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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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 |
work_keys_str_mv |
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