DOI | Resolve DOI: https://doi.org/10.7555/JBR.28.20130184 |
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Author | Search for: Bamji-Mirza, Michelle1; Search for: Zhang, Wandong1; Search for: Yao, Zemin |
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Name affiliation | - National Research Council of Canada. Human Health Therapeutics
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Format | Text, Article |
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Journal title | Journal of Biomedical Research |
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ISSN | 1674-8301 |
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Volume | 28 |
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Issue | 3 |
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Pages | 201–212 |
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Subject | apolipoprotein A1; apolipoprotein E; liver triacylglycerol lipase; Adenoviridae; animal cell; cell fractionation; cell surface; cellular distribution; endoplasmic reticulum; female; gene transfer; genetic transfection; HepG2 cell line; human cell; immunoblotting; liver cell; microsome; mouse; null cell; protein expression; protein secretion; secretory pathway |
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Abstract | This study aimed to examine whether expression of human hepatic lipase (hHL) exerted an intracellular effect on hepatic production of apolipoprotein (apo) A-I. The levels of secreted and cell-associated apoA-I were contrasted between primary hepatocytes isolated from Lipc-null and C57BL/6 mice, and between Lipc-null hepatocytes transfected with either hHL-encoding or control adenovirus. An HSPG-binding deficient hHL protein (hHLmt) was used to determine the impact of cell surface binding on HL action. Accumulation of apoA-I in conditioned media of primary hepatocytes isolated from Lipc-null mice was increased as compared to that from C57BL/6 mice. Metabolic labeling experiments showed that secretion of 35S-apoA-I from Lipc-null cells was significantly higher than that from C57BL/6 cells. Expression of hHL in Lipc-null hepatocytes, through adenovirus-mediated gene transfer, resulted in decreased synthesis and secretion of 35S-apoA-I, but not 35S-apoE, as compared with cells transfected with control adenovirus. Expression of HSPG-binding deficient hHLmt in Lipc-null cells also exerted an inhibitory effect on apoA-I production, even though hHLmt displayed impaired exit from the endoplasmic reticulum as compared with hHL. Subcellular fractionation revealed that expression of hHL or hHLmt led to increased microsome-association of apoA-I relative to non-transfected control. Expression of hHL negatively impacts hepatic production of apoA-I. |
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Publication date | 2014-05 |
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Publisher | National Center for Biotechnology Information |
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Language | English |
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Peer reviewed | Yes |
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NPARC number | 21275578 |
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Export citation | Export as RIS |
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Report a correction | Report a correction |
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Record identifier | 5fefec5e-02ab-497e-b210-5711e1e32667 | Record created | 2015-07-14 |
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Record modified | 2020-04-22 |
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