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The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains

Parkin, Edward and Hussain, I and Turner, A J and Hooper, N M (1997) The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains. Journal of Neurochemistry, 69 (5). pp. 2179-2188. ISSN 0022-3042

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Abstract

The amyloid precursor protein may be processed by several different pathways, one of which produces the amyloid beta-peptide betaA4 present in the amyloid plaques characteristic of Alzheimer's disease. A recent report suggested that axonal-amyloid precursor protein is present in a membrane fraction "with caveolae-like properties." In the present study we have isolated detergent-insoluble, caveolae-like membranes from both mouse cerebellum and the human neuroblastoma cell line SH-SY5Y. Detergent-insoluble membranes from mouse cerebellum retained nearly all of the glycosylphosphatidylinositol-anchored proteins--alkaline phosphatase, 5'-nucleotidase, and the F3 protein--while excluding the majority of the plasmalemmal marker protein alkaline phosphodiesterase I. Although the inositol trisphosphate receptor was highly enriched in this detergent-insoluble fraction, neither amyloid precursor protein nor clathrin immunoreactivity could be detected. Similar results were obtained with SH-SY5Y cells, where 5'-nucleotidase activity was enriched at least 30-fold in the detergent-insoluble membranes, but no amyloid precursor protein or clathrin immunoreactivity could be detected. Caveolin could not be detected in microsomal membranes from either mouse cerebellum or SH-SY5Y cells. These observations suggest that amyloid precursor protein is not normally present in detergent-insoluble, caveolae-like membrane microdomains.

Item Type: Article
Journal or Publication Title: Journal of Neurochemistry
Uncontrolled Keywords: Amyloid beta-Protein Precursor ; Animals ; Biological Markers ; Calcium Channels ; Caveolin 1 ; Caveolins ; Cell Membrane ; Cerebellum ; Detergents ; Glycosylphosphatidylinositols ; Humans ; Inositol 1,4,5-Trisphosphate Receptors ; Membrane Proteins ; Mice ; Mice, Inbred C3H ; Neuroblastoma ; Phosphatidylinositol Diacylglycerol-Lyase ; Polyethylene Glycols ; Receptors, Cytoplasmic and Nuclear ; Solubility ; Tumor Cells, Cultured ; Type C Phospholipases
Subjects: UNSPECIFIED
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 51855
Deposited By: ep_importer_pure
Deposited On: 07 Dec 2011 01:16
Refereed?: Yes
Published?: Published
Last Modified: 09 Apr 2014 22:55
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/51855

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