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beta-amyloid or its precursor protein is found in epithelial cells of the small intestine and is stimulated by high-fat feeding.

Abstract

In Alzheimer's disease (AD), beta-amyloid (Abeta) is deposited in extracellular matrices, initiating an inflammatory response and compromising cellular integrity. Epidemiological evidence and studies in animal models provide strong evidence that high-saturated-fat and/or cholesterol-rich diets exacerbate cerebral amyloidosis, although the mechanisms for this are unclear. Abeta contains hydrophobic domains and is normally bound to lipid-associated chaperone proteins. In previous studies, we have put forward the notion that Abeta is a regulatory component of postprandial lipoproteins (i.e., chylomicrons) and that aberrations in kinetics may be a contributing risk factor for AD. To explore this further, in this study, we utilized an immunohistochemical approach to determine if Abeta or its precursor protein is expressed in epithelial cells of the small intestine -- the site of chylomicron biogenesis. Wild-type mice were fed a low-fat or a high-fat dietary regime and sacrificed, and their small intestines were isolated. We found that, in mice fed low-fat chow, substantial Abeta/precursor protein was found exclusively in absorptive epithelial cells of the small intestine. In contrast, no Abeta/precursor protein was found in epithelial cells when mice were fasted for 65 h. In addition, we found that a high-fat feeding regime strongly stimulates epithelial cell Abeta/precursor protein concentration. Our findings are consistent with the notion that Abeta may serve as a regulatory apolipoprotein of postprandial lipoproteins.

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  • Authors+Show Affiliations

    ,

    School of Biomedical Science, Curtin University of Technology, Perth, Western Australia 6102, Australia.

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    Source

    MeSH

    Amyloid beta-Peptides
    Amyloid beta-Protein Precursor
    Animals
    Cholesterol
    Dietary Fats
    Immunohistochemistry
    Intestinal Mucosa
    Intestine, Small
    Mice
    Mice, Inbred C57BL

    Pub Type(s)

    Journal Article

    Language

    eng

    PubMed ID

    16962759

    Citation

    Galloway, Susan, et al. "Beta-amyloid or Its Precursor Protein Is Found in Epithelial Cells of the Small Intestine and Is Stimulated By High-fat Feeding." The Journal of Nutritional Biochemistry, vol. 18, no. 4, 2007, pp. 279-84.
    Galloway S, Jian L, Johnsen R, et al. Beta-amyloid or its precursor protein is found in epithelial cells of the small intestine and is stimulated by high-fat feeding. J Nutr Biochem. 2007;18(4):279-84.
    Galloway, S., Jian, L., Johnsen, R., Chew, S., & Mamo, J. C. (2007). Beta-amyloid or its precursor protein is found in epithelial cells of the small intestine and is stimulated by high-fat feeding. The Journal of Nutritional Biochemistry, 18(4), pp. 279-84.
    Galloway S, et al. Beta-amyloid or Its Precursor Protein Is Found in Epithelial Cells of the Small Intestine and Is Stimulated By High-fat Feeding. J Nutr Biochem. 2007;18(4):279-84. PubMed PMID: 16962759.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - beta-amyloid or its precursor protein is found in epithelial cells of the small intestine and is stimulated by high-fat feeding. AU - Galloway,Susan, AU - Jian,Le, AU - Johnsen,Russell, AU - Chew,Stewart, AU - Mamo,John C L, Y1 - 2006/09/07/ PY - 2006/03/10/received PY - 2006/06/09/revised PY - 2006/07/05/accepted PY - 2006/9/12/pubmed PY - 2007/4/26/medline PY - 2006/9/12/entrez SP - 279 EP - 84 JF - The Journal of nutritional biochemistry JO - J. Nutr. Biochem. VL - 18 IS - 4 N2 - In Alzheimer's disease (AD), beta-amyloid (Abeta) is deposited in extracellular matrices, initiating an inflammatory response and compromising cellular integrity. Epidemiological evidence and studies in animal models provide strong evidence that high-saturated-fat and/or cholesterol-rich diets exacerbate cerebral amyloidosis, although the mechanisms for this are unclear. Abeta contains hydrophobic domains and is normally bound to lipid-associated chaperone proteins. In previous studies, we have put forward the notion that Abeta is a regulatory component of postprandial lipoproteins (i.e., chylomicrons) and that aberrations in kinetics may be a contributing risk factor for AD. To explore this further, in this study, we utilized an immunohistochemical approach to determine if Abeta or its precursor protein is expressed in epithelial cells of the small intestine -- the site of chylomicron biogenesis. Wild-type mice were fed a low-fat or a high-fat dietary regime and sacrificed, and their small intestines were isolated. We found that, in mice fed low-fat chow, substantial Abeta/precursor protein was found exclusively in absorptive epithelial cells of the small intestine. In contrast, no Abeta/precursor protein was found in epithelial cells when mice were fasted for 65 h. In addition, we found that a high-fat feeding regime strongly stimulates epithelial cell Abeta/precursor protein concentration. Our findings are consistent with the notion that Abeta may serve as a regulatory apolipoprotein of postprandial lipoproteins. SN - 0955-2863 UR - https://www.unboundmedicine.com/medline/citation/16962759/beta_amyloid_or_its_precursor_protein_is_found_in_epithelial_cells_of_the_small_intestine_and_is_stimulated_by_high_fat_feeding_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0955-2863(06)00158-6 DB - PRIME DP - Unbound Medicine ER -