Schmitz, Gerd and Grandl, Margot (2009) The Molecular Mechanisms of HDL and Associated Vesicular Trafficking Mechanisms to Mediate Cellular Lipid Homeostasis. ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, 29 (11). pp. 1718-1722. ISSN 1079-5642, 1524-4636
Full text not available from this repository. (Request a copy)Abstract
HDL functions mainly as a cholesterol scavenger, facilitating transport of cholesterol to the liver for conversion to bile acids and secretion into the bile for elimination or recycling in the enterohepatic bile acid cycle. Because of its major function in cholesterol clearance, HDL is in general considered to be atheroprotective. From cell cholesterol can be removed by efflux especially to apoA-I and HDL as extracellular acceptors which transport the cholesterol to the liver for excretion. This process is called reverse cholesterol transport. In this context the ATP binding cassette transporter protein ABCA1 facilitates cellular cholesterol and phospholipid release to apoA-I-containing HDL precursors. In addition ABCA1 plays a role in vesicular lipid transport mechanisms required for HDL particle formation. In general to maintain intracellular lipid homeostasis, sterols and associated lipids move between cellular compartments by vesicular and nonvesicular pathways. However, cholesterol sorting on vesicle formation is poorly understood. This review summarizes the current knowledge of the molecular mechanisms of HDL and associated vesicular trafficking mechanisms to mediate cellular lipid homeostasis. (Arterioscler Thromb Vasc Biol. 2009; 29: 1718-1722.)
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | APOLIPOPROTEIN-A-I; NONVESICULAR STEROL TRANSPORT; RAB PROTEINS; CHOLESTEROL; CELLS; EFFLUX; GOLGI; ABCA1; ATHEROSCLEROSIS; METABOLISM; HDL; lipid efflux; vesicular trafficking |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Klinische Chemie und Laboratoriumsmedizin |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 Sep 2020 07:18 |
| Last Modified: | 02 Sep 2020 07:18 |
| URI: | https://pred.uni-regensburg.de/id/eprint/28166 |
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