The role of phospholipase D in amyloid b precursor protein processing. | [International Journal of Pharmacology • 2005]

Author(s):

1. Mark Mclaughlin: Applied Neurobiology Group, University of Glasgow Veterinary School, Glasgow G61 1QH, UK

2. Elena Del Rio: Department of Paychiatry, Alzheimer’s Disease Research Centre, University of Dundee Medical School, Ninewells Hospital, Dundee DD I 9SY, UK

3. Hazel Leith: Department of Paychiatry, Alzheimer’s Disease Research Centre, University of Dundee Medical School, Ninewells Hospital, Dundee DD I 9SY, UK

4. Kieran C. Breen: Department of Paychiatry, Alzheimer’s Disease Research Centre, University of Dundee Medical School, Ninewells Hospital, Dundee DD I 9SY, UK

Abstract:

The generation of a secreted N-terminal fragment of the amyloid precursor protein (AbPPs) can be stimulated by a variety of signaling pathways many of which are also known to modulate the activity of the phospholipase D (PLD) enzyme. This study used primary rat neuronal cerebellar granule (CG) cultures and SH-SY5Y human neuroblastoma cell lines to determine the potential role of PLD in the protein kinase C (PKC)-associated generation of AbPPs. Protein release was markedly enhanced by direct PKC stimulation following treatment of both cell type with either phorbol ester or indirectly by the muscarinic agonist carbachol and these effects were greatly attenuated by co-incubation with the PKC inhibitor GF109203X. A partial inhibition of PKC- and carbachol-stimulated AbPPs secretion was also achieved by pre-treatment of the cells with toxin B, a PLD inhibitor. This suggested that PLD may play a role downstream of PKC in the control of AbPPs secretion.

Page(s): 98-103

DOI: DOI not available

Published: Journal: International Journal of Pharmacology, Volume: 1, Issue: 1, Year: 2005

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