: 2004
Autor(en): Loewer, Alexander ; Soba, Peter ; Beyreuther, Konrad ; Paro, Renato ; Merdes, Gunter
Art des Eintrags: Bibliographie
Titel: Cell-type-specific processing of the amyloid precursor protein by Presenilin during Drosophila development.
Sprache: Englisch
Publikationsjahr: 2004
Titel der Zeitschrift, Zeitung oder Schriftenreihe: EMBO reports
Jahrgang/Volume einer Zeitschrift: 5
(Heft-)Nummer: 4
Kurzbeschreibung (Abstract):

The cleavage of proteins within their transmembrane domain by Presenilin (PS) has an important role in different signalling pathways and in Alzheimer's disease. Nevertheless, not much is known about the regulation of PS activity. It has been suggested that substrate recognition by the PS complex depends only on the size of the extracellular domain independent of the amino-acid sequence and that PS activity is constitutive in all cells that express the minimal components of the complex. We report here the development of an in vivo reporter system that allowed us to analyse the processing of human amyloid precursor protein (APP) and the Notch receptor tissue specifically during Drosophila development in the living organism. Using this system, we demonstrate differences between APP and Notch processing and show that PS-mediated cleavage of APP can be regulated in different cell types independent of the size of the extracellular domain.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Systems Biology of the Stress Response
Hinterlegungsdatum: 02 Sep 2015 09:04
Letzte Änderung: 02 Sep 2015 09:04
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