Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine
Background: Amyloid-β is recognized as the major constituent of senile plaque found in subjects with Alzheimer's disease. However, there is increasing evidence that in a physiological context amyloid-β may serve as regulating apolipoprotein, primarily of the triglyceride enriched lipoproteins....
| Main Authors: | , , , |
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| Format: | Journal Article |
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Biomed Central
2009
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| Online Access: | http://hdl.handle.net/20.500.11937/42899 |
| _version_ | 1848756543935217664 |
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| author | Galloway, Susan Takechi, Ryu Galloway, Susan Dhaliwal, Satvinder Mamo, John |
| author_facet | Galloway, Susan Takechi, Ryu Galloway, Susan Dhaliwal, Satvinder Mamo, John |
| author_sort | Galloway, Susan |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Background: Amyloid-β is recognized as the major constituent of senile plaque found in subjects with Alzheimer's disease. However, there is increasing evidence that in a physiological context amyloid-β may serve as regulating apolipoprotein, primarily of the triglyceride enriched lipoproteins. To consider this hypothesis further, this study utilized an in vivo immunological approach to explore in lipogenic tissue whether amyloid-β colocalizes with nascent triglyceride-rich lipoproteins. Results: In murine absorptive epithelial cells of the small intestine, amyloid-β had remarkable colocalization with chylomicrons (Manders overlap coefficient = 0.73 ± 0.03 (SEM)), the latter identified as immunoreactive apolipoprotein B. A diet enriched in saturated fats doubled the abundance of both amyloid-β and apo B and increased the overlap coefficient of the two proteins (0.87 ± 0.02). However, there was no evidence that abundance of the two proteins was interdependent within the enterocytes (Pearson's Coefficient < 0.02 ± 0.03), or in plasma (Pearson's Coefficient < 0.01). Conclusion: The findings of this study are consistent with the possibility that amyloid-β is secreted by enterocytes as an apolipoprotein component of chylomicrons. However, secretion of amyloid-β appears to be independent of chylomicron biogenesis. |
| first_indexed | 2025-11-14T09:13:53Z |
| format | Journal Article |
| id | curtin-20.500.11937-42899 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T09:13:53Z |
| publishDate | 2009 |
| publisher | Biomed Central |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-428992017-09-13T15:15:02Z Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine Galloway, Susan Takechi, Ryu Galloway, Susan Dhaliwal, Satvinder Mamo, John Background: Amyloid-β is recognized as the major constituent of senile plaque found in subjects with Alzheimer's disease. However, there is increasing evidence that in a physiological context amyloid-β may serve as regulating apolipoprotein, primarily of the triglyceride enriched lipoproteins. To consider this hypothesis further, this study utilized an in vivo immunological approach to explore in lipogenic tissue whether amyloid-β colocalizes with nascent triglyceride-rich lipoproteins. Results: In murine absorptive epithelial cells of the small intestine, amyloid-β had remarkable colocalization with chylomicrons (Manders overlap coefficient = 0.73 ± 0.03 (SEM)), the latter identified as immunoreactive apolipoprotein B. A diet enriched in saturated fats doubled the abundance of both amyloid-β and apo B and increased the overlap coefficient of the two proteins (0.87 ± 0.02). However, there was no evidence that abundance of the two proteins was interdependent within the enterocytes (Pearson's Coefficient < 0.02 ± 0.03), or in plasma (Pearson's Coefficient < 0.01). Conclusion: The findings of this study are consistent with the possibility that amyloid-β is secreted by enterocytes as an apolipoprotein component of chylomicrons. However, secretion of amyloid-β appears to be independent of chylomicron biogenesis. 2009 Journal Article http://hdl.handle.net/20.500.11937/42899 10.1186/1476-511X-8-46 Biomed Central fulltext |
| spellingShingle | Galloway, Susan Takechi, Ryu Galloway, Susan Dhaliwal, Satvinder Mamo, John Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title | Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_full | Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_fullStr | Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_full_unstemmed | Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_short | Amyloid-beta colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_sort | amyloid-beta colocalizes with apolipoprotein b in absorptive cells of the small intestine |
| url | http://hdl.handle.net/20.500.11937/42899 |