Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestine
<p>Abstract</p> <p>Background</p> <p>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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2009-10-01
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| Series: | Lipids in Health and Disease |
| Online Access: | http://www.lipidworld.com/content/8/1/46 |
| _version_ | 1818063291102003200 |
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| author | Dhaliwal Satvinder S Pallebage-Gamarallage Menuka MS Takechi Ryusuke Galloway Susan Mamo John CL |
| author_facet | Dhaliwal Satvinder S Pallebage-Gamarallage Menuka MS Takechi Ryusuke Galloway Susan Mamo John CL |
| author_sort | Dhaliwal Satvinder S |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>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.</p> <p>Results</p> <p>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).</p> <p>Conclusion</p> <p>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.</p> |
| first_indexed | 2024-12-10T14:17:46Z |
| format | Article |
| id | doaj.art-59283be6a7d8475b89206b42d1ce220d |
| institution | Directory Open Access Journal |
| issn | 1476-511X |
| language | English |
| last_indexed | 2024-12-10T14:17:46Z |
| publishDate | 2009-10-01 |
| publisher | BMC |
| record_format | Article |
| series | Lipids in Health and Disease |
| spelling | doaj.art-59283be6a7d8475b89206b42d1ce220d2022-12-22T01:45:16ZengBMCLipids in Health and Disease1476-511X2009-10-01814610.1186/1476-511X-8-46Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestineDhaliwal Satvinder SPallebage-Gamarallage Menuka MSTakechi RyusukeGalloway SusanMamo John CL<p>Abstract</p> <p>Background</p> <p>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.</p> <p>Results</p> <p>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).</p> <p>Conclusion</p> <p>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.</p>http://www.lipidworld.com/content/8/1/46 |
| spellingShingle | Dhaliwal Satvinder S Pallebage-Gamarallage Menuka MS Takechi Ryusuke Galloway Susan Mamo John CL Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestine Lipids in Health and Disease |
| title | Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_full | Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_fullStr | Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_full_unstemmed | Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_short | Amyloid-β colocalizes with apolipoprotein B in absorptive cells of the small intestine |
| title_sort | amyloid β colocalizes with apolipoprotein b in absorptive cells of the small intestine |
| url | http://www.lipidworld.com/content/8/1/46 |
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