Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathway

The processing of the amyloid precursor protein (APP) by the secretase family of protease enzymes can be influenced by a variety of diverse factors, including elements of the immune response. In this study, we have investigated the effect of the pro-inflammatory lipopolysaccharide (LPS) on APP proce...

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Main Authors: Claire I. Small, Geoffrey A. Lyles, Kieran C. Breen
Format: Article
Language:English
Published: Elsevier 2005-08-01
Series:Neurobiology of Disease
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S0969996105000318
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spelling doaj-7e45e76e46f0476494413c091117b79c2021-03-20T04:50:56ZengElsevierNeurobiology of Disease1095-953X2005-08-01193400406Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathwayClaire I. Small0Geoffrey A. Lyles1Kieran C. Breen2Alzheimer's Disease Research Centre, Division of Pathology and Neurosciences, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UKAlzheimer's Disease Research Centre, Division of Pathology and Neurosciences, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UKAlzheimer's Disease Research Centre, Division of Pathology and Neurosciences, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UK; CEA-CNRS URA 2210, Service Hospitalier Frédéric Joliot, 4, Place du Général Leclerc, 91406 Orsay, France; Corresponding author. Alzheimer's Disease Research Centre, Division of Pathology and Neurosciences, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UK. Fax: +44 1382 633 923.The processing of the amyloid precursor protein (APP) by the secretase family of protease enzymes can be influenced by a variety of diverse factors, including elements of the immune response. In this study, we have investigated the effect of the pro-inflammatory lipopolysaccharide (LPS) on APP processing in rat glial cell cultures derived from both cortex and cerebellum. LPS activation of the cells, as monitored by the induction of the pro-inflammatory nitric oxide synthase (iNOS) enzyme, elicited no change in the overall cellular expression levels of APP, although there was a marked concentration-related increase in the secretion of the soluble APPs following both short- (4 h) and long-term (18 h) drug treatment times. The stimulation of APPs secretion was blocked by the protein kinase C (PKC) inhibitor GF109203x, suggesting that LPS may act via a PKC-mediated pathway to increase APPs secretion.http://www.sciencedirect.com/science/article/pii/S0969996105000318AlzheimerAmyloidLipopolysaccharideGliaProtein kinase C
collection DOAJ
language English
format Article
sources DOAJ
author Claire I. Small
Geoffrey A. Lyles
Kieran C. Breen
spellingShingle Claire I. Small
Geoffrey A. Lyles
Kieran C. Breen
Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathway
Neurobiology of Disease
Alzheimer
Amyloid
Lipopolysaccharide
Glia
Protein kinase C
author_facet Claire I. Small
Geoffrey A. Lyles
Kieran C. Breen
author_sort Claire I. Small
title Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathway
title_short Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathway
title_full Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathway
title_fullStr Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathway
title_full_unstemmed Lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase C-mediated pathway
title_sort lipopolysaccharide stimulates the secretion of the amyloid precursor protein via a protein kinase c-mediated pathway
publisher Elsevier
series Neurobiology of Disease
issn 1095-953X
publishDate 2005-08-01
description The processing of the amyloid precursor protein (APP) by the secretase family of protease enzymes can be influenced by a variety of diverse factors, including elements of the immune response. In this study, we have investigated the effect of the pro-inflammatory lipopolysaccharide (LPS) on APP processing in rat glial cell cultures derived from both cortex and cerebellum. LPS activation of the cells, as monitored by the induction of the pro-inflammatory nitric oxide synthase (iNOS) enzyme, elicited no change in the overall cellular expression levels of APP, although there was a marked concentration-related increase in the secretion of the soluble APPs following both short- (4 h) and long-term (18 h) drug treatment times. The stimulation of APPs secretion was blocked by the protein kinase C (PKC) inhibitor GF109203x, suggesting that LPS may act via a PKC-mediated pathway to increase APPs secretion.
topic Alzheimer
Amyloid
Lipopolysaccharide
Glia
Protein kinase C
url http://www.sciencedirect.com/science/article/pii/S0969996105000318
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AT kierancbreen lipopolysaccharidestimulatesthesecretionoftheamyloidprecursorproteinviaaproteinkinasecmediatedpathway
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