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

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The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains. / Parkin, Edward; Hussain, I; Turner, A J et al.

In: Journal of Neurochemistry, Vol. 69, No. 5, 11.1997, p. 2179-2188.

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Parkin E, Hussain I, Turner AJ, Hooper NM. The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains. Journal of Neurochemistry. 1997 Nov;69(5):2179-2188. doi: 10.1046/j.1471-4159.1997.69052179.x

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Parkin, Edward ; Hussain, I ; Turner, A J et al. / The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains. In: Journal of Neurochemistry. 1997 ; Vol. 69, No. 5. pp. 2179-2188.

Bibtex

@article{ed6869377f09410a90dab1ac317c393a,
title = "The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains",
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.",
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",
author = "Edward Parkin and I Hussain and Turner, {A J} and Hooper, {N M}",
year = "1997",
month = nov,
doi = "10.1046/j.1471-4159.1997.69052179.x",
language = "English",
volume = "69",
pages = "2179--2188",
journal = "Journal of Neurochemistry",
issn = "0022-3042",
publisher = "Wiley-Blackwell",
number = "5",

}

RIS

TY - JOUR

T1 - The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains

AU - Parkin, Edward

AU - Hussain, I

AU - Turner, A J

AU - Hooper, N M

PY - 1997/11

Y1 - 1997/11

N2 - 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.

AB - 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.

KW - Amyloid beta-Protein Precursor

KW - Animals

KW - Biological Markers

KW - Calcium Channels

KW - Caveolin 1

KW - Caveolins

KW - Cell Membrane

KW - Cerebellum

KW - Detergents

KW - Glycosylphosphatidylinositols

KW - Humans

KW - Inositol 1,4,5-Trisphosphate Receptors

KW - Membrane Proteins

KW - Mice

KW - Mice, Inbred C3H

KW - Neuroblastoma

KW - Phosphatidylinositol Diacylglycerol-Lyase

KW - Polyethylene Glycols

KW - Receptors, Cytoplasmic and Nuclear

KW - Solubility

KW - Tumor Cells, Cultured

KW - Type C Phospholipases

U2 - 10.1046/j.1471-4159.1997.69052179.x

DO - 10.1046/j.1471-4159.1997.69052179.x

M3 - Journal article

C2 - 9349565

VL - 69

SP - 2179

EP - 2188

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

SN - 0022-3042

IS - 5

ER -